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{{Short description|American biologist (born 1951)}}
{{Infobox scientist
{{Infobox scientist
|name = Arthur L. Horwich
| name = Arthur L. Horwich
|image =
| image = WALS 1.27.10 Arthur Horwich 4m49s (cropped).jpg
|image_size =
| image_size =
|caption =
| caption =
|birth_date = 1951
| birth_date = {{birth year and age|1951}}
|birth_place =
| birth_place =
|death_date =
| death_date =
|death_place =
| death_place =
|residence = [[United States]]
| nationality = American
|citizenship =
| field = [[Biology]]
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| work_institutions = {{ubl|[[Yale School of Medicine]]|[[Howard Hughes Medical Institute]]}}
|nationality = [[United States|American]]
|ethnicity =
| alma_mater = [[Brown University]]
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| doctoral_advisor =
|field = [[Biology]]
| notable_students = Tapan K. Chaudhuri<ref>{{Cite web | url=http://web.iitd.ernet.in/~tkchaudhuri | title=Tapan K. Chahudhuri- Chaperone Mediated Protein Folding, Protein Engineering and Molecular Biophysics Group}}</ref>
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|work_institutions = [[Yale School of Medicine]]<br />[[Howard Hughes Medical Institute]]
|alma_mater = [[Brown University]]
| known_for = uncovering chaperonin action
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| author_abbrev_bot =
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|doctoral_advisor =
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| author_abbrev_zoo =
|students = Tapan K. Chaudhuri<ref>http://web.iitd.ernet.in/~tkchaudhuri</ref>
|known_for = uncovering chaperonin action
| influences =
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| influenced =
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|author_abbrev_bot =
| prizes = {{unbulleted list|[[Gairdner Foundation International Award]] (2004)| [[Wiley Prize]] (2007)| [[Rosenstiel Award]] (2008)|[[Louisa Gross Horwitz Prize]] (2008)|[[Lasker Award]] (2011)|[[Albany Medical Center Prize|Albany Prize]] (2016)|[[Shaw Prize]] (2012)|[[Breakthrough Prize in Life Sciences|Breakthrough Prize]] (2020) [[BBVA Foundation Frontiers of Knowledge Award]] (2023)}}
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|author_abbrev_zoo =
|influences =
| religion =
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|influenced =
|prizes = [[Hans Neurath Award]], Protein Society <small>(2001)</small><br> [[Gairdner Foundation International Award]] <small>(2004)</small><br>[[Stein and Moore Award]], Protein Society <small>(2006)</small><br> [[Wiley Prize|Wiley Prize in Biomedical Science]] <small>(2007)</small><br> [[Rosenstiel Award]] <small>(2008)</small><br>[[Louisa Gross Horwitz Prize]] <small>(2008)</small><br>[[Lasker Award]] <small>(2011)</small><br> [[Shaw Prize]] <small>(2012)</small>
|religion =
|footnotes =
}}
}}


