Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Ryan D Baldridge"'
Publikováno v:
eLife, Vol 8 (2019)
Misfolded proteins in the lumen of the endoplasmic reticulum (ER) are retrotranslocated into the cytosol and polyubiquitinated before being degraded by the proteasome. The multi-spanning ubiquitin ligase Hrd1 forms the retrotranslocation channel and
Externí odkaz:
https://doaj.org/article/066ce5841a74423e8cd78e2950f38555
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract The endoplasmic reticulum associated degradation (ERAD) pathway regulates protein quality control at the endoplasmic reticulum. ERAD of lumenal and membrane proteins requires a conserved E3 ubiquitin ligase, called Hrd1. We do not understand
Externí odkaz:
https://doaj.org/article/a5532752c83d4a66b0df46260c138e8e
Autor:
Brian G. Peterson, Jiwon Hwang, Jennifer E. Russ, Jeremy W. Schroeder, P. Lydia Freddolino, Ryan D. Baldridge
Publikováno v:
Cell Reports, Vol 42, Iss 11, Pp 113451- (2023)
Summary: Misfolded endoplasmic reticulum (ER) proteins are degraded through a process called ER-associated degradation (ERAD). Soluble, lumenal ERAD targets are recognized, retrotranslocated across the ER membrane, ubiquitinated, extracted from the m
Externí odkaz:
https://doaj.org/article/db46fcc519de4c12a05059b0174fd544
Autor:
Brian G. Peterson, Jiwon Hwang, Jennifer E. Russ, Jeremy Schroeder, Peter L. Freddolino, Ryan D. Baldridge
SummaryMisfolded endoplasmic reticulum proteins are degraded through a process called endoplasmic reticulum associated degradation (ERAD). Soluble, lumenal ERAD targets are recognized, retrotranslocated across the ER membrane, ubiquitinated, extracte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a83e7a696fc6fa563ed1f0c0942ffb92
https://doi.org/10.1101/2023.04.03.535444
https://doi.org/10.1101/2023.04.03.535444
Publikováno v:
eLife, Vol 8 (2019)
eLife
eLife
Misfolded proteins in the lumen of the endoplasmic reticulum (ER) are retrotranslocated into the cytosol and polyubiquitinated before being degraded by the proteasome. The multi-spanning ubiquitin ligase Hrd1 forms the retrotranslocation channel and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c95ccc70b0f6b063e5d533445256d95
https://doi.org/10.7554/elife.50903
https://doi.org/10.7554/elife.50903
Autor:
Ryan D. Baldridge, Tom A. Rapoport
Publikováno v:
Cell. 166:394-407
Summary Misfolded proteins of the ER are retrotranslocated to the cytosol, where they are polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To investigate how the ER-associated Degradation (ERAD) machinery can accomplish
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc0f55e63d29829674349e1b4cccb8b0
https://doi.org/10.1016/j.cell.2016.05.048
https://doi.org/10.1016/j.cell.2016.05.048
Autor:
Yanan Huang, Ryan D. Baldridge, Jie Chen, Jiuyang He, Jian Zhang, Junfeng Zhang, Minmin Liang, Quan Lu, Chenjie Yao, Wang Yanli, Chenchen Li, Xuelian Yin, Rogério P. Pirraco, Lin Ding, Rui L. Reis, Yong Zhang, Minghong Wu
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Advantages such as strong signal strength, resistance to photobleaching, tunable fluorescence emissions, high sensitivity, and biocompatibility are the driving forces for the application of fluorescent nanoparticles (FNPs) in cancer diagnosis and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56951445857ca11cdce0e6d3abf4fa61
https://doi.org/10.1002/adma.201902409
https://doi.org/10.1002/adma.201902409
Publikováno v:
The Journal of Cell Biology
The Drs2 flippase increases membrane curvature and anionic phospholipid composition of the membrane by flipping phosphatidylserine, which is critical for vesicular transport between the trans-Golgi network and early endosomes.
Vesicle-mediated p
Vesicle-mediated p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1963fd553590b68c9423647527fdd706
https://doi.org/10.1083/jcb.201305094
https://doi.org/10.1083/jcb.201305094
Publikováno v:
Journal of Biological Chemistry. 288:19516-19527
Type IV P-type ATPases (P4-ATPases) use the energy from ATP to "flip" phospholipid across a lipid bilayer, facilitating membrane trafficking events and maintaining the characteristic plasma membrane phospholipid asymmetry. Preferred translocation sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa34664be8179669ab752d6332a9e9cc
https://doi.org/10.1074/jbc.m113.476911
https://doi.org/10.1074/jbc.m113.476911