{{short description|American biochemist and geneticist}} right|thumb|Wickner at the National Institutes of Health in 1995 '''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.<ref name=":0">{{Cite web|url=http://www.einstein.yu.edu/education/phd/alumni/sue-wickner.aspx|title=Sue Wickner|website=Albert Einstein Medical School|access-date=November 28, 2018}}</ref> Her laboratory is under the National Cancer Institute and is located in the Center for Cancer Research (NCI/CCR).<ref name=":1">{{Cite web|url=https://irp.nih.gov/pi/sue-wickner|title=Sue Wickner|website=National Institutes of Health|access-date=November 28, 2018}}</ref>
== Education == Sue earned the B.S. degree from American University and the M.S. from Georgetown University.<ref name=":1" /> She studied at the Corcoran School of Art and went on to earn her Ph.D. in 1973 from Albert Einstein College of Medicine of Yeshiva University. Her dissertation advisor there was Jerard Hurwitz.<ref name=":0" /> She pursued postdoctoral training at National Institutes of Health with Martin Gellert, then joined the Laboratory of Molecular Biology at the National Cancer Institute.<ref name=":1" /> She did a sabbatical with Fred Sanger at the MRC in Cambridge UK in 1983.
== Research == Sue Wickner and her coauthors Michel Wright, 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.<ref>H. G. Echols. (2001) ''Operators and Promoters:The Story of Molecular Biology and Its Creators''. University of California Press, Berkeley, CA. {{ISBN|9780520920767}}.</ref> At NIH, her research has illuminated the action of proteins that utilize adenosine triphosphate (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 regulate most cellular processes including replication and transcription and response to stress. Chaperones function to alter activity, refold as well as degrade proteins.<ref name=":0" /> 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.<ref name=":2">{{Cite web|url=http://www.nasonline.org/member-directory/members/20007479.html|title=Sue Hengren Wickner|website=National Academy of Sciences|access-date=November 28, 2018}}</ref>
== Honors and awards == * National Academy of Sciences Member, 2004<ref name=":2" /> * American Academy of Arts and Science Member, 2002<ref name=":0" /> * American Association for the Advancement of Science Fellow, 2001<ref name=":0" />
== Books == * 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, {{ISBN|9789814749329}}.
== Selected works == *{{cite journal | pmid = 38534118 | doi=10.1128/mmbr.00176-22 | volume=88 | title=Hsp90, a team player in protein quality control and the stress response in bacteria | pmc=11332350 | year=2024 | journal=Microbiol Mol Biol Rev | page=e0017622 | last1 = Wickramaratne | first1 = AC | last2 = Wickner | first2 = S | last3 = Kravats | first3 = AN | issue=2 | article-number=e00176-22 }} *{{cite journal | last1 = Wickramaratne | first1 = AC | last2 = Liao | first2 = JY | last3 = Doyle | first3 = SM | last4 = Hoskins | first4 = JR | last5 = Puller | first5 = G | last6 = Scott | first6 = ML | last7 = Alao | first7 = JP | last8 = Obaseki | first8 = I | last9 = Dinan | first9 = JC | last10 = Maity | first10 = TK | last11 = Jenkins | first11 = LM | last12 = Kravats | first12 = AN | last13 = Wickner | first13 = S | year = 2023 | title = Proteins form Binary Complexes with Hsp90 and Ternary Complexes with Hsp90 and Hsp70 | url = | journal = J Mol Biol | volume = 435 | issue = 17| pages = 168–184 | doi = 10.1016/j.jmb.2023.168184 | pmid = 37348754 | pmc = 10527347 }} *{{cite journal | pmid = 36572186 | doi=10.1016/j.jbc.2022.102826 | volume=299 | title=Diptoindonesin G, a new Hsp90 drug | pmc=9841029 | year=2023 | journal=J Biol Chem | article-number=102826 | last1 = Wickramaratne | first1 = A | last2 = Wickner | first2 = S | issue=1 | doi-access=free }} *{{cite journal | pmid = 34375543 | doi=10.1146/annurev-micro-032421-035644 | volume=75 | title=The Bacterial Hsp90 Chaperone: Cellular