'''Arthur L. Horwich''' (born 1951) is an [[United States|American]] [[biologist]] and [[Sterling Professor|Sterling Professor of Genetics and Pediatrics]] at the [[Yale School of Medicine]].<ref name="About Horwich">{{cite web |url=http://www.med.yale.edu/genetics/fac/ArthurHorwich.php |title=Arthur L. Horwich |accessdate=2008-03-18 |author= |date= |work= |publisher=Yale School of Medicine}}</ref><ref name="Form leads to function">{{cite web |url=http://www.medicineatyale.org/v1i2_august2005/lifelines.html |title=Form leads to function |accessdate=2008-01-24 |author= |date= |work= |publisher=Yale School of Medicine}}</ref> Horwich has also been a [[Howard Hughes Medical Institute]] investigator since 1990.<ref name="Arthur L. Horwich, M.D.">{{cite web |url=http://www.hhmi.org/research/investigators/horwich_bio.html |title=Arthur L. Horwich, M.D |accessdate=2008-01-24 |publisher=Howard Hughes Medical Institute}}</ref> His research into [[protein folding]] uncovered the action of [[chaperonin]]s, protein complexes that assist the folding of other proteins. Horwich first published this work in 1989.<ref>{{cite journal | author =Cheng, M.Y., Hartl, F.U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W., Hallberg, E. M., Hallberg, R. L. & Horwich, A. L. | date =February 16, 1989 | title =Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria | journal =Nature | volume =337 | issue = 6208| pages =620–625 | publisher = | location = | pmid =2645524 | doi =10.1038/337620a0 | url = }}</ref>
'''Arthur L. Horwich''' (born 1951) is an American [[biologist]] and [[Sterling Professor|Sterling Professor of Genetics and Pediatrics]] at the [[Yale School of Medicine]].<ref name="About Horwich">{{cite web|url=http://www.med.yale.edu/genetics/fac/ArthurHorwich.php |title=Arthur L. Horwich |access-date=March 18, 2008 |publisher=Yale School of Medicine |url-status=dead |archive-url=https://web.archive.org/web/20080530172030/http://www.med.yale.edu/genetics/fac/ArthurHorwich.php |archive-date=May 30, 2008 }}</ref><ref name="Form leads to function">{{cite web|url=http://www.medicineatyale.org/v1i2_august2005/lifelines.html |title=Form leads to function |access-date=January 24, 2008 |publisher=Yale School of Medicine |url-status=dead |archive-url=https://web.archive.org/web/20080521105441/http://www.medicineatyale.org/v1i2_august2005/lifelines.html |archive-date=May 21, 2008 }}</ref> Horwich has also been a [[Howard Hughes Medical Institute]] investigator since 1990.<ref name="Arthur L. Horwich, M.D.">{{cite web |url=http://www.hhmi.org/research/investigators/horwich_bio.html |title=Arthur L. Horwich, M.D |access-date=January 24, 2008 |publisher=Howard Hughes Medical Institute}}</ref> His research into [[protein folding]] uncovered the action of [[chaperonin]]s, protein complexes that assist the folding of other proteins; Horwich first published this work in 1989.<ref>{{cite journal | author =Cheng, M.Y. | author2 =Hartl, F.U. | author3 =Martin, J. | author4 =Pollock, R. A. | author5 =Kalousek, F. | author6 =Neupert, W. | author7 =Hallberg, E. M. | author8 =Hallberg, R. L. | author9 =Horwich, A. L. | name-list-style =amp | date =February 16, 1989 | title =Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria | journal =Nature | volume =337 | issue = 6208| pages =620–625 | pmid =2645524 | doi =10.1038/337620a0 | bibcode =1989Natur.337..620C | s2cid =4333381 | url =http://nbn-resolving.de/urn:nbn:de:bvb:19-epub-7516-2}}</ref><ref>{{Cite news|last=Wang|first=Shirley S.|date=2009-09-14|title=The Nobel Prize Will Go To...|language=en-US|work=Wall Street Journal|url=https://www.wsj.com/articles/SB10001424052970204683204574358170813148330|access-date=2022-02-11|issn=0099-9660}}</ref>

For his scientific work Horwich has been awarded the [[Canada Gairdner International Award|Gairdner International Award]] (2004), [[Louisa Gross Horwitz Prize]] (2008), [[Lasker Award]] (2011),<ref>{{Cite news|last=Zimmer|first=Carl|date=2011-09-12|title=Horwich Wins Lasker Award by Straddling Science and Medicine|language=en-US|work=The New York Times|url=https://www.nytimes.com/2011/09/13/science/13profile.html|access-date=2022-02-11|issn=0362-4331}}</ref> [[Shaw Prize]] (2012), [[Albany Medical Center Prize]] (2016), and [[Breakthrough Prize in Life Sciences|Breakthrough Prize]] (2020). He is a member of the [[National Academy of Sciences]] and the [[American Academy of Arts and Sciences]].<ref>{{Cite journal|last=Davis|first=Tinsley H.|date=2004-10-19|title=Biography of Arthur L. Horwich|journal=Proceedings of the National Academy of Sciences|language=en|volume=101|issue=42|pages=15002–15004|doi=10.1073/pnas.0406924101|issn=0027-8424|pmid=15479759|pmc=524080|doi-access=free}}</ref><ref>{{Cite web|first=Madison|last=Hahamy|date=2021-05-04|title=14 Yale faculty recently elected to the American Academy of Arts & Sciences|url=https://yaledailynews.com/blog/2021/05/03/14-yale-faculty-recently-elected-to-the-american-academy-of-arts-sciences/|access-date=2022-02-11|website=Yale Daily News|language=en}}</ref>


