Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Colin J Stirling"'
Publikováno v:
PLoS Biology, Vol 9, Iss 5, p e1001073 (2011)
Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic pro
Externí odkaz:
https://doaj.org/article/60376e1c97c340798328344ab8afaec3
Autor:
Robert F. L. Steuart, Kofi L. P. Stevens, Carl J. Mousley, Paris F. White, Hasindu G. Dassanayake, Aleshanee L. Paxman, Lamprini Baklous, Christopher M. Witham, Benjamin L. Schulz, Colin J. Stirling, Amy L. Black
Publikováno v:
J Biol Chem
The endoplasmic reticulum (ER) is the entry point to the secretory pathway and major site of protein biogenesis. Translocation of secretory and integral membrane proteins across or into the ER membrane occurs via the evolutionarily conserved Sec61 co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d7dc122afdb755ae3a6064ed8348bab
https://doi.org/10.1074/jbc.ra119.010378
https://doi.org/10.1074/jbc.ra119.010378
Autor:
Colin J. Stirling, Amy L. Black, K. Y. Benjamin Yeo, Kelsi Wells, Carl J. Mousley, Robert F. L. Steuart, Kofi L. P. Stevens, Benjamin L. Schulz
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(47)
BiP (Kar2 in yeast) is an essential Hsp70 chaperone and master regulator of endoplasmic reticulum (ER) function. BiP's activity is regulated by its intrinsic ATPase activity that can be stimulated by two different nucleotide exchange factors, Sil1 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45de2b4874522457d06da8be5f7c31fd
https://pubmed.ncbi.nlm.nih.gov/29109265
https://pubmed.ncbi.nlm.nih.gov/29109265
Autor:
Michael P. Spiller, Colin J. Stirling
Publikováno v:
The Journal of Biological Chemistry
Protein translocation across the endoplasmic reticulum membrane occurs via a "translocon" channel formed by the Sec61p complex. In yeast, two channels exist: the canonical Sec61p channel and a homolog called Ssh1p. Here, we used trapped translocation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37aa1b13a248d990c325246d8106a443
https://doi.org/10.1074/jbc.m111.219568
https://doi.org/10.1074/jbc.m111.219568
Publikováno v:
The Journal of Biological Chemistry
Protein translocation across the endoplasmic reticulum membrane occurs at the Sec61 translocon. This has two essential subunits, the channel-forming multispanning membrane protein Sec61p/Sec61α and the tail-anchored Sss1p/Sec61γ, which has been pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b77ad929f6ce5f608b0034b5bef40da6
http://europepmc.org/articles/PMC2952269
http://europepmc.org/articles/PMC2952269
Publikováno v:
The Journal of Biological Chemistry
The Journal of Biological Chemistry, 285(28), 21600-21606. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
The Journal of Biological Chemistry, 285(28), 21600-21606. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Kar2p, an essential Hsp70 chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae, facilitates the transport and folding of nascent polypeptides within the endoplasmic reticulum lumen. The chaperone activity of Kar2p is regulated by its in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9b0f0b36d2bdf2a1f6376575a0290c9
http://europepmc.org/articles/PMC2898433
http://europepmc.org/articles/PMC2898433
Publikováno v:
Journal of Biological Chemistry. 283:33883-33888
Misfolded proteins in the endoplasmic reticulum (ER) are exported to the cytosol for degradation by the proteasome in a process known as ER-associated degradation (ERAD). CPY* is a well characterized ERAD substrate whose degradation is dependent upon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::66447a5b1a44033663d586c4824822aa
https://doi.org/10.1074/jbc.m803054200
https://doi.org/10.1074/jbc.m803054200
Publikováno v:
Journal of Biological Chemistry. 281:6325-6333
Glucosidase II is essential for sequential removal of two glucose residues from N-linked glycans during glycoprotein biogenesis in the endoplasmic reticulum. The enzyme is a heterodimer whose alpha-subunit contains the glycosyl hydrolase active site.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ba0c7c61c49ce32fc7ab40ee50639c9
https://doi.org/10.1074/jbc.m510455200
https://doi.org/10.1074/jbc.m510455200
Publikováno v:
Science. 303:98-101
Hsp70s are a ubiquitous family of molecular chaperones involved in many cellular processes. Two Hsp70s, Lhs1p and Kar2p, are required for protein biogenesis in the yeast endoplasmic reticulum. Here, we found that Lhs1p and Kar2p specifically interact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::923ba469e5ebc46bce040f907d51d273
https://doi.org/10.1126/science.1092287
https://doi.org/10.1126/science.1092287
Publikováno v:
Molecular Biology of the Cell. 15:1-10
Posttranslational translocation of prepro-α-factor (ppαF) across the yeast endoplasmic reticulum membrane begins with the binding of the signal sequence to the Sec complex, a membrane component consisting of the trimeric Sec61p complex and the tetr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bd3dd4a198c29c334d70d71d649c8cf
https://doi.org/10.1091/mbc.e03-06-0390
https://doi.org/10.1091/mbc.e03-06-0390