text:
VOL. 132 | NO. 207 | Wednesday, October 18, 2017
City Lays Out Numerous Options in Confederate Monuments Controversy
The city administration and Memphis City Council laid out numerous paths forward in the Confederate monuments controversy Tuesday, Oct. 17, that include closing Health Sciences Park entirely or building a memorial to lynching victims in the park plaza where a statue of Nathan Bedford Forrest is now the centerpiece.
The likeness of the Confederate General, slave trader and Ku Klux Klan Grand Wizard is at the center of the city's efforts that went to the Tennessee Historical Commission this month for a hearing.
That hearing prompted a denial by the commission to hear and act on the city's request to let the city remove Forrest's statue. But the commission sent another challenge to the waiver process to an administrative law judge for a November hearing.
With the council's unanimous approval of the ordinance, the city administration has until Nov. 21 to deliver a plan for the removal of a statue of Forrest to the council.
The ordinance approved on third and final reading is a substitute version from the original and lays out numerous paths forward in the controversy for the administration and council.
The memorial to lynching victims would come into play if the city cannot find a way to remove and relocate the statue.
"One of the other options for us is to speak volumes about how blacks were lynched," said council attorney Allan Wade, who is also representing the city administration in the two-track legal effort out of the Historical Commission that is likely on its way to Davidson County Chancery Court. "If we cannot come to a permanent solution for removal then you have an alternative path to repurpose that whole plaza to minimize his impact."
The other paths include the city starting the process with the Tennessee Historical Commission to remove the statue of Confederacy president Jefferson Davis from Memphis Park and the city closing Health Science Park where the Forrest statue has stood for more than 100 years.
Council member Patrice Robinson proposed the closing option during council committee sessions Tuesday.
"I'd like to see the park closed for the safety of our community," she said. "The council opened it. We need to close it. I just need to know the process."
Wade said the city would also pursue mediation with those opposed to the statues removal and field offers from those interested in buying the statue for relocation. That would happen even as the city keeps all of its legal options open including litigation at several levels. And he expressed hope that the city would prevail with the administration and the council acting together in a process Wade described as "Confederate hell."
"If not then I think we are going to be presenting something powerful to minimize and repurpose that whole area," he said.
The council also has Wade drafting a referendum ordinance to repeal the city's move to ranked-choice voting in the 2019 city elections under an earlier city charter amendment. First of three readings on the ordinance would be at the first council meeting in November.
Council member Edmund Ford Jr. also wants Wade to offer options for eliminating the runoff provision in races for the seven single-member council districts that are the only surviving runoff provision left in all of Shelby County politics.
"It looks at the legal points of the 1991 decision by (Federal) Judge Jerome Turner, which eliminated runoffs in particular races," Ford said of the ruling that eliminated the citywide or at-large council seats as well as the runoff requirement in the Memphis Mayor's race when no candidate got a simple majority of the votes cast.
Turner's ruling left in place runoffs in the single-member districts and Turner left it up to the council on what to replace the at-large council seats with. The council established two super districts – each taking in a half of the city with three council members elected to each super district with no runoff provision.
"Many of my council members asked about that because they did not want their single-member districts singled out, especially when that group of individuals could be susceptible to a process that is different from everybody else," Ford said.
Former Shelby County Commissioner Steve Mulroy argued the council should not scrap the ranked-choice voting charter amendment without at least trying it. RCV is also referred to as instant-runoff voting.
"If the city council succeeds in repealing instant-runoff voting they will essentially be diluting minority voting strength," said Mulroy who is a former civil rights attorney for the U.S. Justice Department and currently a University of Memphis law professor. "People asked for it. Try it once. The city council is trying to stop it -- I think, respectfully, they don't full apprehend how instant runoff voting works."
In other council action Tuesday, a 21-lot single family residential planned development at 6610 Messick Road by Kircher-Uhlhorn Development LLC on part of the Emmanuel United Methodist Church property was approved by the council.
The council approved an allocation of $4.4 million in federal Choice Neighborhoods grant money for capital improvement projects in the South City redevelopment area which includes the former Foote Homes and Cleaborn Homes public housing developments. Another $700,000 in city capital funding was approved and moved into place for a renovation of L.E. Brown Park in the Cleaborn Pointe at Heritage Landing development that is on the site of Cleaborn Homes.
And the council approved $498,800 in federal grant funding toward studying and planning for a roundabout at or near the intersection of West Georgia Avenue and Riverside Drive.


Last Monday, students rallied in front of Rice Hall. These individuals urged GW to affiliate with the Worker Rights Consortium – an organization aligned to prevent the use of sweatshop labor when making college apparel – and to adopt a workers' rights code of conduct ensuring a living wage, affordable healthcare and the right to organize unions. At approximately 1 p.m., demonstrators marched across the street to the Marvin Center. Several students resolved to set up tents in the lobby and refuse to leave until the University acceded to their demands. Students had prepared written statements to both university administrators and the University Police Department. Both parties also refused student requests that President Stephen Joel Trachtenberg be called.
Immediately following their entrance into the building, students were told the police were coming. One student read a prepared statement in order to inform the public of what was occurring. Rally participants were chanting as students set up tents. Brandon Neal – National Director of the Youth and College Division of the NAACP – made a statement in support of the students. When told that the noise level was problematic, students ceased the use of megaphones and asked their supporters to stop chanting. They immediately complied.
Once the Metropolitan Police arrived, students were told that they would be under arrest if they did not vacate the premises. Reiterating their position – and once again asking that President Trachtenberg be called – the students were told that there would be no negotiation. Eleven students – nine from GW and two from Georgetown – sat in a circle on the floor of the Great Hall and did not leave. At approximately 1:30 p.m., those students were handcuffed and placed under arrest by MPD. They are currently being charged with unlawful entry and are to appear in court for arraignment April 21. One of the Georgetown students arrested is now barred from entering the GW campus.
The University claims they had no choice but to immediately arrest the students. A 1968 resolution of the Board of Trustees states that if University officials feel that demonstrators must be removed or arrested at any point, the executive chair of the Faculty Senate and the student body president are to be called, if at all possible. Neither individual was notified, despite the fact that the students were simply seated peacefully. The students were not damaging any property. The students were not engaged in any act of violence. The students were not obstructing the movement of any individual, nor blocking any entrance. The students were not harassing, threatening or even engaging in conversation with anyone outside of the circle. The notion that the University administration had no choice but to immediately arrest these students is absolutely absurd. The students were simply carrying out a peaceful demonstration of solidarity with GW workers. The administration acted rashly and inappropriately.
The struggle for workers' right at GW continues. President Trachtenberg has still refused to affiliate with the Worker Rights Consortium or to even meet with students to discuss a labor code of conduct. Prior to Monday's arrests, students had followed every other possible avenue in an attempt to garner administrative support for workers' rights. They have obtained thousands of petition signatures and several Student Association resolutions. They have held teach-ins, worker panels and other educational forums. They have held numerous demonstrations and have met with administrators. The students felt they had no choice but to escalate their actions in order to demonstrate to the administration that their concerns were serious.
We are not criminals. We are students who believe that workers' rights are human rights, and we are appalled that the university would take such action. President Trachtenberg has said he is ashamed of us. Other administrators have said they are disappointed in us. They tell us they admire our passion for a cause, and they believe in workers' rights just as we do. Yet, they refuse to take action or to even meet with us regarding our concerns. Thus, the campaign continues, and we need even more help than ever. We demand the University affiliate with the Worker Rights Consortium, adopt a labor code of conduct and drop all charges against the 11 students arrested last Monday. Our resolve is now even stronger, and our struggle will continue. Please join us April 7 at 8 p.m. in Marvin Center room 403 to learn more about the issues and how you can help out with the campaign for workers' rights at GW.
-The writer is a GW tent city resident.


