Sue Wickner
Sue Hengren Wickner is an American Biochemist and Geneticist who is a Distinguished Investigator and the head of the DNA Molecular Biology Section of the National Institutes of Health.[1] Her laboratory is under the National Cancer Institute and is located in the Center for Cancer Research (NCI/CCR).[2]
Education
Sue Wickner was awarded the BS from American University and the MS from Georgetown University.[2] She received her PhD in 1973 from Albert Einstein College of Medicine of Yeshiva University. Her dissertation advisor there was Dr. Jerry Hurwitz.[1] She pursued postdoctoral training at National Institutes of Health with Martin Gellert, then joined the Laboratory of Molecular Biology at the National Cancer Institute.[2]
Research
Sue Wickner and her coauthors Reed Wickner and Jerry Hurwitz published an early paper showing DNA replication in the test tube. They found that the bacterial virus or phage Phi X174 could be converted from single stranded to the double stranded replicative form in the test tube and that the reaction required the gene products of dnaC, dnaE, and dnaG genes of the phage. Operators and Promoters.
At NIH, her research has illuminated the action of proteins that utilize Adenosine Tri Phosphate (ATP) energy in tiny machines to replicate DNA, remodel proteins, and break down proteins. She has been a major contributor to the understanding of molecular chaperones, proteins that assist other proteins to change in shape, to move about, and to break down.[1] 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.[3]
Honors and Awards
National Academy of Sciences Member, 2004[3]
American Academy of Arts and Science Member, 2002[1]
American Association for the Advancement of Science Fellow, 2001[1]
Book
Lila Gierasch, Arthur Horwich, Christine Slingsby, Sue Wickner, and David Agard. ( 2016)Structure And Action Of Molecular Chaperones: Machines That Assist Protein Folding In The Cell World Scientific Publishing Company Pte Ltd, ISBN13 9789814749329.
Selected Works
S. Wickner (1978) “DNA Replication Proteins of Escherichia coli.” Annu Review of Biochem. 78: 1163-1191.
A. N. Kravats, S. M. Doyle, J.R. Hoskins, O.Genest, E, Doody, S. Wickner (2017) “Interaction of E. coli Hsp90 with DnaK involves the DnaJ bionding region of DnaK. Journal of Molecular Biology 429 (6):858-872.
O.Genest, M. Reidy, T.O. Street, J.R.Hoskins, J.L.Camberg, D.A.Agard, D.C. Masison, and S.Wickner (2013) “ Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.” Mol. Cell. 49(3):464-473.
S. M. Doyle, O. Genest, and S. Wickner (2013) “Protein rescue from aggregates by powerful molecular chaperone machines.” Nat Rev Mol Cell Biol. 14(10): 617-629.
M. Miot. M. Reidy, S.M. Doyle, J.R. Hoskins, D.M. Johnston, O. Genest, M.C.Vitery, D.C. Masison, and S. Wickner (2011) “Species-specific collaboration of heat shock proteins (Hsp)70 and 100 in thermotolerance and protein disaggregation. Proc. Natl. Acad. Sci. USA 108 (17): 6915-6920.
O. Genest, J.R.Hoskins, J.L.Camberg, S.M.Doyle, and S. Wickner (2011) “Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Natl Acad Sci U S A. 108(20):8206-11.
- ^ a b c d e "Sue Wickner". Albert Einstein Medical School. Retrieved November 28, 2018.
{{cite web}}: Cite has empty unknown parameter:|dead-url=(help) - ^ a b c "Sue Wickner". National Institutes of Health. Retrieved November 28, 2018.
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