Zobrazeno 1 - 10
of 50
pro vyhledávání: '"R. B. Freedman"'
Publikováno v:
Journal of Biological Chemistry. 268:19210-19217
Protein disulfide isomerase (PDI) is a multifunctional protein resident in the lumen of the rough endoplasmic reticulum that facilitates protein folding via disulfide bond isomerization. Previously we determined that PDI binds a variety of peptides t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25b15f646efcf1d721b2e9187ff63f98
https://doi.org/10.1016/s0021-9258(19)36501-9
https://doi.org/10.1016/s0021-9258(19)36501-9
Publikováno v:
The Biochemical journal. 354(Pt 3)
Using a cross-linking approach, we have recently demonstrated that radiolabelled model peptides or misfolded proteins specifically interact in vitro with two members of the protein disulphide- isomerase family, namely PDI and PDIp, in a crude extract
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3b085691fe28abf88fc4ca831339a306
https://pubmed.ncbi.nlm.nih.gov/11237859
https://pubmed.ncbi.nlm.nih.gov/11237859
Publikováno v:
The Journal of biological chemistry. 276(14)
Protein disulfide isomerase (PDI) is a modular polypeptide consisting of four domains, a, b, b', and a', plus an acidic C-terminal extension, c. PDI carries out multiple functions, acting as the beta subunit in the animal prolyl 4-hydroxylases and in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::56a9caf203962556d47f142bb5685436
https://pubmed.ncbi.nlm.nih.gov/11134056
https://pubmed.ncbi.nlm.nih.gov/11134056
Publikováno v:
Animal Cell Technology: Basic & Applied Aspects ISBN: 9780792344865
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::808caf97034e513f63dff4afd37b4de3
https://doi.org/10.1007/978-94-011-5746-9_83
https://doi.org/10.1007/978-94-011-5746-9_83
Publikováno v:
The Journal of biological chemistry. 271(32)
The B subunits of Escherichia coli heat-labile enterotoxin (EtxB) and cholera toxin (CtxB) assemble in vivo into exceptionally stable homopentameric complexes, which maintain their quaternary structure in a range of conditions that would normally be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b3944e71eb336239e93cfbbb4fe2ca56
https://pubmed.ncbi.nlm.nih.gov/8702586
https://pubmed.ncbi.nlm.nih.gov/8702586
Publikováno v:
The Journal of biological chemistry. 270(50)
The B-subunit pentamer of Escherichia coli heat-labile enterotoxin (EtxB) is highly stable, maintaining its quaternary structure in a range of conditions that would normally be expected to cause protein denaturation. In this paper the structural stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::175519898ea3b5afe7f28750f4895de9
https://pubmed.ncbi.nlm.nih.gov/8530395
https://pubmed.ncbi.nlm.nih.gov/8530395