Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Amirthaa Suntharalingam"'
Autor:
Jeremy D Baker, Lindsey B Shelton, Dali Zheng, Filippo Favretto, Bryce A Nordhues, April Darling, Leia E Sullivan, Zheying Sun, Parth K Solanki, Mackenzie D Martin, Amirthaa Suntharalingam, Jonathan J Sabbagh, Stefan Becker, Eckhard Mandelkow, Vladimir N Uversky, Markus Zweckstetter, Chad A Dickey, John Koren, Laura J Blair
Publikováno v:
PLoS Biology, Vol 15, Iss 6, p e2001336 (2017)
The accumulation of amyloidogenic proteins is a pathological hallmark of neurodegenerative disorders. The aberrant accumulation of the microtubule associating protein tau (MAPT, tau) into toxic oligomers and amyloid deposits is a primary pathology in
Externí odkaz:
https://doaj.org/article/b8e1004e37a14f80868d70e4b48f50e7
Autor:
Anthony Hazel, Chad A. Dickey, Mackenzie D. Martin, Shannon E. Hill, Raquel L. Lieberman, James C. Gumbart, Michelle S. Kwon, Amirthaa Suntharalingam
Publikováno v:
J Biol Chem
Nonsynonymous gene mutations can be beneficial, neutral, or detrimental to the stability, structure, and biological function of the encoded protein, but the effects of these mutations are often not readily predictable. For example, the β-propeller o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29e922b7332b16dc2b6886daa6548341
https://doi.org/10.1074/jbc.ra119.009419
https://doi.org/10.1074/jbc.ra119.009419
Autor:
Dustin J. E. Huard, John Koren, Laura J. Blair, Jack M. Webster, Bryce A. Nordhues, Christopher L. Passaglia, Brian S. J. Blagg, Vincent M. Crowley, Raquel L. Lieberman, Andrew R. Stothert, Xiaolan Tang, Amirthaa Suntharalingam, Sanket J. Mishra, Chad A. Dickey
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
The heat shock protein 90 (Hsp90) family of molecular chaperones regulates protein homeostasis, folding, and degradation. The ER-resident Hsp90 isoform, glucose-regulated protein 94 (Grp94), promotes the aggregation of mutant forms of myocilin, a pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adec88378146352dcc630329f482d810
https://doi.org/10.1038/s41598-017-18344-4
https://doi.org/10.1038/s41598-017-18344-4
Autor:
Chad A. Dickey, Laura J. Blair, Markus Zweckstetter, Jeremy D. Baker, Dali Zheng, Stefan Becker, Leia E. Sullivan, Parth K. Solanki, Zheying Sun, Filippo Favretto, April L. Darling, Vladimir N. Uversky, Jonathan J. Sabbagh, Eckhard Mandelkow, Mackenzie D. Martin, Lindsey B. Shelton, John Koren, Amirthaa Suntharalingam, Bryce A. Nordhues
Publikováno v:
PLoS Biology
PLoS Biology, Vol 15, Iss 6, p e2001336 (2017)
PLoS biology 15(6), e2001336 (2017). doi:10.1371/journal.pbio.2001336
PLoS Biology, Vol 15, Iss 6, p e2001336 (2017)
PLoS biology 15(6), e2001336 (2017). doi:10.1371/journal.pbio.2001336
The accumulation of amyloidogenic proteins is a pathological hallmark of neurodegenerative disorders. The aberrant accumulation of the microtubule associating protein tau (MAPT, tau) into toxic oligomers and amyloid deposits is a primary pathology in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68f6b2bd08582824ce677c0cf860aa60
https://hdl.handle.net/21.11116/0000-0001-7953-A
https://hdl.handle.net/21.11116/0000-0001-7953-A
Autor:
Dustin J. E. Huard, Sarah N. Fontaine, Amirthaa Suntharalingam, Andrew R. Stothert, Brian S. J. Blagg, Raquel L. Lieberman, Sanket J. Mishra, Vincent M. Crowley, Chad A. Dickey
Publikováno v:
Human Molecular Genetics. 23:6470-6480
Gain-of-function mutations in the olfactomedin domain of the MYOC gene facilitate the toxic accumulation of amyloid-containing myocilin aggregates, hastening the onset of the prevalent ocular disorder primary open-angle glaucoma. Aggregation of wild-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0820ac904af2b35c2d53984f9ab27846
https://doi.org/10.1093/hmg/ddu367
https://doi.org/10.1093/hmg/ddu367
Autor:
Timothy A.J. Haystead, Lindsey B. Shelton, Jeremy D. Baker, Chad A. Dickey, Mackenzie D. Martin, Jonathan J. Sabbagh, Jason E. Gestwicki, Bryce A. Nordhues, Dali Zheng, Amirthaa Suntharalingam
Publikováno v:
ACS chemical biology. 11(7)
Three scaffolds with inhibitory activity against the heat shock protein 70 (Hsp70) family of chaperones have been found to enhance the degradation of the microtubule associated protein tau in cells, neurons, and brain tissue. This is important becaus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f799790d9880cb5e6b51355f4e762c1
https://pubmed.ncbi.nlm.nih.gov/27177119
https://pubmed.ncbi.nlm.nih.gov/27177119
Autor:
Umesh K. Jinwal, Amirthaa Suntharalingam, Karthik Arulselvam, Sarah Brady, Matthew Cockman, Ying Jin, Jose F. Abisambra, Chad A. Dickey, Bo Zhang
Publikováno v:
Journal of Molecular Biology. 421:653-661
Tau aggregation and amyloidogenesis are common hallmarks for neurodegenerative disorders called tauopathies. The molecular chaperone network constitutes the cellular defense against insults such as tau aggregation. However, chaperone effects on tau a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b6a53e87f0832e4d29d7d3986331e29
https://doi.org/10.1016/j.jmb.2012.02.003
https://doi.org/10.1016/j.jmb.2012.02.003
Autor:
John Koren, Brian S. J. Blagg, Matthew Cockman, Shannon E. Hill, Umesh K. Jinwal, Laura J. Blair, Jose F. Abisambra, Adam S. Duerfeldt, Myung Kuk Joe, Bo Zhang, Stanislav I. Tomarev, John C. O'Leary, Amirthaa Suntharalingam, Raquel L. Lieberman, Chad A. Dickey
Publikováno v:
The Journal of biological chemistry. 287(48)
Mutant myocilin accumulates in the endoplasmic reticulum for unknown reasons.Glucose-regulated protein (Grp) 94 depletion reduces mutant myocilin by engaging autophagy.Grp94 triages mutant myocilin through ER-associated degradation, subverting autoph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d040ca7d581454c4c1b2be589b44a765
https://pubmed.ncbi.nlm.nih.gov/23035116
https://pubmed.ncbi.nlm.nih.gov/23035116