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Pick up the pace with the lightweight Swift Run Athletic Shoe from adidas in hot new red/camo! Optimized for comfort and style, the Swift Run Athletic Shoe features a breathable knit upper with signature side stripes, and lightweight EVA midsole for exceptional impact resistance and support. Available online at Journeys.com!


'Beetle Queen,' by M.G. Leonard, cover illustration by Elisabet Portabella.
Having loved the first book in this trilogy (Beetle Boy), when I found out that there was a limited edition of Beetle Queen with sprayed edges, I was straight on-line ordering myself a copy. And it was worth it! The yellow ladybird spots are a true delight. Let me just fill you in quickly … Continue reading 'Beetle Queen,' by M.G. Leonard, cover illustration by Elisabet Portabella.
'The Bear Who Stared,' and 'The Lumberjack's Beard,' by Duncan Beedie.
I'm delighted to bring you not one, but two, brilliant picture books in this post. And one of them has just been nominated for the Waterstone's Children's Book Prize 2017! The Bear Who Stared Bear liked nothing better than to come out of his cave in the morning and stare, and stare, and stare.... The … Continue reading 'The Bear Who Stared,' and 'The Lumberjack's Beard,' by Duncan Beedie.
'The Everything Machine,' by Ally Kennen, illustrated by Chris Jevons.
Welcome to my stop on the 'The Everything Machine' blog tour. I was very excited to be able to get my hands on a copy to read and review. Have you ever wished you could print yourself anything you wanted? Rare Pokémon cards, strawberry ice cream, a brand new bike? How about a mountain of … Continue reading 'The Everything Machine,' by Ally Kennen, illustrated by Chris Jevons.
'Alistair Grim's Odditorium,' by Gregory Funaro.
I'd like to share a delightfully odd duo set in a world where the odd is the ordinary: 'Alistair Grim's Odditorium,' by Gregory Funaro, illustrated by Chris Mould The unlikely hero of this piece is Grubb, a twelve-year-old orphan scraping a living as a chimney sweep in Victorian England. After an unfortunate accident … Continue reading 'Alistair Grim's Odditorium,' by Gregory Funaro.
'Lucy Lady Bird,' by Sharon King-Chai.
This glorious book has just been published with a new cover after the release of Sharon's second book, 'Snail Mail.' Lucy Lady Bird is feeling sad as her spotty friends keep telling her she doesn't belong with them as she has no spots. She flies off to be alone but keeps bumping into some of … Continue reading 'Lucy Lady Bird,' by Sharon King-Chai.
'Follow the Trail series,' from DK.
The next two books are from a new interactive book series aimed at toddlers and pre-schoolers. Both books have lots of fun interactive elements to physically engage young readers. There are plenty of glittery, bumpy trails for fingers to follow, encouraging the development of the fine motor skills needed for pre-writing. My three year old … Continue reading 'Follow the Trail series,' from DK.
'Harry Potter Quidditch Deluxe Book and Model Set,' from Incredibuilds, written by Jody Revenson.
In celebration of Harry Potter Book Night last week, I built a rather magical golden snitch courtesy of this book: I am huge fan of all things Harry Potter so was very excited to be sent a copy of this title and another in the Incredibuilds series, 'Aragog' but as I'm scared of spiders, I … Continue reading 'Harry Potter Quidditch Deluxe Book and Model Set,' from Incredibuilds, written by Jody Revenson.
It's Good to be You!
For this blog post, I have chosen two fantastic books which celebrate the importance of being yourself and pursuing your dreams. 'Duck Gets a Job,' by Sonny Ross Duck wants a job. All his friends quack on and on about how amazing their jobs in the city are. Duck thinks their jobs sound a bit … Continue reading It's Good to be You!


This is a 15 credit Level 4 qualification which consists of 3 units which due to popular demand we have decided to offer on an 'open access basis'.
This course fits latest policy and practice and meets the needs of the current workforce. We have developed a comprehensive professional guidance resource and a reflective workbook to support and embed learning.
The open training runs over 6-day face to face training days. There is also a comprehensive assessment process over 6 months which includes assignments, work products and case studies. All learners will have a one to one professional discussion in their workplace and all assessments are done individually based on the learner's role and agreed at the start of the course.
We have received excellent feedback from the course with 100% of registered learners completing and gaining the full qualification in under 12 months.
This could include those working in Early Help setting, Children's Centres, Family Support, Schools, Social Work, Police and many more….
For more information on the Unit content see here.


text:
Jan 05 2016 January 5, 2016 January 5, 2016 3Comments by Administrator
'For the wrong acts of previous Govt. we are blamed for deforestation' – President
When there is a possibility to provide lands from other places for the purpose of resettlement without doing the deforestation, taking narrow decisions the previous government damaged the Wilpattu National Park and today, some section of our society allegedly blames for the present government in this regard, President Maithripala Sirisena said.
He made these observations participating in a ceremony to present appointment letters to 290 Forest Field Assistants held at the Ape Gama premises in Battaramulla, today (4).
The President said that his government will take stern actions to protect the natural resources including the forests.
He further said that as the Minster of Mahaweli Development and Environment ha has planned a three-year national strategy to protect the environment including the forest resource.
Everyone should be committed to fulfill their responsibilities towards protecting Earth's biodiversity , the President said that adding the new government is working with a plan to increase the country's forest cover from its existing 29 per cent to 32%.
The President also said that he will take steps to ban the tobacco cultivation fully in the country in 2020 and said that the policy of the present government is to choose only good quality productions for the people's health and eliminate everything which pose a threat to the health of the public.
The Laws will be strictly imposed against the persons who break the rules on polythene ban, which is effective from 1st of January, 2016, he added.
Secretary Ministry of Ministry of Mahaweli Development and Environment- Mr. Udaya R. Seneviratne , The Director General of the Forest Conservation and others participated in the event.
(President's Media)
3 Responses to 'For the wrong acts of previous Govt. we are blamed for deforestation' – President
Amarakoon says:
Mr. President it is true that deforestation of Wilpattu National Park started during the previous government. It is the duty of the present government to put an immediate holt to this act of insanity.
ISama Gunawardhana says:
What is the forestry department doing in Battarmulla?
What is the mahaweli authority doing in Colombo?
The paddy marketing board and the agriculture department b holed in Kandy.
The executives in their air conditioned offices has little else ought to formulate viable policy for they are most likely ought to have data. These guys are nothing more time serving yes men.
If Mr Sirisena means business then they should be given the option of working in areas that would serve the purpose further they must be mde accountable.
In order to achieve accountability they bureaucrats should be devise policies and plan to accommodate these policies. Since these are in their making failure is not option and should face the consequences
In the past members of Parliament were accused of illegal deforestation and was done with the conniving of all the department cpncerne
Sam Fernando says:
Yes what is MY3 doing. What are u waiting for take immediate action to correct or halt all wrong doings by the previous leaders. Do something great that the people will remember you like MR did saving our country from the tigers
Stop complaining about MR. He has been away almost a year now
Home » 'For the wrong acts of previous Govt. we are blamed for deforestation' – President

redpajama_set_name: RedPajamaCommonCrawl


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The Glaucoma Professional Education Programme is for New Zealand optometrists, nurses, orthoptists, ophthalmic technicians and other eye health professionals interested in furthering their understanding of glaucoma and its clinical management. Registered optometrists can earn credits as part of their ongoing professional registration requirements.
The programme is largely case-based, comprising a series of seminars based on clinical case studies. The seminars cover a planned programme of topics which will link academic knowledge with practice. As well as questions and answers to accompany each case, there is an academic discussion of the important features of the case described.
The programme consists of 7 courses, each with a case history, questions and answers for self-directed learning, followed by an associated web-based examination. The examination associated with each case is made up of 25 multi-choice and true/false questions.
All cases have been produced by qualified glaucoma specialists. The 2019 cases were compiled and prepared by Dr Jinny Yoon in conjunction with Professor Helen Danesh-Meyer and Dr Hannah Kersten.