== Early years ==
== Early years ==
Horwich was born in 1951. He grew up in [[Oak Park, Illinois|Oak Park]], west of [[Chicago]].<ref name="Biography of Arthur Horwich">{{cite web |url=http://www.pnas.org/cgi/content/full/101/42/15002 |title=Biography of Arthur L. Horwich |accessdate=2008-01-24 |author=Tinsley H. Davis |date=2004 |work= |publisher=The National Academy of Sciences, USA}}</ref> In 1969, he entered [[Brown University]] as part of a new program that combined the undergraduate degree with medical school.<ref name="Biography of Arthur Horwich"/> During medical school, Horwich studied fat cell metabolism in the laboratory of [[John Fain]]. Horwich received his [[Bachelor of Arts|A.B.]] in biomedical sciences in 1972 and his [[Doctor of Medicine|M.D.]] in 1975.<ref name="About Horwich"/><ref name="Arthur L. Horwich, M.D."/> He graduated as valedictorian of the first class to complete the combined program.<ref name="Biography of Arthur Horwich"/> Horwich went on to do an internship and residency in pediatrics at [[Yale University]]. Midway through, Horwich was not sure about an entirely clinical future. After completing his residency, he joined the [[Salk Institute for Biological Studies]] in [[La Jolla, California]] for a postdoctoral position in molecular biology and virology.<ref name="Biography of Arthur Horwich"/> At Salk, he worked in Walter Eckhart's laboratory alongside [[Anthony R. Hunter|Tony Hunter]] and witnessed Hunter's discovery of tyrosine phosphorylation.<ref name="Biography of Arthur Horwich"/> He credits this time with sharpening his skills as a scientist. He said, "Tony taught me the nuts and bolts of thinking about a problem."<ref name="Biography of Arthur Horwich"/>
Horwich was born in 1951. He grew up in [[Oak Park, Illinois|Oak Park]], west of Chicago.<ref name="Biography of Arthur Horwich">{{cite journal |title=Biography of Arthur L. Horwich |journal=Proceedings of the National Academy of Sciences |volume=101 |issue=42 |pages=15002–15004 |author=Tinsley H. Davis |date=2004 |doi=10.1073/pnas.0406924101 |pmid = 15479759|pmc=524080 |doi-access=free }}</ref> In 1969, he entered [[Brown University]] as part of a new program that combined the undergraduate degree with medical school.<ref name="Biography of Arthur Horwich"/> During medical school, Horwich studied fat cell metabolism in the laboratory of John Fain. Horwich received his [[Bachelor of Arts|A.B.]] in biomedical sciences in 1972 and his [[Doctor of Medicine|M.D.]] in 1975.<ref name="About Horwich"/><ref name="Arthur L. Horwich, M.D."/> He graduated as valedictorian of the first class to complete the combined program.<ref name="Biography of Arthur Horwich"/> Horwich went on to do an internship and residency in pediatrics at [[Yale University]]. Midway through, Horwich was not sure about an entirely clinical future. After completing his residency, he joined the [[Salk Institute for Biological Studies]] in [[La Jolla, California]] for a postdoctoral position in molecular biology and virology.<ref name="Biography of Arthur Horwich"/> At Salk, he worked in Walter Eckhart's laboratory alongside [[Anthony R. Hunter|Tony Hunter]] and witnessed Hunter's discovery of tyrosine phosphorylation.<ref name="Biography of Arthur Horwich"/> He credits this time with sharpening his skills as a scientist. He said, "Tony taught me the nuts and bolts of thinking about a problem."<ref name="Biography of Arthur Horwich"/>


== Research ==
== Research ==
In 1981, Horwich moved back to [[New Haven, Connecticut]] for a postdoctoral fellowship at [[Yale University School of Medicine]]. He worked in the laboratory of [[Leon Rosenberg]].
In 1981, Horwich moved back to [[New Haven, Connecticut]] for a postdoctoral fellowship at [[Yale University School of Medicine]]. He worked in the laboratory of Leon Rosenberg.<ref>[http://archives.news.yale.edu/v32.n12/story7.html "Horwich is Higgins Professor of Cellular, Molecular Physiology"]. Yale</ref>


