Zobrazeno 1 - 10 of 497 pro vyhledávání: '"R B Freedman"'
1
Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
Autor: R B Freedman, Robert Noiva, W J Lennarz
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
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6
Akademický článek
The Role of Protein Disulfide Isomerase Inhibitors in Cancer Therapy.
Autor: Nie Q; School of Pharmacy, State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou, 730000, China., Yang J; School of Pharmacy, State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou, 730000, China., Zhou X; School of Pharmacy, State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou, 730000, China., Li N; School of Pharmacy, State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou, 730000, China., Zhang J; School of Pharmacy, State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou, 730000, China.
Publikováno v: ChemMedChem [ChemMedChem] 2024 Sep 25, pp. e202400590. Date of Electronic Publication: 2024 Sep 25.
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7
The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands
Autor: P, Klappa, R B, Freedman, M, Langenbuch, M S, Lan, G K, Robinson, L W, Ruddock
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
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8
Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57
Autor: A, Pirneskoski, L W, Ruddock, P, Klappa, R B, Freedman, K I, Kivirikko, P, Koivunen
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
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10
Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitro
Autor: L W, Ruddock, J J, Coen, C, Cheesman, R B, Freedman, T R, Hirst
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
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