词条 | Andrew P. Carter |
释义 |
| name = Andrew P Carter | native_name = | native_name_lang = | image = AndrewCarter wikki 2018.jpg | image_size = | alt = | caption = | birth_date = | residence = | citizenship = | nationality = British | fields = {{Plainlist|
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| doctoral_advisor = Venki Ramakrishnan | academic_advisors = Ron Vale | known_for = | awards = EMBO Member (2016) | website = {{URL|https://www2.mrc-lmb.cam.ac.uk/groups/cartera/}} | footnotes = | honorific_suffix = | education = }}Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.[1][2][3][4] EducationCarter studied Biochemistry at the University of Oxford, graduating in 1999.[5] He obtained a PhD in 2003 from the MRC Laboratory of Molecular Biology where he worked with Venki Ramakrishnan on the ribosome. He was a member of the team in Ramakrishnan's lab that solved the first X-ray crystal structure of the small (30S) ribosomal subunit.[6] Carter also determined structures of 30S bound to antibiotics[7] and bound to the initiation factor IF1.[8] Ramakrishnan shared the Nobel prize in Chemistry for the team's work on the 30S.[9] Career and researchCarter was a post-doc in Ron Vale's lab[10] at University of California, San Francisco from 2003 to 2010. During his post-doc, he studied the molecular motor protein, dynein using X-ray crystallography and single molecule fluorescence microscopy.[11][12] He became a group leader at MRC Laboratory of Molecular Biology in Cambridge in 2010 where he uses X-ray crystallography, electron microscopy, and single molecule microscopy assays to understand how dynein transports cargo. His group solved X-ray crystal structures of the dynein motor domain showing how it generates force to pull cargos along microtubules[1] and reconstituted a recombinant dynein, showing how its processive movement is activated by cofactors/cargo adaptors.[13] His group used cryoEM to solve the structure of dynein's cofactor dynactin[2] and the full length dynein complex.[3] They showed how dynein and dynactin come together in the presence of cargos and how this activates transport. Grants, awards and honours
References1. ^1 {{Cite journal|last=Schmidt|first=Helgo|last2=Zalyte|first2=Ruta|last3=Urnavicius|first3=Linas|last4=Carter|first4=Andrew P.|date=2015-02-19|title=Structure of human cytoplasmic dynein-2 primed for its power stroke|journal=Nature|volume=518|issue=7539|pages=435–438|doi=10.1038/nature14023|issn=1476-4687|pmc=4336856|pmid=25470043}} {{authority control}}{{DEFAULTSORT:Carter, Andrew P.}}2. ^1 {{Cite journal|last=Urnavicius|first=Linas|last2=Zhang|first2=Kai|last3=Diamant|first3=Aristides G.|last4=Motz|first4=Carina|last5=Schlager|first5=Max A.|last6=Yu|first6=Minmin|last7=Patel|first7=Nisha A.|last8=Robinson|first8=Carol V.|last9=Carter|first9=Andrew P.|date=2015-03-27|title=The structure of the dynactin complex and its interaction with dynein|journal=Science|volume=347|issue=6229|pages=1441–1446|doi=10.1126/science.aaa4080|issn=1095-9203|pmc=4413427|pmid=25814576}} 3. ^1 {{Cite journal|last=Zhang|first=Kai|last2=Foster|first2=Helen E.|last3=Rondelet|first3=Arnaud|last4=Lacey|first4=Samuel E.|last5=Bahi-Buisson|first5=Nadia|last6=Bird|first6=Alexander W.|last7=Carter|first7=Andrew P.|date=2017-06-15|title=Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated|journal=Cell|volume=169|issue=7|pages=1303–1314.e18|doi=10.1016/j.cell.2017.05.025|issn=1097-4172|pmc=5473941|pmid=28602352}} 4. ^{{Cite journal|last=Urnavicius|first=Linas|last2=Lau|first2=Clinton K.|last3=Elshenawy|first3=Mohamed M.|last4=Morales-Rios|first4=Edgar|last5=Motz|first5=Carina|last6=Yildiz|first6=Ahmet|last7=Carter|first7=Andrew P.