Functions and Mechanism of Action | year=2021 | journal=Annu Rev Microbiol | pages=719–739 | last1 = Wickner | first1 = S | last2 = Nguyen | first2 = TL | last3 = Genest | first3 = O}} * {{cite journal | last1 = Genest | first1 = O | last2 = Wickner | first2 = S | last3 = Doyle | first3 = SM | year = 2019 | title = Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling | url = | journal = J Biol Chem | volume = 294 | issue = 6| pages = 2109–2120 | doi = 10.1074/jbc.REV118.002806 | doi-access = free | pmid = 30401745 | pmc = 6369297 | bibcode = 2019JBiCh.294.2109G }} * {{cite journal | last1 = Kravats | first1 = A. N. | last2 = Doyle | first2 = S. M. | last3 = Hoskins | first3 = J.R. | last4 = Genest | first4 = O. | last5 = Doody | first5 = E. | last6 = Wickner | first6 = S. | year = 2017 | title = Interaction of E. coli Hsp90 with DnaK involves the DnaJ binding region of DnaK | url = | journal = Journal of Molecular Biology | volume = 429 | issue = 6| pages = 858–872 | doi = 10.1016/j.jmb.2016.12.014 | pmid = 28013030 | pmc = 5357148 }} * {{cite journal | last1 = Reidy | first1 = M. | last2 = Street | first2 = T.O. | last3 = Hoskins | first3 = J.R. | last4 = Camberg | first4 = J.L. | last5 = Agard | first5 = D.A. | last6 = Masison | first6 = D.C. | last7 = Wickner | first7 = S. | year = 2013 | title = Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast | url = | journal = Mol. Cell | volume = 49 | issue = 3| pages = 464–473 | doi = 10.1016/j.molcel.2012.11.017 | pmid = 23260660 | pmc = 3570620 }} * {{cite journal | last1 = Doyle | first1 = S. M. | last2 = Genest | first2 = O. | last3 = Wickner | first3 = S. | year = 2013 | title = Protein rescue from aggregates by powerful molecular chaperone machines | url = | journal = Nat Rev Mol Cell Biol | volume = 14 | issue = 10| pages = 617–629 | doi = 10.1038/nrm3660 | pmid = 24061228 }} * {{cite journal | last1 = Miot | first1 = M. | last2 = Reidy | first2 = M. | last3 = Doyle | first3 = S.M. | last4 = Hoskins | first4 = J.R. | last5 = Johnston | first5 = D.M. | last6 = Genest | first6 = O. | last7 = Masison | first7 = D.C. | last8 = Wickner | first8 = S. | year = 2011 | title = Species-specific collaboration of heat shock proteins (Hsp)70 and 100 in thermotolerance and protein disaggregation | url = | journal = Proc. Natl. Acad. Sci. USA | volume = 108 | issue = 17| pages = 6915–6920 | doi = 10.1073/pnas.1102828108 | doi-access = free | pmid = 21474779 | pmc = 3084080 | bibcode = 2011PNAS..108.6915M }} * {{cite journal | last1 = Genest | first1 = O. | last2 = Hoskins | first2 = J.R. | last3 = Camberg | first3 = J.L. | last4 = Doyle | first4 = S.M. | last5 = Wickner | first5 = S. | year = 2011 | title = Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling | url = | journal = Proc Natl Acad Sci U S A | volume = 108 | issue = 20| pages = 8206–11 | doi = 10.1073/pnas.1104703108 | doi-access = free | pmid = 21525416 | pmc = 3100916 | bibcode = 2011PNAS..108.8206G }} * {{cite journal | last1 = Wickner | first1 = S. | year = 1978 | title = DNA Replication Proteins of ''Escherichia coli'' | url = | journal = Annu Rev Biochem | volume = 78 | issue = | pages = 1163–1191 | doi = 10.1146/annurev.bi.47.070178.005503 | pmid = 354492 }}
== References == {{Reflist}}
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{{DEFAULTSORT:Wickner, Sue Hengren}} Category:Year of birth missing (living people) Category:Living people Category:American geneticists Category:American women geneticists Category:American molecular biologists Category:American women microbiologists Category:Members of the United States National Academy of Sciences Category:American University alumni Category:Georgetown University alumni Category:Albert Einstein College of Medicine alumni Category:Fellows of the American Association for the Advancement of Science Category:National Institutes of Health people Category:20th-century American women scientists Category:21st-century American women scientists