In 1984, he moved across the hall from Rosenberg's lab to start his own laboratory as an assistant professor in the department of genetics. He still collaborated with members of the Rosenberg laboratory, including Wayne Fenton. As an independent researcher, Horwich asked whether the pathway that imports an enzyme called [[ornithine transcarbamylase]] (OTC) into the [[mitochondria]] of mammalian cells also could work in yeast. In 1987, during a genetic screen in yeast, Horwich and his colleagues stumbled across a protein folding function inside [[mitochondria]]. In the mutant strain, proteins entered mitochondria from the [[cytosol]] normally but then misfolded and aggregated. They named the protein encoded by the affected gene [[HSP60]], Heat shock protein 60, because it has a mass of 60 kDa and is produced in larger quantity in response to heat. Hsp60 is found in an 850 kDa double ring assembly, each ring containing 7 copies of Hsp60. Such assemblies, known as chaperonins, also exist in other cellular compartments and are essential components, mediating protein folding under both heat shock and normal conditions.<ref>{{cite journal |author=Cheng, M.Y., Pollock, R.A., Hendrick, J. P. & Horwich, A. L. |date=June 15, 1987 |title=Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae |journal=PNAS |volume=84 |issue=12 |pages=4063–4067 |publisher = The National Academy of Sciences, USA |url=http://www.pnas.org/cgi/content/abstract/84/12/4063?ijkey=e3c8d44826a7f44b3adcbd534f79a90522659f39&keytype2=tf_ipsecsha |accessdate= 2008-01-25 |doi=10.1073/pnas.84.12.4063 |pmid=3295876 |pmc=305022 }}</ref>
In 1984, he moved across the hall from Rosenberg's lab to start his own laboratory as an assistant professor in the department of genetics. He still collaborated with members of the Rosenberg laboratory, including Wayne Fenton. As an independent researcher, Horwich asked whether the pathway that imports an enzyme called [[ornithine transcarbamylase]] (OTC) into the [[mitochondria]] of mammalian cells also could work in yeast. In 1987, during a genetic screen in yeast, Horwich and his colleagues stumbled across a protein folding function inside [[mitochondria]]. In the mutant strain, proteins entered mitochondria from the [[cytosol]] normally but then misfolded and aggregated. They named the protein encoded by the affected gene [[HSP60]], Heat shock protein 60, because it has a mass of 60 kDa and is produced in larger quantity in response to heat. Hsp60 is found in an 850 kDa double ring assembly, each ring containing 7 copies of Hsp60. Such assemblies, known as chaperonins, also exist in other cellular compartments and are essential components, mediating protein folding under both heat shock and normal conditions.<ref>{{cite journal |author=Cheng, M.Y. |author2=Pollock, R.A. |author3=Hendrick, J. P. |author4=Horwich, A. L. |name-list-style=amp |date=June 15, 1987 |title=Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae |journal=PNAS |volume=84 |issue=12 |pages=4063–4067 |doi=10.1073/pnas.84.12.4063 |pmid=3295876 |pmc=305022 |bibcode=1987PNAS...84.4063C |doi-access=free }}</ref>


Since 1987, Horwich and his colleagues have been studying these molecules both in ''vivo'' and ''in vitro'', with particular emphasis on the Hsp60 homologue in ''E. coli'' known as GroEL. They and others found early on that a chaperonin-mediated folding reaction can be reconstituted in a test tube, and that has enabled structural and functional studies that have begun to explain how chaperonins work.
Since 1987, Horwich and his colleagues have been studying these molecules both in ''vivo'' and ''in vitro'', with particular emphasis on the Hsp60 homologue in ''E. coli'' known as GroEL. They and others found early on that a chaperonin-mediated folding reaction can be reconstituted in a test tube, and that has enabled structural and functional studies that have begun to explain how chaperonins work.