|date=2018-02-07|title=Cryo-EM shows how dynactin recruits two dyneins for faster movement|journal=Nature|volume=554|issue=7691|pages=202–206|doi=10.1038/nature25462|issn=1476-4687|pmc=5988349|pmid=29420470}} 5. ^{{Cite web|url=http://www.bioch.ox.ac.uk/about/archives2012/2012-alumni-lecture-celebrating-oxford-biochemistry-graduate-success|title=2012 Alumni Lecture celebrating Oxford Biochemistry graduate success Page - Department of Biochemistry, University of Oxford|website=www.bioch.ox.ac.uk|access-date=2018-08-26}} 6. ^{{Cite journal|last=Wimberly|first=B. T.|last2=Brodersen|first2=D. E.|last3=Clemons|first3=W. M.|last4=Morgan-Warren|first4=R. J.|last5=Carter|first5=A. P.|last6=Vonrhein|first6=C.|last7=Hartsch|first7=T.|last8=Ramakrishnan|first8=V.|date=2000-09-21|title=Structure of the 30S ribosomal subunit|journal=Nature|volume=407|issue=6802|pages=327–339|doi=10.1038/35030006|issn=0028-0836|pmid=11014182}} 7. ^{{Cite journal|last=Carter|first=A. P.|last2=Clemons|first2=W. M.|last3=Brodersen|first3=D. E.|last4=Morgan-Warren|first4=R. J.|last5=Wimberly|first5=B. T.|last6=Ramakrishnan|first6=V.|date=2000-09-21|title=Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics|journal=Nature|volume=407|issue=6802|pages=340–348|doi=10.1038/35030019|issn=0028-0836|pmid=11014183}} 8. ^{{Cite journal|last=Carter|first=A. P.|last2=Clemons|first2=W. M.|last3=Brodersen|first3=D. E.|last4=Morgan-Warren|first4=R. J.|last5=Hartsch|first5=T.|last6=Wimberly|first6=B. 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R.|date=2008-12-12|title=Structure and functional role of dynein's microtubule-binding domain|journal=Science|volume=322|issue=5908|pages=1691–1695|doi=10.1126/science.1164424|issn=1095-9203|pmc=2663340|pmid=19074350}} 12. ^{{Cite journal|last=Carter|first=Andrew P.|last2=Cho|first2=Carol|last3=Jin|first3=Lan|last4=Vale|first4=Ronald D.|date=2011-03-04|title=Crystal structure of the dynein motor domain|journal=Science|volume=331|issue=6021|pages=1159–1165|doi=10.1126/science.1202393|issn=1095-9203|pmc=3169322|pmid=21330489}} 13. ^{{Cite journal|last=Schlager|first=Max A.|last2=Hoang|first2=Ha Thi|last3=Urnavicius|first3=Linas|last4=Bullock|first4=Simon L.|last5=Carter|first5=Andrew P.|date=2014-09-01|title=In vitro reconstitution of a highly processive recombinant human dynein complex|journal=The EMBO Journal|volume=33|issue=17|pages=1855–1868|doi=10.15252/embj.201488792|issn=1460-2075|pmc=4158905|pmid=24986880}} 14. ^{{Cite news|url=https://www2.mrc-lmb.cam.ac.uk/students/lmb-student-prize/|title=LMB Student Prize - MRC Laboratory of Molecular Biology|work=MRC Laboratory of Molecular Biology|access-date=2018-08-26|language=en-GB}} 15. ^{{Cite web|url=https://agi.org/structural-biology/fellowships/|title=Agouron Institute {{!}} Fellowships|website=agi.org|language=en-US|access-date=2018-08-26}} 16. ^{{Cite web|url=http://www.clare.cam.ac.uk/Fellows-and-Staff-Directory/apc48/|title=Dr Andrew Carter - Clare College Cambridge|last=Cambridge|first=Clare College|website=www.clare.cam.ac.uk|language=en|access-date=2018-08-25}} 17. ^{{Cite news|url=http://www.embo.org/news/press-releases/2012/22-young-group-leaders-recognized-as-embo-young-investigators|title=22 young group leaders recognized as EMBO Young Investigators|last=adit|work=EMBO|access-date=2018-08-26|language=en-gb}} 18. ^1 {{Cite web|url=https://wellcome.ac.uk/what-we-do/directories/investigator-awards-science-people-funded|title=Investigator Awards in Science: people we've funded {{!}} Wellcome|website=wellcome.ac.uk|language=en|access-date=2018-08-26}} 19. ^{{Cite web|url=https://people.embo.org/profile/andrew-p-carter|title=Find people in the EMBO Communities|website=people.embo.org|language=en|access-date=2018-08-26}} 20. ^{{Cite news|url=http://www.embo.org/news/press-releases/2016/58-life-science-researchers-elected-as-new-embo-members|title=58 life science researchers elected as new EMBO Members|last=User|first=Super|work=EMBO|access-date=2018-08-26|language=en-gb}} 6 : Structural biologists|Alumni of the University of Oxford|University of California, San Francisco faculty|Year of birth missing (living people)|Living people|21st-century British biologists |
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