Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Seema Chakravarthi"'
Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation
Autor:
Hui-ling Lu, Alyson M Sheppard, Karl M Baker, Kevin P Langton, Neil J. Bulleid, Seema Chakravarthi
Publikováno v:
The EMBO Journal. 27:2988-2997
Formation of disulphide bonds within the mammalian endoplasmic reticulum (ER) requires the combined activities of Ero1α and protein disulphide isomerase (PDI). As Ero1α produces hydrogen peroxide during oxidation, regulation of its activity is crit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0449364513353a5b2b17fc56cbb02648
https://doi.org/10.1038/emboj.2008.230
https://doi.org/10.1038/emboj.2008.230
Autor:
Seema Chakravarthi, Neil J. Bulleid
Publikováno v:
Journal of Biological Chemistry. 279:39872-39879
The formation of native disulfide bonds is an essential event in the folding and maturation of proteins entering the secretory pathway. For native disulfides to form efficiently an oxidative pathway is required for disulfide bond formation and a redu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e25337c0ecfc7d7b2eacacf8660e68f
https://doi.org/10.1074/jbc.m406912200
https://doi.org/10.1074/jbc.m406912200
Publikováno v:
Oxidative Folding of Peptides and Proteins ISBN: 9780854041480
An essential step during the maturation of many membrane and secretory proteins in the endoplasmic reticulum (ER) is the formation of native disulfide bonds. Any two cysteines within a protein have the potential to form a disulfide bond. Hence, the f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f03b16cd884be47e74d5416cb4c0582
https://doi.org/10.1039/9781847559265-00081
https://doi.org/10.1039/9781847559265-00081
Autor:
Günter J. Hämmerling, Neil J. Bulleid, Seema Chakravarthi, Catherine E. Jessop, Simon C. Lovell, Natalio Garbi
ERp57 is a member of the protein disulphide isomerase family of oxidoreductases, which are involved in native disulphide bond formation in the endoplasmic reticulum of mammalian cells. This enzyme has been shown to be associated with both calnexin an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09b8b23ebc32dc7610e9e197f84dc5be
https://europepmc.org/articles/PMC1782378/
https://europepmc.org/articles/PMC1782378/
Publikováno v:
EMBO reports. 7(3)
Glutathione is a ubiquitous molecule found in all parts of the cell where it fulfils a range of functions from detoxification to protection from oxidative damage. It provides the main redox buffer for cells and as such has been implicated in the form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c8ec0032334939df59cc17f472e68ed
https://pubmed.ncbi.nlm.nih.gov/16607396
https://pubmed.ncbi.nlm.nih.gov/16607396
Publikováno v:
Biochemical Society transactions. 32(Pt 5)
Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4689c6b161fb279e42eba1b21e57536
https://pubmed.ncbi.nlm.nih.gov/15493980
https://pubmed.ncbi.nlm.nih.gov/15493980
Publikováno v:
Biochemical Journal; 2007, Vol. 404 Issue 3, p403-411, 9p