== Awards and honors ==
== Awards and honors ==
* 2001: Hans Neurath Award (Protein Society Award)<ref>{{cite web|url=http://www.proteinsociety.org/pages/page03b.htm |title=Past Recipients |access-date=February 1, 2008 |publisher=The Protein Society |url-status=dead |archive-url=https://web.archive.org/web/20080513115337/http://www.proteinsociety.org/pages/page03b.htm |archive-date=May 13, 2008 }}</ref>
* 2003: Elected to the [[United States National Academy of Sciences|National Academy of Sciences]].
* 2003: Elected to the [[United States National Academy of Sciences|National Academy of Sciences]].
* 2004: Received Gairdner International Award "for his fundamental discoveries concerning chaperone assisted protein folding in the cell and its relevance to neurodegeneration".<ref>{{cite web |url=http://www.gairdner.org/winners2004.html |title=2004 winners |accessdate=2008-01-24 |publisher=The Gairdner Foundation| archiveurl= http://web.archive.org/web/20071214073646/http://www.gairdner.org/winners2004.html| archivedate= 14 December 2007 <!--DASHBot-->| deadurl= no}}</ref>
* 2004: [[Canada Gairdner International Award]]<ref>{{cite web |url=http://www.gairdner.org/winners2004.html |title=2004 winners |access-date=January 24, 2008 |publisher=The Gairdner Foundation |archive-url=https://web.archive.org/web/20071214073646/http://www.gairdner.org/winners2004.html |archive-date=December 14, 2007 |url-status=dead }}</ref>
* 2006: Stein and Moore Award (Protein Society Award)<ref>{{cite web|url=http://www.proteinsociety.org/pages/page03b.htm |title=Past Recipients |access-date=February 1, 2008 |publisher=The Protein Society |url-status=dead |archive-url=https://web.archive.org/web/20080513115337/http://www.proteinsociety.org/pages/page03b.htm |archive-date=May 13, 2008 }}</ref>
* 2007: Received [[Wiley Prize]] in Biomedical Science jointly with [[Franz-Ulrich Hartl]], Managing Director of the [[Max Planck Institute of Biochemistry]], "for their significant contribution in protein folding."<ref>{{cite web |url=http://www.medicalnewstoday.com/articles/62018.php |title=Recipients Of 6th Annual Wiley Prize In Biomedical Sciences Announced By Wiley Foundation |accessdate=2008-01-24 |author= |date=2007-02-02 |work= |publisher=Medical News Today }}</ref>
* 2007: [[Wiley Prize]], awarded jointly with [[Franz-Ulrich Hartl]]<ref>{{cite web |url=http://www.medicalnewstoday.com/articles/62018.php |title=Recipients Of 6th Annual Wiley Prize In Biomedical Sciences Announced By Wiley Foundation |access-date=January 24, 2008 |date=February 2, 2007 |publisher=Medical News Today |archive-date=August 13, 2007 |archive-url=https://web.archive.org/web/20070813043539/http://www.medicalnewstoday.com/articles/62018.php |url-status=dead }}</ref>
* 2008: Received Lewis S. Rosenstiel Award for Distinguished Work in Basic Medical Science jointly with Franz-Ulrich Hartl "for their pioneering work in the field of protein-mediated protein folding."<ref>{{cite web |url=http://www.rose.brandeis.edu/Center/rose_current.html |title=Award Winners 2008 |accessdate=2008-02-01 |author= |date= |work= |publisher=Brandeis University}}</ref>
* 2008: [[Rosenstiel Award]], awarded jointly with Hartl<ref>{{cite web|url=http://www.rose.brandeis.edu/Center/rose_current.html |title=Award Winners 2008 |access-date=February 1, 2008 |publisher=Brandeis University |url-status=dead |archive-url=https://web.archive.org/web/20070820041803/http://www.rose.brandeis.edu/Center/rose_current.html |archive-date=August 20, 2007 }}</ref>
* 2008: Received the [[Louisa Gross Horwitz Prize]] for Biology or Biochemistry from [[Columbia University]], also with Hartl.
* 2008: [[Louisa Gross Horwitz Prize]] for Biology or Biochemistry, [[Columbia University]]; awarded jointly with Hartl<ref>[https://www.cuimc.columbia.edu/research/louisa-gross-horwitz-prize/horwitz-prize-awardees/2010-2001-awardees Louisa Gross Horwitz Prize 2008]</ref>
* 2011: Received the [[Massry Prize]] from the [[Keck School of Medicine]], [[University of Southern California]] and the [[Albert Lasker Award for Basic Medical Research]] jointly with Hartl "for discoveries concerning the cell's protein-folding machinery, exemplified by cage-like structures that convert newly made proteins into their biologically active forms."<ref>{{cite web |url=http://www.laskerfoundation.org/awards/2011_b_description.htm |title=2011 Lasker Award Description |accessdate=2011-09-12 |author= |date= |work= |publisher=The Lasker Foundation}}</ref>
* 2008: Elected to the [[National Academy of Medicine]]
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* 2014: Received an honorary Doctorate of Medical Science from [[Brown University]].<ref name="brownu">{{cite web|title=Brown confers nine honorary degrees|url=http://news.brown.edu/pressreleases/2014/05/hdcitations#Horwich|publisher=Brown University|accessdate=27 May 2014|date=25 May 2014}}</ref>
* 2011: [[Massry Prize]], [[Keck School of Medicine]], [[University of Southern California]]

