Replication Data for: A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins
<|begin_of_text|><|start_header_id|>system<|end_header_id|> You are a research archivist expert in dataset metadata. Answer the question truthfully.  <|eot_id|><|start_header_id|>user<|end_header_id|> Here is the Description of a dataset. Description:'The datasets provide source data for this study, sorted by topic and technique. After expanding the archives additional metadata can be found. Abstract: The nucleocapsid (N-)protein of SARS-CoV-2 is one of the most abundant and multi-functional viral proteins. It is composed of two folded domains for nucleic acid binding and dimerization, respectively, that are linked and flanked by large segments of intrinsically disordered regions (IDRs). N-protein has a key role in viral assembly and scaffolding of the viral RNA. It promotes liquid-liquid phase separation (LLPS), forming dense droplets that support the assembly of ribonucleoprotein particles with as-of-yet unknown macromolecular architecture. Here we describe a heretofore unknown oligomerization site that contributes to LLPS, is required for the assembly of higher-order protein-nuclei' . Please return only a json list of at most 3 Keywords corresponding to the Description:.<|eot_id|><|start_header_id|>assistant<|end_header_id|> {"Answer" : ["nucleocapsid protein","SARS-CoV-2"]} <|eot_id|>
 Here is the Description of a dataset. Description:'The datasets provide source data for this study, sorted by topic and technique. After expanding the archives additional metadata can be found. Abstract: The nucleocapsid (N-)protein of SARS-CoV-2 is one of the most abundant and multi-functional viral proteins. It is composed of two folded domains for nucleic acid binding and dimerization, respectively, that are linked and flanked by large segments of intrinsically disordered regions (IDRs). N-protein has a key role in viral assembly and scaffolding of the viral RNA. It promotes liquid-liquid phase separation (LLPS), forming dense droplets that support the assembly of ribonucleoprotein particles with as-of-yet unknown macromolecular architecture. Here we describe a heretofore unknown oligomerization site that contributes to LLPS, is required for the assembly of higher-order protein-nuclei' . Please return only a json list of at most 3 Keywords corresponding to the Description:.
The datasets provide source data for this study, sorted by topic and technique. After expanding the archives additional metadata can be found. Abstract: The nucleocapsid (N-)protein of SARS-CoV-2 is one of the most abundant and multi-functional viral proteins. It is composed of two folded domains for nucleic acid binding and dimerization, respectively, that are linked and flanked by large segments of intrinsically disordered regions (IDRs). N-protein has a key role in viral assembly and scaffolding of the viral RNA. It promotes liquid-liquid phase separation (LLPS), forming dense droplets that support the assembly of ribonucleoprotein particles with as-of-yet unknown macromolecular architecture. Here we describe a heretofore unknown oligomerization site that contributes to LLPS, is required for the assembly of higher-order protein-nuclei
nucleocapsid protein; SARS-CoV-2