text:
16 and 17-year-olds can now register to vote in next year's Senedd elections
Monday 1 June 2020, 4:05pm
Credit: PA
Young people aged 16 and 17 can now register to vote in Senedd and council elections in Wales.
It comes into force as part of the Senedd and Elections (Wales) Act which was passed last year.
An Electoral Commission survey found that 75% of 16 and 17-year-olds voted in the Scottish independence referendum.
Now in Wales, 16 and 17-year olds can now register to vote in next year's Senedd election. The move means young people in Wales will now be able to have a say in devolved issues such as health, education and the economy.
The Health Minister Vaughan Gething said it gives young people a ''voice in democracy''.
Next year's Senedd elections, which are due to take place next Spring, will be the first in which 16 and 17-year-olds and legally resident foreign nationals will be allowed to vote in Wales.
The Electoral Reform Society, an organisation that campaigns for voting reform in the UK, said it is a ''victory for young people'':
This is a victory for young people, following campaigning from ERS Cymru and a coalition of youth and civil society campaigners. As we've already seen in Scotland, this is a boost for our democracy as a whole – strengthening citizenship and boosting political engagement.
Electoral Reform Society
Assembly passes new law to give 16 and 17-year-olds the right to vote in Welsh elections


text:
//
// NCWorkerParent.m
// Newton Commander
//
#if ! __has_feature(objc_arc)
#error This file must be compiled with ARC. Use -fobjc-arc flag (or convert project to ARC).
#endif

#import "NCLog.h"
#import "NCWorker.h"
#import "NCWorkerThread.h"
#import "NCWorkerProtocol.h"
#include <unistd.h>

@interface NCWorker () {
	id m_controller;
	NSString* m_path_to_worker;
	NCWorkerThread* m_thread;
	NSString* m_identifier;
	int m_uid;
}

+(NSString*)createIdentifier;
-(void)restartTask;
@end

@implementation NCWorker

-(id)initWithController:(id<NCWorkerController>)controller pathToWorker:(NSString*)pathToWorker {
    self = [super init];
    if(self != nil) {
		m_controller = controller;
		m_path_to_worker = [pathToWorker copy];
		m_thread = nil;
		m_identifier = [NCWorker createIdentifier];
		[self resetUid];

		NSAssert(m_controller, @"must be initialized");
		NSAssert(m_path_to_worker, @"must be initialized");
		NSAssert(m_identifier, @"must be initialized");
    }
    return self;
}

-(id)initWithController:(id<NCWorkerController>)controller {
	return [self initWithController:controller pathToWorker:[NCWorker defaultPathToWorker]];
}

+(NSString*)defaultPathToWorker {
	NSString *bundlePath = [[NSBundle mainBundle].resourcePath stringByAppendingPathComponent:@"NewtonCommanderBrowse.bundle"];
	NSBundle *bundle = [NSBundle bundleWithPath:bundlePath];
	NSAssert(bundle, @"cannot find our bundle");
	NSString *path = [bundle.resourcePath stringByAppendingPathComponent:@"NewtonCommanderHelper"];
	NSAssert(path, @"bundle does not contain the worker");
	return path;
}

+(NSString*)createIdentifier {
	static NSUInteger tag_counter = 0;
	NSUInteger pid = getpid();
	NSUInteger tag = tag_counter++; // autoincrement it
	return [NSString stringWithFormat:@"browse_worker_%lu_%lu",
		(unsigned long)pid, (unsigned long)tag];
}

-(void)setUid:(int)uid {
	m_uid = uid;
}

-(void)resetUid {
	m_uid = getuid();
}

-(void)start {
	if(m_thread) return;

	NSString* uid_str = [NSString stringWithFormat:@"%i", m_uid];
	// uid_str = @"501"; // user: neoneye
	// uid_str = @"503"; // user: johndoe
	// uid_str = @"-2";  // user: nobody
	// uid_str = @"0";   // user: root
	// uid_str = @"";    // ignore user

	m_thread = [[NCWorkerThread alloc]
		initWithWorker:self
		controller:m_controller
		path:m_path_to_worker
		uid:uid_str
		identifier:m_identifier
	];
	[m_thread setName:@"WorkerThread"];
	[m_thread start];
}

-(void)restart {
	LOG_DEBUG(@"ncworker.%s", _cmd);

	NCWorkerThread* t = m_thread;
	if(!t) {
		[self start];
		t = m_thread;
		NSAssert(t, @"start is always supposed to initialize m_thread");
	}

	NSString* uid_str = [NSString stringWithFormat:@"%i", m_uid];

	NSThread* thread = t;
	id obj = t;
	SEL sel = @selector(setUid:);

	NSInvocation* inv = [NSInvocation invocationWithMethodSignature:[obj methodSignatureForSelector:sel]];
	[inv setTarget:obj];
	[inv setSelector:sel];
	// arguments starts at 2, since 0 is the target and 1 is the selector
	[inv setArgument:&uid_str atIndex:2];
	[inv retainArguments];

	[inv performSelector:@selector(invoke)
    	onThread:thread
		withObject:nil
		waitUntilDone:NO];

	[self restartTask];
}

-(void)restartTask {
	NCWorkerThread* t = m_thread;
	if(!t) return;
	NSAssert(t, @"start is always supposed to initialize m_thread");

	//NSThread* thread = t;
	id obj = t;
	SEL sel = @selector(restartTask);

	NSInvocation* inv = [NSInvocation invocationWithMethodSignature:[obj methodSignatureForSelector:sel]];
	[inv setTarget:obj];
	[inv setSelector:sel];
	[inv performSelector:@selector(invoke)
    	onThread:m_thread
		withObject:nil
		waitUntilDone:NO];
}

-(void)request:(NSDictionary*)dict {

	// start thread if not already started
	NCWorkerThread* t = m_thread;
	if(!t) {
		[self start];
		t = m_thread;
		NSAssert(t, @"start is always supposed to initialize m_thread");
	}

	NSData* data = [NSArchiver archivedDataWithRootObject:dict];

	NSThread* thread = t;
	id obj = t;
	SEL sel = @selector(addRequestToQueue:);

	NSInvocation* inv = [NSInvocation invocationWithMethodSignature:[obj methodSignatureForSelector:sel]];
	[inv setTarget:obj];
	[inv setSelector:sel];
	// arguments starts at 2, since 0 is the target and 1 is the selector
	[inv setArgument:&data atIndex:2];
	[inv retainArguments];

	[inv performSelector:@selector(invoke)
    	onThread:thread
		withObject:nil
		waitUntilDone:NO];
}

