Zobrazeno 1 - 10
of 82
pro vyhledávání: '"Randolph Y Hampton"'
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e41119 (2012)
Escherichia coli Shiga-like toxin 1 normally traffics to the endoplasmic reticulum (ER) in sensitive mammalian cells from where the catalytic A chain (SLTxA1) dislocates to the cytosol to inactivate ribosomes. Currently, no molecular details of the d
Externí odkaz:
https://doaj.org/article/3e467bd503c24aa9930490197ae9259f
Autor:
Margaret A. Wangeline, Sonya E. Neal, Matthew P. Flagg, Christopher Benner, Sascha H. Duttke, Sarah R. Holland, Randolph Y. Hampton
Publikováno v:
Molecular Biology of the Cell
Molecular biology of the cell, vol 32, iss 7
Molecular biology of the cell, vol 32, iss 7
Before their delivery to and degradation by the 26S proteasome, misfolded transmembrane proteins of the endoplasmic reticulum (ER) and inner-nuclear membrane (INM) must be extracted from lipid bilayers. This extraction process, known as retrotransloc
Autor:
Nidhi Vashistha, Randolph Y. Hampton, Amanjot Singh, Xin Tang, Peter Wipf, Jarrod W. Heck, Jeffrey L. Brodsky
Publikováno v:
Molecular biology of the cell, vol 31, iss 24
Molecular Biology of the Cell
Molecular Biology of the Cell
Chaperones can mediate both protein folding and degradation. This process is referred to as protein triage, which demands study to reveal mechanisms of quality control for both basic scientific and translational purposes. In yeast, many misfolded pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbb149d34a92457890063f60206f954f
https://escholarship.org/uc/item/8h92z2fj
https://escholarship.org/uc/item/8h92z2fj
Publikováno v:
The Journal of biological chemistry, vol 292, iss 8
A surprising feature of endoplasmic reticulum (ER)-associated degradation (ERAD) is the movement, or retrotranslocation, of ubiquitinated substrates from the ER lumen or membrane to the cytosol where they are degraded by the 26S proteasome. Multispan
Publikováno v:
The FASEB Journal. 33
Publikováno v:
Methods in enzymology. 619
Elimination of misfolded proteins by endoplasmic reticulum (ER)-associated protein degradation (ERAD) ensures that proteins proceeding through the secretory pathway are correctly folded and processed, which is critical to minimize ER stress. All ERAD
Publikováno v:
Yeast (Chichester, England)REFERENCES. 36(10)
Yeast recombination cloning is a straightforward and powerful method for recombining a plasmid backbone with a specific DNA fragment. However, the utility of yeast recombination cloning is limited by the requirement for the backbone to contain an CEN
Elimination of misfolded proteins by endoplasmic reticulum (ER)-associated protein degradation (ERAD) ensures that proteins proceeding through the secretory pathway are correctly folded and processed, which is critical to minimize ER stress. All ERAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e65777efd2ca4d1c9339b93ee079dfb
https://doi.org/10.1016/bs.mie.2019.01.002
https://doi.org/10.1016/bs.mie.2019.01.002
Autor:
Man Shi, Xiaoman Zhang, Daniel L. Kastner, Ellen M. Gravallese, Charles V. Rosadini, Murali K. Akula, Kira Gritsman, Donghai Wang, Susan Carpenter, Katherine A. Fitzgerald, Zhaozhao Jiang, Annie S Li, Randolph Y. Hampton, David Miao, Jonathan C. Kagan, Ruth M Gavin, Celia E Foster, Douglas T. Golenbock, Martin O. Bergo, Sorcha D. Forde, Jae Jin Chae, Neal S. Silverman, Gail Germain
Publikováno v:
Nature immunology
Nature immunology, vol 17, iss 8
Nature immunology, vol 17, iss 8
Deficiency in mevalonate kinase (MVK) causes systemic inflammation. However, the molecular mechanisms linking the mevalonate pathway to inflammation remain obscure. Geranylgeranyl pyrophosphate, a non-sterol intermediate of the mevalonate pathway, is
Publikováno v:
iScience, vol 23, iss 9
iScience, Vol 23, Iss 9, Pp 101493-(2020)
iScience
iScience, Vol 23, Iss 9, Pp 101493-(2020)
iScience
Summary ER-associated degradation (ERAD) targets misfolded ER proteins for degradation. Retrotranslocation, a key feature of ERAD, entails removal of ubiquitinated substrates into the cytosol for proteasomal destruction. Recently, it has been shown t