Arthur L. Horwich
Affiliations: | Genetics and Pediatrics | Yale University, New Haven, CT |
Area:
chaperoninsWebsite:
http://medicine.yale.edu/labs/horwich/www/Google:
"Arthur Horwich"Bio:
http://www.nasonline.org/member-directory/members/2540934.html
http://news.yale.edu/2011/09/12/yales-horwich-wins-lasker-award-one-sciences-top-honors
Mean distance: 18.33 (cluster 31)
Cross-listing: Neurotree
Children
Sign in to add trainee| Yuyu Song | post-doc | Yale (Neurotree) | |
| Jiou Wang | post-doc | Yale (Neurotree) | |
| Jonathan S. Weissman | post-doc | Yale | |
| Hays S. Rye | post-doc | 1995-2000 | Yale University Medical School |
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Publications
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| Horwich AL, Fenton WA. (2020) Chaperonin-assisted protein folding: a chronologue. Quarterly Reviews of Biophysics. 53: e4 |
| Natesh R, Clare DK, Farr GW, et al. (2018) A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin. International Journal of Biological Macromolecules |
| Nagy M, Fenton WA, Li D, et al. (2016) Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110. Proceedings of the National Academy of Sciences of the United States of America |
| Ambrose AJ, Fenton W, Mason DJ, et al. (2015) Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system. Febs Letters. 589: 497-9 |
| Horwich AL. (2014) Molecular chaperones in cellular protein folding: the birth of a field. Cell. 157: 285-8 |
| Horwich AL. (2013) Chaperonin-mediated protein folding. The Journal of Biological Chemistry. 288: 23622-32 |
| Song Y, Nagy M, Ni W, et al. (2013) Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm. Proceedings of the National Academy of Sciences of the United States of America. 110: 5428-33 |
| Bilguvar K, Tyagi NK, Ozkara C, et al. (2013) Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration. Proceedings of the National Academy of Sciences of the United States of America. 110: 3489-94 |
| Saibil HR, Fenton WA, Clare DK, et al. (2013) Structure and allostery of the chaperonin GroEL. Journal of Molecular Biology. 425: 1476-87 |
| Clare DK, Vasishtan D, Stagg S, et al. (2012) ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Cell. 149: 113-23 |