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个人简介
Life demands that proteins fold into elaborate structures to perform the overwhelming majority of biological functions. We investigate how components of the proteostasis (protein homeostasis) network enable cells to achieve successful protein folding. In particular, we seek to understand how cells prevent, reverse, or even promote the formation of diverse misfolded conformers, encompassing: prions, amyloids, fibrillar structures, amorphous aggregates and toxic soluble oligomers.
Amyloid fibers are self-templating protein conformers. They self-replicate their specific ‘cross-β’ conformation at their growing ends, by converting other copies of the same protein to the ‘cross-β’ amyloid form. When amyloid fibers grow and divide with high efficiency they can be infectious, and are then termed prions (Cushman et al., 2010; Shorter & Lindquist, 2005; Shorter, 2010). Cells have evolved a sophisticated machinery to alleviate such aberrant protein aggregation. For example, protein disaggregases resolve protein aggregates, molecular chaperones prevent protein aggregation, osmolytes act as chemical chaperones, and degradation systems eliminate misfolded proteins (Shorter, 2008; Vashist et al. 2010).
Amyloid fibers are self-templating protein conformers. They self-replicate their specific ‘cross-β’ conformation at their growing ends, by converting other copies of the same protein to the ‘cross-β’ amyloid form. When amyloid fibers grow and divide with high efficiency they can be infectious, and are then termed prions (Cushman et al., 2010; Shorter & Lindquist, 2005; Shorter, 2010). Cells have evolved a sophisticated machinery to alleviate such aberrant protein aggregation. For example, protein disaggregases resolve protein aggregates, molecular chaperones prevent protein aggregation, osmolytes act as chemical chaperones, and degradation systems eliminate misfolded proteins (Shorter, 2008; Vashist et al. 2010).
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Edward Chuang,Ryan R. Cupo, Jeffrey R. Bevan,Mikhaila L. Rice,Shuli Mao, Erica L. Gorenberg,Korrie L. Mack,Donna M. Huryn,Peter Wipf,Jeffrey L. Brodsky,James Shorter
biorxiv(2024)
Sonia Vazquez-Sanchez, Britt Tilkin,Fatima Gasset-Rosa, Sitao Zhang,Diana Piol,Melissa McAlonis-Downes,Jonathan Artates, Noe Govea-Perez, Yana Verresen,Lin Guo,Don W. Cleveland,James Shorter,Sandrine Da Cruz
Katelyn M Sweeney, Sapanna Chantarawong,Edward M Barbieri, Greg Cajka,Matthew Liu,Lynn Spruce,Hossein Fazelinia,Bede Portz,Katie Copley, Tomer Lapidot,Lauren Duhamel, Phoebe Greenwald,Naseeb Saida,Reut Shalgi,James Shorter,Ophir Shalem
PLoS geneticsno. 2 (2024): e1011138-e1011138
Linamarie Miller,James Shorter
CELL CHEMICAL BIOLOGYno. 1 (2024): 14-16
ISRAEL JOURNAL OF CHEMISTRY (2024)
Molecular Neurodegenerationno. 1 (2024): 1-29
crossref(2024)
Chemical reviews (2023)
Kartikay Sharma,Sambhasan Banerjee,Dilan Savran, Cedric Rajes,Sebastian Wiese,Amandeep Girdhar,Nadine Schwierz, Christopher Lee,James Shorter,Matthias Schmidt,Lin Guo,Marcus Faendrich
JOURNAL OF MOLECULAR BIOLOGYno. 18 (2023)
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作者统计
#Papers: 270
#Citation: 21651
H-Index: 72
G-Index: 146
Sociability: 7
Diversity: 0
Activity: 2
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