@end /* end of class NCWorker */

redpajama_set_name: RedPajamaGithub


text:
Aging Pipelines - What Are the Risks?
Groundbreaking independent research sponsored by Enbridge and CAEPLA will find out
By Paul Vogel
Canada's nationally regulated oil and gas pipelines were originally constructed more than 50 or 60 years ago. Many of these pipelines are reaching the end of their useful economic life. The National Energy Board (NEB) has the regulatory authority to authorize pipeline companies to decommission or abandon these pipelines.
While the NEB has implemented a toll surcharge to generate funds for this purpose, the abandonment funding currently being generated will be sufficient only to accomplish removal of approximately 20 per cent of this pipeline infrastructure. Landowners across Canada who may be left with the remaining pipelines buried in their lands are becoming increasingly concerned about resulting interference with their agricultural operations, human and livestock health and safety risks, and potential future costs and liabilities.
In a decision released April 25, 2016, the NEB granted Enbridge Pipelines Inc.'s application for authorization to decommission its aging Line 3 pipeline in Western Canada and to replace it with a new Line 3 pipeline in an adjacent easement.
CAEPLA, the Manitoba Pipeline Landowners Association (MPLA) and the Saskatchewan Association of Pipeline Landowners (SAPL) jointly intervened in this proceeding to represent their landowner member interests with respect to Line 3 decommissioning. Enbridge's Line 3 decommissioning plan contemplates leaving the decommissioned Line 3 pipeline in place after internal cleaning while continuing cathodic protection to reduce corrosion rates as well as periodic monitoring for ground subsidence.
In responding to Enbridge's proposal, CAEPLA/MPLA/SAPL raised landowner concerns including definition of appropriate cleaning criteria; development of segmentation methodology to prevent the pipeline becoming a conduit for ground water and contaminants; and hazards for agricultural equipment, people, machinery and livestock that could result from pipe collapse and ground subsidence.
Enbridge has acknowledged that the extensive disbonding of the Line 3 polyethylene tape pipe coating will render cathodic protection ineffective to prevent corrosion, and has estimated time to through-wall penetration at 25 to 50 years. Progressively greater agricultural surface loads increase the potential for pipeline collapse and ground subsidence. In addition to health and safety concerns and related costs and liabilities, topsoil loss upon ground subsidence would result in permanent long-term production losses.
The CAEPLA – Enbridge jointly commissioned study is now underway at the University of Calgary. It is an important first step to better defining the risks and liabilities of pipelines decommissioned and abandoned in place and to developing acceptable methodologies to reduce risks for landowners.
In the negotiated settlement resolving landowner concerns with respect to the new Line 3 construction in March 2015, CAEPLA/MPLA/SAPL and Enbridge agreed to continue consultation on how to resolve these Line 3 decommissioning issues. CAEPLA/MPLA/SAPL and Enbridge subsequently concluded and filed with the NEB a further Settlement Agreement addressing Line 3 decommissioning.
Under the terms of this agreement, Enbridge acknowledges its liability with respect to decommissioned or abandoned pipelines and agrees to implement measures similar to active pipelines to maintain depth of cover, facilitate crossing with agricultural equipment and address subsidence/drainage issues.
Recognizing the considerable uncertainties related to anticipated Line 3 corrosion rates, pipe collapse potential and resulting implications for landowners, CAEPLA/MPLA/SAPL and Enbridge agreed to jointly commission and direct independent, third-party research at a Canadian university to study the impacts of decommissioning and abandoning pipelines in place, with a view to further defining the associated risks and consideration of alternative decommissioning/abandonment methodologies.
Enbridge is responsible both for the funding of this research project and for the costs of CAEPLA's participation, including CAEPLA's own independent consultants. As part of this agreement, Enbridge has also provided to landowners a prepayment to be applied on account of possible future decommissioning or abandonment damages.
In its decision granting Enbridge's application for Line 3 decommissioning, the Board references the CAEPLA/MPLA/SAPL – Enbridge Settlement Agreement:
"The Board views this Agreement as a positive initiative and found it to be a persuasive factor in favour of the reasonableness of Enbridge's decommissioning plan… The Board expects Enbridge to continue to consult with affected… landowners during the Decommissioning Activities and the Decommissioning Period and periodically reassess the constraints and hazards that limit pipeline removal to arrive at a solution that is agreeable to all parties, based on site-specific circumstances."
While authorizing Enbridge's Line 3 decommissioning, the Board expressly states:
"However, this does not mean that the Board will not order pipeline removal in a future case, should the evidence support it. It also does not mean that the Board will not order the removal of the Decommissioned Line 3 Pipeline in the future if circumstances change. This may occur where the benefits of removing certain segments of the Existing line 3 Pipeline outweigh the risks of the pipeline remaining in-place."
The CAEPLA/MPLA/SAPL – Enbridge jointly commissioned study represents part of Enbridge's required Line 3 decommissioning continuing landowner consultation. This research is now underway at the University of Calgary. It is an important first step to better defining the risks and liabilities of pipelines decommissioned and abandoned in place, and to developing acceptable methodologies to reduce these risks for landowners.
The final report that results from this research will assist landowners, the industry, and regulators in addressing these issues as Canada's aging energy pipeline infrastructure is removed from use. It is anticipated that this report will be filed with the NEB prior to Line 3 decommissioning and will then form the basis for regulatory approval for possible required changes to Enbridge's current Line 3 decommissioning plan.
Paul G. Vogel is a partner in the London, Ont., law firm of Cohen Highley LLP. He practices in the area of commercial litigation and environmental law.


Come out for an evening of appetizers and drinks (wine tasting with beer option), plus vote for the winners of the cat photo contest! There will also be a raffle and silent auction. Please come out and help us raise funds to aid our less fortunate feline friends here in Western NC!
Kids' Mad Mountain Mud Run!


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With a mill located in Schwedt, Germany, LEIPA has for many years been providing continental Europe and the UK with 100% recycled white-top linerboard. Board produced from waste paper decreases consumption of naturally occurring forest products and reduces landfill deposits.
Leipa has teamed with SHARP International to make their full line of coated and uncoated white-top linerboards available to corrugators in the US and Canada.
For additional information on LEIPA Georg Leinfelder GmbH and their products, please visit their website.


text:
Never-before-seen colour footage has emerged of JFK riding in his presidential motorcade moments before he is assassinated. The short clip, which was believed lost until earlier this year, shows the President looking relaxed and giving a thumbs up as he is driven past cheering crowds lined up along Main Street in Dallas.
The footage was shot shortly before the motorcade headed west towards Dealey Plaza, where Kennedy was assassinated.
It was taken by office worker Andre Leche, who was living in Dallas at the time. He had just bought a new movie camera and thought the President's visit would be a perfect opportunity to use it. Mr Leche died in 1987 and the film canister was thought lost. But this year his son Paul was placing something in his safety deposit box and discovered a yellow Kodak box with 'Kennedy' written on it.
He said: 'My family lived in Dallas in November of 1963. On the 22nd my father, Andre Leche, decided we should use his new movie camera to film President Kennedy. 'After my father's death in 1987 the original film canister was lost until this year. After looking in vain in my house, I was putting something valuable in my safety deposit box and came across a yellow Kodak box with "Kennedy" written on it.'
Read more about this fascinating story here.
Tags: 11-22, 11-22-1963, 11-22-63, dealey plaza, jfk assassination, jfk assassination conspiracy, jfk conspiracy, jfk evidence, JFK home movie, jfk new evidence, John F. Kennedy, kennedy assassination, Kennedy Film, Kennedy Movie, Lee Harvey Oswald, New Evidence, New JFK Film, New JFK Movie, november 22, november 22 1963, November 22nd, November 22nd 1963, Zapruder
Categories 11-22, 11-22-1963, 11-22-2013, 11-22-63, 1963, assassination conspiracy, dealey plaza, JFK, jfk assassination conspiracy, jfk conspiracy, JFK Film, JFK II, JFK Movie, john f. kennedy, John F. Kennedy Film, John F. Kennedy Movie, kennedy assassination, kennedy conspiracy, Kennedy Film, Kennedy Movie, Lee Harvey Oswald, LHO, november 22, november 22 1963, november 22nd, Zapruder
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One Response to "New Never-Seen Film of President Kennedy in Dallas"
James Morrison January 11, 2015 at 3:38 pm #
just read an interesting ebook entitled The Camelot Coup The Overthrow Our Government Tried to Hide, a historical fiction detailing the conspiracy to murder kennedy and pin it on Oswald; the tale is weaved using the historical figures as the main characters of the book, including Oswald, Johnson, Hoover, etc, some of which is told through Lee's perspective; it certainly challenges the warren report and tells why that fairy tale was produced to cover up the true killers and the men behind it. Jim


