Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Kevin C Stein"'
Autor:
Kevin C Stein, Heather L True
Publikováno v:
PLoS Pathogens, Vol 10, Iss 9, p e1004328 (2014)
Externí odkaz:
https://doaj.org/article/da021ee868fb487898403e678fc64700
Autor:
Kevin C Stein, Heather L True
Publikováno v:
PLoS Genetics, Vol 10, Iss 5, p e1004337 (2014)
Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of forming several distinct self-templating conformers. In prion diseases, these different structures, called prion strains (or variants), confer dramatic va
Externí odkaz:
https://doaj.org/article/4ed89be211c245d1ab6bca0bc7f81b76
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e87521 (2014)
Molecular chaperones play a significant role in preventing protein misfolding and aggregation. Indeed, some protein conformational disorders have been linked to changes in the chaperone network. Curiously, in yeast, chaperones also play a role in pro
Externí odkaz:
https://doaj.org/article/a6a99c2902a34874be2bf2f14eb63642
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e79582 (2013)
Prion strains (or variants) are structurally distinct amyloid conformations arising from a single polypeptide sequence. The existence of prion strains has been well documented in mammalian prion diseases. In many cases, prion strains manifest as vari
Externí odkaz:
https://doaj.org/article/21cf5e980e70475185b3bd81553e86ee
Autor:
Judith Frydman, Kevin C. Stein
Publikováno v:
Journal of Biological Chemistry. 294:2076-2084
Generating a functional proteome requires the ribosome to carefully regulate disparate co-translational processes that determine the fate of nascent polypeptides. With protein synthesis being energetically expensive, the ribosome must balance the cos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d237dfd113d8cbb0f07925068e80fe95
https://doi.org/10.1074/jbc.rev118.002814
https://doi.org/10.1074/jbc.rev118.002814
Autor:
Carina Groh, Kevin C. Stein, Johannes M. Herrmann, L. Kraemer, K. Knoeringer, Felix Boos, K. G. Hansen, Judith Frydman
Almost all mitochondrial proteins are synthesized in the cytosol and subsequently targeted to mitochondria. The accumulation of non-imported precursor proteins occurring upon mitochondrial dysfunction can challenge cellular protein homeostasis. Here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c80c980ab48eebcdda8be7c0eabbb6b4
https://doi.org/10.1101/2021.05.19.444788
https://doi.org/10.1101/2021.05.19.444788
Autor:
Ankan K. Bhadra, Hao Shao, Kevin C. Stein, Sara K. Pittman, Rocio Bengoechea, Jil A. Wright Daw, Heather L. True, Conrad C. Weihl, Andrew R. Findlay, Jason E. Gestwicki
Publikováno v:
J Clin Invest
The Journal of clinical investigation, vol 130, iss 8
The Journal of clinical investigation, vol 130, iss 8
Dominant mutations in the HSP70 co-chaperone DNAJB6 cause a late onset muscle disease termed limb girdle muscular dystrophy type 1D (LGMD1D), which is characterized by protein aggregation and vacuolar myopathology. Disease mutations reside within the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::beb16b18d69eebb54fb9420377ac5b66
https://pubmed.ncbi.nlm.nih.gov/32427588
https://pubmed.ncbi.nlm.nih.gov/32427588
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed. Cross-seeding, where one aggregated protein templates the misfolding of a he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::891092de67396725b04f794c4ee5605b
https://doi.org/10.1038/s41598-017-05829-5
https://doi.org/10.1038/s41598-017-05829-5
Publikováno v:
Journal of Biological Chemistry. 289:21120-21130
The molecular chaperone network protects against the toxic misfolding and aggregation of proteins. Disruption of this network leads to a variety of protein conformational disorders. One such example recently discovered is limb-girdle muscular dystrop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa19de3d85d71470ec4f87b2564d8e1a
https://doi.org/10.1074/jbc.m114.572461
https://doi.org/10.1074/jbc.m114.572461
Publikováno v:
Mol Cell
Summary Cotranslational protein folding requires assistance from elaborate ribosome-associated chaperone networks. It remains unclear how the changing information in a growing nascent polypeptide dictates the recruitment of functionally distinct chap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c63954975f5c913a025c9f52cc16804f
https://doi.org/10.1016/j.molcel.2019.06.036
https://doi.org/10.1016/j.molcel.2019.06.036