She has been a major contributor to the understanding of molecular chaperones, proteins that regulate most cellular processes including replication and transcription and response to stress. Chaperones function to alter activity, refold as well as degrade proteins.[2] Her citation from election to the National Academy of Sciences notes her most recent contributions to ATP-dependent chaperones for proteolysis (protein breakdown), showing how they participate in stress responses by removing proteins that folded incorrectly and how they degrade regulatory proteins once their signals have been delivered. Since there are some human diseases that result from abnormally folded and/or aggregated proteins, these ATP-dependent chaperones are important in disease treatment development.[4]