text:
/*
 * the entry of the App root store
 */

import { useMemo } from 'react'
import { applySnapshot } from 'mobx-state-tree'

import type { TRootStore } from '@/spec'
import RootStore from './RootStore'

let clientSideRootStore: TRootStore | undefined

const initRootStore = (snapshot = null): TRootStore => {
  // if (!snapshot) return clientSideRootStore
  const rootStore = RootStore.create(snapshot, {})

  if (snapshot) {
    applySnapshot(rootStore, snapshot)
  }

  // For SSG and SSR always create a new store
  if (typeof window === 'undefined') return rootStore
  // Create the store once in the client
  if (!clientSideRootStore) clientSideRootStore = rootStore

  return rootStore
}

// this is from next.js offical MST example
export const useStore = (initialState = {}): TRootStore => {
  const store = useMemo(() => initRootStore(initialState), [initialState])
  return store
}

export const holder = 1


text:
Missions - Dye, Paul
Paul and Pat Dye
Paul and Pat Dye became acquainted with Scenic Park Bible Church in the very early 2000's as a result of Brian Porterfield's having his plane worked on there at the New Tribes Mission Aviation (NTMA) facilities in McNeal, Arizona. Brian invited Paul to speak at Scenic Park Church during our annual missions conference that year, and Paul, Pat, and their son Larry made an exciting first trip to Alaska.
Since that time Scenic Park has been an intricate part of the Dye's missionary lives. Because of NTMA policy, the Dyes had to retire as employees in the fall of 2015 when they turned seventy-five years old. However they still continue as volunteers and NTMA members. Paul trains NTMA students on a fill-in basis as needed. He also works doing aircraft maintenance at the hangar with his son/boss, Larry, who is head of maintenance at the McNeal NTMA facility.
Paul continues to be of help to the widows of the community…It could be a full-time job, but Paul and Pat's Sunday morning prison ministry takes preeminence in Paul's use of time. Last year he calculated that he spends sixteen hours a month in the Douglas Arizona Prison Complex if all goes well and there are no lock downs or storms to close down the chapel. The Dyes are in their twentieth year in this prison ministry, and find the men to be a very captive audience to Paul's teaching. Pat has the worship service first and plays the keyboard as they sing.
Paul and Pat attend a local church fellowship not far from NTMA and serve there when possible. Pat enjoys helping teach in Kids Club meetings every Tuesday. Paul and Pat have begun a Bible study with a couple from the church and pray for the salvation of the husband of the couple.
Paul was able to pass his medical to keep his license to fly. God spared his life during a kidnapping by communist guerilla fighters in Colombia, S.A. in 1985, and he has been able to fly the Cessna 185 that God used to get him away from the guerrillas. Paul and Larry were able to go to OshKosh, the largest air show in the USA, to represent NTMA. Paul and Pat also took part in two NTMA expositions to inform people and churches in the Phoenix area about NTMA and the ministry they do around the world.
Paul and Pat are very thankful that they have their son Larry and his wife Kim next door, although both of Larry and Kim's children are out of the nest and out on their own. Paul and Pat now have four grandchildren in Tucson and so get to see them occasionally!
The Dye's other two children are serving the Lord in other areas of the country. Their daughter Lisa and her husband are ministering to the Hispanic population in Aurora, CO. and are translating chronological Bible Studies into the Spanish language for pastors to use and teach. Paul and Pat's youngest son, Luke, is still Senior Pastor at Whitestone Community Church in Oconomowoc, WI, and he and his wife celebrated their tenth year there. Luke's wife suffers from much pain and so Luke not only has the care of the church but also the care of his household. Being so far away makes it difficult for Paul and Pat to help in his situation except for prayer.
Paul and Pat are so grateful to God for their children and that they have continued to choose to walk in truth. They have no greater joy than that! Now they are praying for their grandchildren that they also would make wise choices to walk with God in this wicked world.
In February 2016, Paul was told by his heart doctor that he had either lymphoma or leukemia. It was a hard blow for Paul and Pat both. But after further blood tests, an oncologist determined that Paul has a chronic non-aggressive type of leukemia. The doctor said that if Paul lives to be one hundred years old, he would die with it but not because of it. At this point it is at "stage zero". However every six months he will have to have more blood tests to monitor it. What blessed news that was for them!
The Dyes ask the Scenic Park Bible Church family to pray that Paul and Pat might know good health in the coming year. Pray for their contact with the many inmates, that the Dyes can see fruit and that the inmates will desire to walk close to the Lord. Please pray for the salvation of the people the Dyes have Bible studies and contact with each week.
9314 N. Wynn Drive
McNeal, AZ 85617
Return to Missions page


text:
ArchyFantasy Reviews, The Lost History of Ancient America
All Your Bases is Underwater: Section 3 of Lost History of Ancient America.
April 10, 2017 ArchyFantasies	1 Comment
In the briefest of introductions, Joseph outlines the purposes of the Section III.
"Our pursuit of Upper Michigan's Copper Barons…" (Joseph 71)
So, among other things, we're still looking for transoceanic bronze-age travelers.
We've already met two of the three authors from this section. Wayne May provides a second article about a possible underwater village in Wisconsin, and the mysterious Julia Patterson tells us about a sunken civilization in near Oregon.
Added to this is Andrew E. Rothovious (1919-2009). He is one of those rare individuals who is actually pretty interesting to learn about in his own right. An extremely prolific writer, he has potentially 4000 articles written across numerous publications, including Ancient America, Fate, and other alternative history/archaeology magazines. He was verbosely interested in a wide range of topics that included religion, Lovecraft, and Celtic visits to the New World (Magnus N.d). Rothovious had no formal education in archaeology or history from the sounds of it, but he did appear to be self informed, and as such drew some interesting conclusions about American Prehistory. Honestly though, beyond warm words and the occasion reference to his work, I can't find anything out about the man or his actual writings.
Joseph erroneously refers to Rothovious with the title of "Sage of Providence" (Joseph 71). I can only find Lovecraft himself referred to by this title, though there is one reference to Rothovious as "The Sage of Milford" (The City 2010), so perhaps that was just a typo as Rothoviuous appears to be a dedicated fan of Lovecraft's.
Then we are thrust into the articles of Section III:
Chapter 9: Drowned Village of the Ancient Copper Miners by Wayne N. May
Chapter 10: Sunken Civilization Found off Oregon? by Julia Patterson
Chapter 11: The Walls in the Lake by Andrew E. Rothovious
With that we're on our way into the next section.
If you'd like to support this blog, consider donating on Patreon or PayPal under ArchyFantasies@gmail.com
Want more on this topic? Go to: ArchyFantasies Reviews – The Lost History of Ancient America.
Comment below or send an email to ArchyFantasies@gmail.com.
Magnus, Margaret
N.d Andrew Rothovius. http://www.trismegistos.com/MagicalLetterPage/Rothovius/index.html. Retrieved 4/6/17
ANDREW ROTHOVIUS, RIP. October 7, 2010.
http://thecityintheworld.blogspot.com/2010/10/andrew-rothovius-rip.html Retrieved 4/6/17
Book ReviewsSunken CivilizationsThe Lost History of Ancient AmericaUnderwater Cities
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One thought on "All Your Bases is Underwater: Section 3 of Lost History of Ancient America."
busterggi says:
I can't help wondering why, if North America was such a paradise for these bronze mining Europeans, said Europeans didn't just settle here in NA and build communities as they had back in Europe. Would have saved them one hell of a commute.