He has also received two Protein Society awards - the Hans Neurath Award in 2001 and the Stein and Moore Award in 2006.<ref>{{cite web |url=http://www.proteinsociety.org/pages/page03b.htm |title=Past Recipients |accessdate=2008-02-01 |author= |date= |work= |publisher=The Protein Society }}</ref>
* 2011: [[Albert Lasker Award for Basic Medical Research]], awarded jointly with Hartl<ref>{{cite web |url=http://www.laskerfoundation.org/awards/2011_b_description.htm |title=2011 Lasker Award Description |access-date=September 12, 2011 |publisher=The Lasker Foundation}}</ref>
* 2012: [[Shaw Prize]], awarded jointly with Hartl
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* 2014: Honorary Doctorate of Medical Science, [[Brown University]].<ref name="brownu">{{cite web|title=Brown confers nine honorary degrees|url=http://news.brown.edu/pressreleases/2014/05/hdcitations#Horwich|publisher=Brown University|access-date=May 27, 2014|date=May 25, 2014}}</ref>
* 2016: [[Albany Medical Center Prize]]
* 2019: [[Paul Ehrlich and Ludwig Darmstaedter Prize]]
* 2019: [[Dr. Paul Janssen Award for Biomedical Research]], awarded jointly with Hartl<ref>{{Cite web|title=Dr. Paul Janssen Award|url=https://www.pauljanssenaward.com/|access-date=2022-02-11|website=Dr. Paul Janssen Award|language=en}}</ref>
* 2020: [[Breakthrough Prize in Life Sciences]]<ref>[https://breakthroughprize.org/News/54 Breakthrough Prize in Life Sciences 2020]</ref>
* 2021: Elected to the [[American Academy of Arts and Sciences]]
* 2022: [[Human Frontier Science Program]] Nakasone Award<ref>{{Cite web|last=Backman|first=Isabella|title=Nakasone Prize Won By Arthur Horwich, MD|url=https://medicine.yale.edu/news-article/nakasone-prize-won-by-arthur-horwich-md/|access-date=2022-02-11|website=medicine.yale.edu|language=en}}</ref>
* 2023: [[BBVA Foundation Frontiers of Knowledge Award]]<ref>[https://www.frontiersofknowledgeawards-fbbva.es/ BBVA Foundation Frontiers of Knowledge Award 2023]</ref>


== References ==
== References ==
{{Reflist|2}}
{{reflist}}


== External links ==
== External links ==
* [http://info.med.yale.edu/genetics/horwich/ Art Horwich Lab at Yale]
* [http://info.med.yale.edu/genetics/horwich/ Art Horwich Lab at Yale]
* [http://www.sciencewatch.com/interviews/arthur_horwich1.htm Interview with Arthur Horwich]
* [https://web.archive.org/web/20071117062139/http://www.sciencewatch.com/interviews/arthur_horwich1.htm Interview with Arthur Horwich]
* [http://www.hhmi.org/research/investigators/horwich.html Chaperonin-Mediated Protein Folding]
* [http://www.hhmi.org/research/investigators/horwich.html Chaperonin-Mediated Protein Folding]
*[http://www.ibiology.org/ibioseminars/cell-biology/arthur-horwich-part-1a.html Arthur Horwich Seminars: "Chaperone-Assisted Protein Folding"]
*[https://www.ibiology.org/cell-biology/chaperone/ Arthur Horwich Seminars: "Chaperone-Assisted Protein Folding"]


