Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Miguel Betegon"'
Autor:
Rebecca Freilich, Miguel Betegon, Eric Tse, Sue-Ann Mok, Olivier Julien, David A. Agard, Daniel R. Southworth, Koh Takeuchi, Jason E. Gestwicki
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Small heat shock proteins (sHSPs) limit the aggregation of proteins, such as tau. Here the authors show that Hsp27 recognizes two aggregation-prone regions of tau and that this interaction competes with Hsp27 oligomerization.
Externí odkaz:
https://doaj.org/article/ea828c6ee26840cd8de08621cb5f0b7d
Autor:
Daniel Elnatan, Miguel Betegon, Yanxin Liu, Theresa Ramelot, Michael A Kennedy, David A Agard
Publikováno v:
eLife, Vol 6 (2017)
Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate ‘client’ proteins, facilitating their folding and activating them for biological function. Despite decades of research, the mechanism connecting ATP hydrolysis a
Externí odkaz:
https://doaj.org/article/dec2959eea6d4b2abe575a0f8f110a03
Publikováno v:
eLife, Vol 3 (2014)
The characterization of the transcriptome and proteome of Plasmodium falciparum has been a tremendous resource for the understanding of the molecular physiology of this parasite. However, the translational dynamics that link steady-state mRNA with pr
Externí odkaz:
https://doaj.org/article/02a38a5b848d401cb6119495dd72d2c9
Autor:
Alexander L. Greninger, Giselle M. Knudsen, Miguel Betegon, Alma L. Burlingame, Joseph L. DeRisi
Publikováno v:
mBio, Vol 4, Iss 2 (2013)
ABSTRACT Despite wide sequence divergence, multiple picornaviruses use the Golgi adaptor acyl coenzyme A (acyl-CoA) binding domain protein 3 (ACBD3/GCP60) to recruit phosphatidylinositol 4-kinase class III beta (PI4KIIIβ/PI4KB), a factor required fo
Externí odkaz:
https://doaj.org/article/c7d541f3a3864218b34980e79249e6dc
Autor:
Miguel Betegon, Jeffrey L. Brodsky
Publikováno v:
Nat Cell Biol
Misfolded proteins in the endoplasmic reticulum (ER) are returned to the cytosol and destroyed by a process known as ER-associated degradation (ERAD). Hrd1 has been implicated as the channel that mediates the transport of ERAD substrates to the cytos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::528d9076469aa75f5a2bdd80477a834e
https://europepmc.org/articles/PMC7199279/
https://europepmc.org/articles/PMC7199279/
Autor:
David Bulkley, Yifan Cheng, Sam Li, Eugene Palovcak, Zanlin Yu, Shawn Q. Zheng, David A. Agard, Feng Wang, Miguel Betegon
Publikováno v:
Journal of structural biology, vol 204, iss 1
Graphene oxide (GO) sheets have been used successfully as a supporting substrate film in several recent cryogenic electron-microscopy (cryo-EM) studies of challenging biological macromolecules. However, difficulties in preparing GO-covered holey carb
Autor:
Jianhua Zhao, Sam Li, David A. Agard, Melody G. Campbell, Tural Aksel, Shawn M. Douglas, Feng Wang, Yifan Cheng, Miguel Betegon, Zanlin Yu
Publikováno v:
J Struct Biol
Journal of structural biology, vol 209, iss 2
Journal of structural biology, vol 209, iss 2
Cryo-EM samples prepared using the traditional methods often suffer from too few particles, poor particle distribution, or strongly biased orientation, or damage from the air-water interface. Here we report that functionalization of graphene oxide (G
Autor:
Eric Tse, Sue-Ann Mok, Jason E. Gestwicki, David A. Agard, Rebecca Freilich, Koh Takeuchi, Daniel R. Southworth, Olivier Julien, Miguel Betegon
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Nature communications, vol 9, iss 1
Nature Communications
Nature communications, vol 9, iss 1
Small heat shock proteins (sHSPs) are a class of oligomeric molecular chaperones that limit protein aggregation. However, it is often not clear where sHSPs bind on their client proteins or how these protein-protein interactions (PPIs) are regulated.
Autor:
Miguel Betegon, Michael A. Kennedy, Theresa Ramelot, Daniel Elnatan, David A. Agard, Yanxin Liu
Publikováno v:
eLife, Vol 6 (2017)
eLife
eLife
Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate “client” proteins, facilitating their folding and activating them for biological function. Despite decades of research, the mechanism connecting ATP hydrolysis a