Yeah, sure dare me to read your eerie tales of supernatural horror. Or is it weird yarns of unseen terrors? Well, if you are going to dare me, make up your mind!
Here we see the most gummy skeleton around. He must have really taken the healthly gums lecture from the dentist to heart, because he's keep a real great pair of them! The guy he's "kissing and killing", and hopefully in that order, isn't screaming as he gets hit, but demanding the skeleton tell him his gum-brushing ritual.
Skeleton's a jerk, though. Not going to tell him. Might kiss him. Will certainly kill him, but will never tell him his gum hygiene secrets. He'll take that to the grave. Or already did!


The Washington, DC Water and Sewer Authority's (DC Water) new facility reflects a commitment to sustainable initiatives in Washington, DC. The project, an active utility, is designed to LEED-Platinum specification, and employs technology which has yet to be used in the United States. While the building's design alleviates over-abundant daylighting and solar heat gain, the heating and cooling system is particularly noteworthy. The system harnesses DC Water's wastewater as a source of thermal energy to condition the building, making it one of the lowest energy consuming buildings in the region. Upon completion in 2017, the facility will serve as an international model for innovation and resiliency in a water management facility.
As a nod to the utility's mission, the design keeps water at a visual and auditory level – especially when it rains. Conceived as a functioning model of stormwater management, the facility illustrates the hydrologic cycle of storm events – from rainfall to collection, to treatment, to re-use. Runnels within the facility's paving channel stormwater from both the building's roof gardnes and surface to bio-retention swales: planted areas that are designed to remove pollutants and silt from surface runoff. Water that does not infiltrate the plantings is held in an underground cistern and used for future plant irrigation and to flush the building's toilets.
In addition to the new headquarters for DC Water, the site houses over 300 employees, bill paying services, and tours of the working sewage pumping station. The site development is intricately woven through the existing tapestry of functioning and abandoned pipe lines, and provides views on the Anacostia River and optimizes opportunities for human engagement.