{{Shaw Prize laureates}}
{{Shaw Prize laureates}}
{{E.B. Wilson Medal recipients}}


{{Authority control}}
{{Authority control}}

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[[Category:Massry Prize recipients]]
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[[Category:Alpert Medical School alumni]]
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[[Category:21st-century American biologists]]
[[Category:Members of the National Academy of Medicine]]

Latest revision as of 11:44, 4 February 2024

Arthur L. Horwich
Born1951 (age 72–73)
NationalityAmerican
Alma materBrown University
Known foruncovering chaperonin action
Awards
Scientific career
FieldsBiology
Institutions
Notable studentsTapan K. Chaudhuri[1]

Arthur L. Horwich (born 1951) is an American biologist and Sterling Professor of Genetics and Pediatrics at the Yale School of Medicine.[2][3] Horwich has also been a Howard Hughes Medical Institute investigator since 1990.[4] His research into protein folding uncovered the action of chaperonins, protein complexes that assist the folding of other proteins; Horwich first published this work in 1989.[5][6]

For his scientific work Horwich has been awarded the Gairdner International Award (2004), Louisa Gross Horwitz Prize (2008), Lasker Award (2011),[7] Shaw Prize (2012), Albany Medical Center Prize (2016), and Breakthrough Prize (2020). He is a member of the National Academy of Sciences and the American Academy of Arts and Sciences.[8][9]

Early years

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Horwich was born in 1951. He grew up in Oak Park, west of Chicago.[10] In 1969, he entered Brown University as part of a new program that combined the undergraduate degree with medical school.[10] During medical school, Horwich studied fat cell metabolism in the laboratory of John Fain. Horwich received his A.B. in biomedical sciences in 1972 and his M.D. in 1975.[2][4] He graduated as valedictorian of the first class to complete the combined program.[10] Horwich went on to do an internship and residency in pediatrics at Yale University. Midway through, Horwich was not sure about an entirely clinical future. After completing his residency, he joined the Salk Institute for Biological Studies in La Jolla, California for a postdoctoral position in molecular biology and virology.[10] At Salk, he worked in Walter Eckhart's laboratory alongside Tony Hunter and witnessed Hunter's discovery of tyrosine phosphorylation.[10] He credits this time with sharpening his skills as a scientist. He said, "Tony taught me the nuts and bolts of thinking about a problem."[10]

Research

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In 1981, Horwich moved back to New Haven, Connecticut for a postdoctoral fellowship at Yale University School of Medicine. He worked in the laboratory of Leon Rosenberg.[11]

In 1984, he moved across the hall from Rosenberg's lab to start his own laboratory as an assistant professor in the department of genetics. He still collaborated with members of the Rosenberg laboratory, including Wayne Fenton. As an independent researcher, Horwich asked whether the pathway that imports an enzyme called ornithine transcarbamylase (OTC) into the mitochondria of mammalian cells also could work in yeast. In 1987, during a genetic screen in yeast, Horwich and his colleagues stumbled across a protein folding function inside mitochondria. In the mutant strain, proteins entered mitochondria from the cytosol normally but then misfolded and aggregated. They named the protein encoded by the affected gene HSP60, Heat shock protein 60, because it has a mass of 60 kDa and is produced in larger quantity in response to heat. Hsp60 is found in an 850 kDa double ring assembly, each ring containing 7 copies of Hsp60. Such assemblies, known as chaperonins, also exist in other cellular compartments and are essential components, mediating protein folding under both heat shock and normal conditions.[12]

Since 1987, Horwich and his colleagues have been studying these molecules both in vivo and in vitro, with particular emphasis on the Hsp60 homologue in E. coli known as GroEL. They and others found early on that a chaperonin-mediated folding reaction can be reconstituted in a test tube, and that has enabled structural and functional studies that have begun to explain how chaperonins work.

Awards and honors

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References

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  1. ^ "Tapan K. Chahudhuri- Chaperone Mediated Protein Folding, Protein Engineering and Molecular Biophysics Group".
  2. ^ a b "Arthur L. Horwich". Yale School of Medicine. Archived from the original on May 30, 2008. Retrieved March 18, 2008.
  3. ^ "Form leads to function". Yale School of Medicine. Archived from the original on May 21, 2008. Retrieved January 24, 2008.
  4. ^ a b "Arthur L. Horwich, M.D". Howard Hughes Medical Institute. Retrieved January 24, 2008.
  5. ^ Cheng, M.Y.; Hartl, F.U.; Martin, J.; Pollock, R. A.; Kalousek, F.; Neupert, W.; Hallberg, E. M.; Hallberg, R. L. & Horwich, A. L. (February 16, 1989). "Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria". Nature. 337 (6208): 620–625. Bibcode:1989Natur.337..620C. doi:10.1038/337620a0. PMID 2645524. S2CID 4333381.
  6. ^ Wang, Shirley S. (2009-09-14). "The Nobel Prize Will Go To..." Wall Street Journal. ISSN 0099-9660. Retrieved 2022-02-11.
  7. ^ Zimmer, Carl (2011-09-12). "Horwich Wins Lasker Award by Straddling Science and Medicine". The New York Times. ISSN 0362-4331. Retrieved 2022-02-11.
  8. ^ Davis, Tinsley H. (2004-10-19). "Biography of Arthur L. Horwich". Proceedings of the National Academy of Sciences. 101 (42): 15002–15004. doi:10.1073/pnas.0406924101. ISSN 0027-8424. PMC 524080. PMID 15479759.
  9. ^ Hahamy, Madison (2021-05-04). "14 Yale faculty recently elected to the American Academy of Arts & Sciences". Yale Daily News. Retrieved 2022-02-11.
  10. ^ a b c d e f Tinsley H. Davis (2004). "Biography of Arthur L. Horwich". Proceedings of the National Academy of Sciences. 101 (42): 15002–15004. doi:10.1073/pnas.0406924101. PMC 524080. PMID 15479759.
  11. ^ "Horwich is Higgins Professor of Cellular, Molecular Physiology". Yale
  12. ^ Cheng, M.Y.; Pollock, R.A.; Hendrick, J. P. & Horwich, A. L. (June 15, 1987). "Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae". PNAS. 84 (12): 4063–4067. Bibcode:1987PNAS...84.4063C. doi:10.1073/pnas.84.12.4063. PMC 305022. PMID 3295876.
  13. ^ "Past Recipients". The Protein Society. Archived from the original on May 13, 2008. Retrieved February 1, 2008.
  14. ^ "2004 winners". The Gairdner Foundation. Archived from the original on December 14, 2007. Retrieved January 24, 2008.
  15. ^ "Past Recipients". The Protein Society. Archived from the original on May 13, 2008. Retrieved February 1, 2008.
  16. ^ "Recipients Of 6th Annual Wiley Prize In Biomedical Sciences Announced By Wiley Foundation". Medical News Today. February 2, 2007. Archived from the original on August 13, 2007. Retrieved January 24, 2008.
  17. ^ "Award Winners 2008". Brandeis University. Archived from the original on August 20, 2007. Retrieved February 1, 2008.
  18. ^ Louisa Gross Horwitz Prize 2008
  19. ^ "2011 Lasker Award Description". The Lasker Foundation. Retrieved September 12, 2011.
  20. ^ "Brown confers nine honorary degrees". Brown University. May 25, 2014. Retrieved May 27, 2014.
  21. ^ "Dr. Paul Janssen Award". Dr. Paul Janssen Award. Retrieved 2022-02-11.
  22. ^ Breakthrough Prize in Life Sciences 2020
  23. ^ Backman, Isabella. "Nakasone Prize Won By Arthur Horwich, MD". medicine.yale.edu. Retrieved 2022-02-11.
  24. ^ BBVA Foundation Frontiers of Knowledge Award 2023
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