Shiitake Mushroom Extract - 4 oz.
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Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, very often the target protein accumulates into insoluble aggregates in a misfolded and biologically inactive form. Bacterial inclusion bodies are major bottlenecks in protein production and are hampering the development of top priority research areas such structural genomics. Inclusion body formation was formerly considered to occur via non-specific association of hydrophobic surfaces in folding intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria resembles to the well-studied process of amyloid fibril formation. Both processes appear to rely on the formation of specific, sequence-dependent, intermolecular interactions driving the formation of structured protein aggregates. This similarity in the mechanisms of aggregation will probably allow applying anti-aggregational strategies already tested in the amyloid context to the less explored area of protein aggregation inside bacteria. Specifically, new sequence-based approaches appear as promising tools to tune protein aggregation in biotechnological processes.
In the last decade, protein aggregation has moved beyond being a mostly ignored area of protein chemistry to become a key topic both in medical and biotechnological sciences . The biological significance of protein deposition has been shown to be much higher than formerly thought. First, because the presence of insoluble protein deposits in human tissues correlates with the development of some debilitating human disorders of growing incidence such as Alzheimer's disease, Parkinson's disease, type II diabetes and the transmissible spongiform encephalopathies [2–4]. Second, because it has been shown than under cellular stress conditions, such us severe heat, massive protein misfolding exceeds the buffering capacity of the folding quality machinery and results in the aggregation of proteins, which usually results in cell death [5, 6]. Finally, the use of bacteria as factories for recombinant expression is limited by their intrinsic tendency to accumulate the target protein into inactive insoluble aggregates, called inclusion bodies (IBs). IBs are dense, amorphous protein deposits that can be found in both the cytoplasmic and periplasmic space of bacteria [7–11]. In fact, the formation of IBs is the main bottleneck in protein production, narrowing the spectrum of relevant polypeptides obtained by recombinant techniques and hampering the development of top priority research areas such as the de novo design of novel proteins, the rational modification of natural proteins or structural and functional genomics. The rising recognition of the crucial significance of protein aggregation has resulted in a number of recent reviews [12–19]. This review focuses mainly on the role played by intrinsic polypeptide properties in protein aggregation.
One should distinguish between precipitates, in which proteins maintain the native folded conformation and aggregates, in which proteins adopt new non-native structures. The first type of self-assembly is generated during random precipitation of already native protein due to an environment promoted reduction of solubility in the polypeptide chain. Examples of these processes are salting out by ammonium sulfate or isoelectric precipitation. Reducing ionic force or shifting solution's pH results in immediate dissolution of these precipitates. The second type of macromolecular structures exhibits, without exception, an increase in β-sheet secondary structure content relative to the native conformation and very high concentrations of denaturants or detergents are needed to dissolve them into mainly unfolded polypeptide chains. We will focus our attention on these aggregates, which include amyloid fibrils, thermal aggregates and bacterial IBs. The progress made on the control of their aggregation propensities by means of primary sequence modulation is discussed.
Protein aggregation has long been considered to be an unspecific process driven by the establishment of non-native contacts between proteins in totally or partially unfolded conformations to form a disordered precipitate. This idea was sustained in part by the diversity of morphologies of aggregates that were observed by techniques such as electron microscopy and atomic force microscopy . This way, the typical amyloid aggregate is a long, straight and unbranched fibril with a diameter between 40 Å and 120 Å , whereas inclusion bodies appear as bigger globular electro-dense structures seen as refractile bodies under phase contrast microscopy usually with near 1 micron in diameter  and thermal aggregates are usually amorphous . Recent work shows however that often aggregation is a much more specific event than previously expected at least in amyloid fibrils and bacterial IBs [24–27]. In fact, for many biotechnologically relevant proteins, isolation of the IBs is an efficient initial step in the purification process, since they contain usually more than 90% of recombinant protein , other proteins trapped in the aggregates are proteolytic fragments of the aggregating protein , other aggregation-prone polypeptides deposited by titration of chaperones during recombinant expression [30, 31] or even contaminants from the purification process . Similarly in Alzheimer and related neurodegenerative diseases in vivo amyloid plaques are composed primarily of the pathogenic aggregating protein rather than resulting from a widespread recruitment of other amyloidogenic proteins, although proteins such as proteases or chaperones have been also found to co-localize in the amyloid deposits .
Amyloid fibrils are thought to form trough self-assembly of protein monomers via a nucleation dependent pathway similar to the highly ordered process of protein crystallization . This mechanism is also behind physiological ordered protein aggregation processes as viral coat assembly, microtubule formation or flagellum formation . All these processes are characterized by an initial slow nucleation phase, in which the protein associates to form ordered oligomeric nucleus followed by a growth phase, in which the nucleus rapidly growths to form larger insoluble polymers. Addition of preformed protein nucleus during the lag time results in immediate polymerization. All these aggregation processes and in particular amyloid fibril formation are highly specific. This way, in the aggregation of β-amyloid protein, islet amyloid peptide, transthyrretin, and prion protein the formation of amyloid fibrils is not seeded by preformed fibrils of similar amyloidogenic proteins [34–36]. Although it has been shown that some amyloid fibrils can accommodate up to 1% of a foreign peptide, indicating than some co-aggregation can occur , the efficiency of this event decreases rapidly as differences in protein sequence of co-aggregating proteins increases showing that specific protein-protein interactions are needed for amyloid fibril formation to occur .
Aggregation into IBs during recombinant protein expression has been usually though to occur via non-specific association of hydrophobic patches on the surface of folding intermediates. However, the reduced number of IBs (usually one) formed during recombinant protein expression in bacteria suggested that the may be formed by the growth of a reduced number of "founder" aggregates in a nucleation-like mechanism. In this respect, the aggregation of the P22 coat protein has been extensively characterized [39–42] and it was demonstrated that when partially folded species of this protein where mixed in vitro with those of tailspike protein, no co-aggregation occurs, despite the fact that both form IBs when expressed individually in bacteria . The folding intermediates for each protein preferred to self-associate indicating specificity in the in vitro aggregation process and suggesting that specific interactions may underlie IBs formation in the cell. Very recently, we have confirmed this extent by showing that the preformed IBs of an aggregation-prone β-galactosidase variant are able to act as effective aggregating cores for the aggregation of its soluble, partially folded counterpart in a dose-dependent manner . Moreover, the aggregation process is highly specific as shown by the fact that preformed IBs promote deposition of homologous but not heterologous polypeptides. Both protein sequence and conformation appear to play a role in the establishment of specific intermolecular contacts between aggregating polypeptide chains to form IBs, since aggregated β-galactosidase moiety in IBs do not recognize the properly folded tetrameric enzyme .
Inclusion bodies in mammalian cells, the so-called aggresomes, are far more complex structures that those in bacteria containing many proteins, including molecular chaperones, components of the ubiquitin-proteasome system, centrosomal material, and cytoskeletal proteins . This suggested that co-aggregation of misfolded, damaged, or mutant proteins with normal cellular proteins could explain both the presence of multiple proteins in IBs and the toxicity associated with protein aggregation in many neurodegenerative diseases . However, also in this complex system, protein aggregation into IBs exhibits exquisite specificity even among extremely hydrophobic substrates expressed at very high levels . Thus, independent of the source, both amyloid fibril formation and IBs aggregation depend, at least partially, on the formation of specific protein-protein interactions between non-native species.
The formation of amyloid fibrils was initially associated to a reduced number of proteins related to recognized pathological situations. Nevertheless, a growing number of globular proteins not related to disease can be induced to generate similar fibrils in vitro, albeit in some cases only in non-native conditions, leading to the suggestion than the ability to form amyloids is intrinsic to many or all polypeptides when their normal folding pathways are compromised [47–50]. This appears to be true for IBs as well since deposition in such structures has been reported in the recombinant expression of many, but not all, heterologous genes and in the high level expression of several endogenous genes [7, 51, 52].
No sequence or structural similarities are apparent between any of the proteins that display the ability to form amyloids. Prior to fibrillation, amyloidogenic polypeptides may be rich in β-sheet, α-helix, β-helix, or combine α-helices and β-sheets. They may be globular proteins with a stable unique conformation in the native state or belong to the class of natively unfolded proteins. Despite these differences, the fibrils formed by different polypeptides display many common properties including high content of β-sheet secondary structure forming a core cross-β architecture in which continuous β-sheets are formed with β-strands running perpendicular to the long axis of the fibrils .
As in the case of amyloids, proteins incorporated in IBs are not related either structurally or sequentially and deposition during heterologous expression in bacteria has been reported for small, large, monomeric or multimeric proteins. The internal architecture of IBs has long thought by molecular biologists to be amorphous, despite the fact that several observations in the early 90's pointed to the presence of ordered structure in IBs [54–56]. The use of attenuated total reflectance FTIR in IBs formed by all-α, all-β or α +β showed that in all cases, even for all-β proteins, significant new β structure, compared to that in the native conformation, was observed. Interestingly, the amount of secondary structure in the inclusion body varies from one protein to another, as does the amount of disordered structure. More recently, others and we have recapitulated these studies in previously unexplored protein systems, showing clearly that the intermolecular interactions leading to aggregation in IBs in the cell involve β-sheet like interactions [27, 57]. Although the exact nature of the intermolecular interactions is unknown, and could be different in different IBs, the overall FTIR data suggest that the newly formed β-sheets in IBs are tightly packed with short hydrogen bonds providing them high stability. These features are reminiscent of those stabilizing the structure of amyloid fibrils . In addition, Thioflavin-T and Congo red, two dyes used for the diagnostic of amyloid structures also bind to IBs, confirming thus certain resemblance in the internal organization of both kinds of aggregates . Also, even if we still lack structural information on thermal aggregates purified directly from bacteria under stress conditions, it has been shown that in vitro heat denaturation leads to the formation of thermal aggregates that display the β-sheet signature as analyzed by FTIR  and are also able to bind amyloid dyes .
Despite the fact that the different types of aggregates share similar characteristics, they are obviously not identical and exhibit a series of distinctive features. First, most amyloid fibrils are SDS-insoluble, whereas SDS can usually dissolve IBs. This observation is in agreement with the higher extent of β-sheet content of amyloids relative to that in IBs, in which the presence of some native or disordered structure can be still detected [27, 60]. As a result amyloids would display more and stronger intermolecular non-covalent interactions that would provide them with higher order and stability in front of denaturation, while sharing similar overall connectivity between polypeptide chains than this present in IBs. Also, the regulation of amyloid and bacterial aggregates formation in vivo appears to be somehow different. In this sense, it has been demonstrated that in yeast the formation of amyloids by the Sup 35 prion is highly dependent on the presence of the Hsp 104 chaperone . In contrast, the role of the bacterial Hsp 104 homologue, ClpB, in the regulation of inclusion body formation in E. coli is more controversial, some studies indicating that, as in the case of Hsp 104, it binds preferentially to the hydrophobic surface of aggregated protein , while others suggesting only a moderate role in the process of aggregation, which is mainly controlled by the chaperones DnaK and GroEL . Interestingly, the bacterial chaperone GroEL is able to modulate both in vitro  and in vivo in mammalian cells  the aggregation of proteins involved in amyloid pathologies, suggesting that in spite of the constrains imposed by the different cellular contexts some similitude may still exist between the mechanisms of bacterial and eukaryotic protein aggregation.
Regardless of the existence of some structural or functional differences between the aggregates formed in bacteria and those in eukaryotic cells, in both cases there is an inherent tendency to kidnap misfolded protein in the interior of such supra-molecular structures. It is suggested that this is a mechanism evolved to reduce the potential toxicity of partially folded monomers or small oligomers, which by exposing large hydrophobic surfaces could interact inappropriately with a wide range of cellular components, hampering this way cell function . In these sense, specific aggregation could be a conserved strategy playing a cellular protective role.
One of the major unanswered questions of protein aggregation is the specificity with which primary sequence determines both the aggregation propensity and the specific details of the aggregated structure. The hypothesis that the ability of proteins to form ordered aggregates is a general property of the polypeptide chain rather to be limited to a restricted set of proteins  seems reasonable, especially if the main driving force for aggregation is the formation of an inter-backbone hydrogen-bonded network leading to the above described β-sheets structures, since all polypeptides regardless of sequence share the polypeptide backbone. In this regard, IBs and amyloid formation abilities has not been associated a priori to particular protein sequences, being this fact, an additional obstacle to predict the yield of a given protein in a new production process or its cellular toxicity. However, in recent times it is coming clear that sequence modulates aggregation, giving a chance to control the unwanted protein deposition phenomena.
A first indication that sequence controls deposition comes from the observation that not all regions of a polypeptide are equally important for determining the aggregation propensities. This way, we have proved recently that very short specific amino acid stretches can act as facilitators or inhibitors in the incorporation of globular proteins into amyloid fibrils . These relevant regions are usually known as aggregation "hot spots". Aggregation-prone regions are blocked in the native state of globular proteins because their side chains are usually hidden in the interior of the protein hydrophobic core or already involved in the establishment of the network of native contacts that stabilizes a protein. This is the reason why globular proteins rarely aggregate from their native states. Destabilization usually results in an increased population of partially folded molecules and is well established as a trigging factor in disorders associated with the deposition of proteins that are globular in their normal functional states .
Accordingly, peptides and proteins involved in the most prevalent human neurodegenerative diseases are mostly unstructured within the cell . In these disorders, protein deposition does not require the unfolding of a globular native conformation and occurs by direct self-assembly of the unstructured polypeptide chains, in which aggregation-prone, usually hydrophobic, regions are already exposed to solvent. The presence of aggregation "hot spots" have been already described in the peptides and proteins underlying Alzheimer's, Creutzfeldt-Jakob disease, or some systemic amyloidogenic disorders [69–71]. Independent of the native conformation and stability of the protein, the high level of expression during recombinant production results in a large number of polypeptides emerging from the ribosome in at least partially unfolded conformations which usually associate to form IBs. Even if not yet proved, it is thinkable that the presence of aggregation prone sequences in these conformers will influence at least partially the equilibrium between aggregated and folded protein during recombinant expression. Interestingly, it is observed that proteins assembled into amyloid in vitro usually render insoluble during recombinant protein expression. For example, this happens for proteins involved in disease such us Aβ42 amyloid peptide, β-2-microglobulin, mammalian prions and human islet amyloid polypeptide [72–75].
The study of the effects of mutations on the formation of amyloid fibrils and IBs also point to the role of sequence as an aggregation controller. Two types of mutations should be distinguished according to their ability to destabilize or not significantly the native state of the protein. As stated before, destabilizing mutations favour aggregation by originating an ensemble of partially unfolded conformations allowing this way the establishment of inter-molecular interactions. In addition, it has been shown that punctual mutations can also facilitate aggregation without affecting the native state stability when they promote the conversion of already unfolded or partially folded polypeptides into oligomeric forms that further aggregate to form insoluble species. In these cases, protein aggregation has been found to be tuned by mutations that change the polarity, the secondary structure propensity or the net charge of the polypeptide. In general, increases in hydrophobicity and β-sheet propensity result in increased aggregation whereas an increase in the overall net charge decreases this tendency [24, 76, 77]. There are a good number of protein systems in which it has been shown that point mutations may dramatically affect the amount of aggregate formation; these include the P22 tailspike protein, single-chain antibodies, interferon-γ, colicin A, Che Y, immunoglobulin domains, and interleukin-1β for IBs formation [43, 78–83] and SH3-domains, acylphosphatase, amylin, prion peptides, α-synuclein, amyloid-β-peptide and tau for amyloid formation [25, 67, 84–88]. Notably, mutant proteins with reduced in vitro amyloid propensity are expressed usually in E. coli as more soluble proteins than the natural occurring ones , whereas providing a previously in vitro soluble protein increased amyloid propensity results in accumulation as IBs during recombinant expression [90, 91]. Moreover, when amyloid proteins have been designed de novo, all proteins displaying amyloid properties in vitro accumulated in vivo as bacterial IBs , but the rational introduction of point mutations that convert these aggregation-prone proteins into monomeric β-sheet forms allowed their expression in bacteria in soluble forms . These observations strongly suggest that both aggregation phenomena are related and depend in last term on tendency to self-aggregate associated to individual protein sequences. This way, it appears that the study of bacterial models may contribute significantly in the future to the understanding of protein misfolding and aggregation, since they are fast, simple and biologically relevant experimental systems. Conversely, it is thinkable that the application of successful anti-depositional strategies derived from the numerous studies dealing with amyloid fibril formation to the less explored area of protein aggregation within the cell may provide clues to optimize biotechnological protein production. In this regard, simple sequence-based computational approaches have been developed very recently which permit to predict with reasonable accuracy the aggregation propensity of polypeptides [94–97]. In particular, TANGO a statistical mechanics algorithm based on the physico-chemical principles of β-sheet formation, extended by the assumption that the core regions of an aggregate are fully buried, accurately predicts the aggregation propensity of a data set of more than 200 different peptides [95, 96]. Without doubt, these new algorithms born in the sinus of the amyloid area are going to be very useful tools for the rational modification of polypeptides for biotechnological applications, opening the door to a fully automated, sequence-based design strategies to improve the solubility of proteins of industrial interest.
There is an increasing need for the efficient production of genetically engineered proteins as a result of the success of the genome sequencing projects. From the different host that may be used to produce this large set of proteins, bacteria, mainly E. coli, still appears as the default option, particularly when the biological activity of the protein does not depends on post-translational modifications. E. coli is fast and inexpensive to culture, easy to handle and manipulate genetically and usually renders high levels of recombinant products. However, expression of recombinant proteins in E. coli often results in the accumulation of the protein product in inactive IBs in the cell. The recovery of bioactive proteins from IBs is a complex process. Still, IBs formation is such a frequent phenomena in protein production that a large number of in house and commercial protocols and solutions have been developed in order to obtain pure, active and soluble protein from IBs [17, 98]. Nevertheless, the purification of protein from IBs usually requires the optimization of refolding conditions for each individual target, the recovery yields are usually poor and one should be sure that the refolding procedure does not affect the integrity and activity of the recovered protein. In addition, purification of over-expressed soluble proteins is faster and cheaper than obtaining it in a pure form from IBs, especially at large scale. Overall, optimizing the levels of soluble protein is nowadays a more attractive strategy to increase pure and active protein yield than recovering highly expressed protein in aggregated form .
The observation that natural proteins are usually soluble in their biological environments may help to maximize soluble expression levels in recombinant approaches. This way, nature has provided proteins with a reasonable conformational stability in the native state, in which most of the hydrophobic residues, amide and carboxyl groups and aggregation-prone sequence stretches are buried or involved in intra-molecular interactions. This appears as a very successful strategy used to avoid aggregation, since few proteins are able to aggregate from its stable native conformation. Along with this, over-stabilized proteins of thermophilic organisms are usually expressed in soluble forms during recombinant protein production [100–102] and a positive correlation between thermostability and solubility has been recently reported . In addition, the analysis of protein databases has shown that highly aggregating sequences are less frequent in proteins than innocuous amino acid combinations and that, if present; they are surrounded by amino acids that disrupt their aggregating capability . These evidences support the suggestion that natural protein sequences have evolved in part to code for structural characteristics other than those included in the native fold, such as avoidance of aggregation. According to this, protein aggregation results from a failure of the natural protective strategies under special circumstances, such as recombinant protein expression.
Using rational design to engineer target proteins in order to emulate and reinforce natural anti-aggregation mechanisms, taking advantage of the above mentioned computational methods to predict aggregation, appears thus as a reasonable approach to overwhelm protein deposition and optimizing the levels of soluble protein in biotechnological processes. Few, but successful experimental steps have been taken already in this direction. First, improving thermodynamic stability by rational mutation has been shown to render more soluble heterologous protein versions . Second, it has been proven that decreasing the intrinsic propensity to aggregate of the partially unfolded state of an aggregation-prone protein by modulating the net polypeptide charge and introduction of electrostatic repulsions also results in increased solubility . Finally, the analysis, identification and disruption by mutation of sequential "hot spots" of aggregation has allowed the recovering from the E. coli supernatant of previously aggregated polypeptides [67, 93, 106].
The raising interest to understand the mechanisms underlying protein aggregation in the cell has crystallized in a good number of recent relevant studies in an area whose biological significance is coming of central importance in biotechnology. The scenario emerging from these efforts is especially encouraging because one can foresee a future in which rational design of protein solubility based on natural laws will allow to tune aggregation, permitting to over-pass the main bottleneck in high throughput expression projects.
The author is recipient of a "Ramón y Cajal" contract awarded by the MCYT-Spain and co-financed by the Universitat Autonoma de Barcelona (UAB) and founded by PNL2004-40 from UAB.