The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
about
EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factorSite-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cellsCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsFunctional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins.An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.Nitrosative stress-induced Parkinsonian Lewy-like aggregates prevented through polyphenolic phytochemical analog interventionOrganocatalysts of oxidative protein folding inspired by protein disulfide isomerase.Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.Modulation of conotoxin structure and function is achieved through a multienzyme complex in the venom glands of cone snails.An introduction to thiol redox proteins in the endoplasmic reticulum and a review of current electrochemical methods of detection of thiols.Identification of the thiol isomerase-binding peptide, mastoparan, as a novel inhibitor of shear-induced transforming growth factor β1 (TGF-β1) activation.Analysis of protein covalent modification by xenobiotics using a covert oxidatively activated tag: raloxifene proof-of-principle study.Participation of low molecular weight electron carriers in oxidative protein folding.Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.Succination of Protein Disulfide Isomerase Links Mitochondrial Stress and Endoplasmic Reticulum Stress in the Adipocyte During Diabetes.Building bridges: disulphide bond formation in the cell.Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit.The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.Enzymes as chaperones and chaperones as enzymes.Catalysis of protein disulfide bond isomerization in a homogeneous substratepH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate.The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate.The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase.Assisted refolding of recombinant prochymosin with the aid of protein disulphide isomerase.Identification of alkylation-sensitive target chaperone proteins and their reactivity with natural products containing Michael acceptor.Protein disulfide isomerase reaction kinetics in endoplasmic reticulum for monoclonal antibody refolding and assembly.Novel photosystem involving protonation and deprotonation processes modelled on a PYP photocycle.Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase.Challenges in the evaluation of thiol-reactive inhibitors of human protein disulfide Isomerase.Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties.A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase.Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4-Hydroxylases
P2860
Q28205813-51CBEC9B-B0A9-468A-86CD-D8C556E87360Q28212078-060C019B-C4B6-4C6C-A930-49D05096FE02Q29999427-80D78A85-4146-436D-B38A-8E0E7224DDEDQ33202816-7FA23DEC-297B-48B3-89FC-4D58E8DF9938Q34371713-72F76D49-A5D2-47BB-90FC-A389B468C29AQ35203626-79BE3081-2757-4A06-A282-F3745FCDA805Q35285491-99A23234-CE1B-4447-8AAA-B28229362058Q35479588-FB37E254-147E-4286-A28C-F6B869C38097Q36298403-0CC35E70-8472-4102-99B2-18823320F47EQ36433608-289A6A1E-B800-4DF1-8CEC-6BDBEABB148BQ36760362-8B259A32-55B8-49E2-BCAB-087E8AC06F5BQ36840069-E0DA67E9-7B7D-4163-8F5B-A658CACC3C6AQ37462269-75D987FD-8885-439F-BF20-A0BF98AF9AD2Q38421683-F39A6721-A674-4AA6-8ED0-1DA0BFEA872EQ40258446-6D15B214-BEB7-4506-9FD2-790512B3A16EQ40576198-92EE4ADC-046A-4A6B-9913-8CFDC1032CB0Q40872620-6DEF90BF-E8C9-468A-A7D2-546616572280Q41065191-1431421B-66AB-482E-B09C-2B2968A2F7DBQ41752216-C6DD8336-FE08-4CFF-84D5-FCEDD99A2959Q41892268-D8DBEADF-F6D2-4377-9F2F-25CEE67BCD78Q41971990-EC24DD11-DF00-4DD5-918A-B6B22BD023C5Q41997546-80EDB197-DD76-40C5-AD70-3A38BE7E632BQ42063969-C572D3A7-CC6B-49F0-8911-B9520F3685F7Q42112518-8980E9C4-CF20-47F0-A0B7-F65ABECF1100Q42141967-99CDE467-55E8-46EA-A401-38CB7B009B47Q42156942-3494ADAA-C0B1-496F-B167-BE6A8C727CD2Q42828318-D54F008D-845D-4DE2-9E95-73D1DD676478Q44727978-4DB899F2-5A12-4D28-95CA-6E64FC86594EQ45970041-9663D0B2-E690-4DD9-A5DE-5CA01E8A16BCQ46432963-C403C391-B2F9-47BA-BAD2-64929F532A66Q48023868-804C7F08-6768-47FC-A821-598A81A8A024Q51023637-D642BBB3-A861-4174-B04B-B813E6475B27Q54559625-F6855EF4-241C-4562-8F92-591C5C3874DEQ54603426-3D8F5DC8-7E6F-4CED-AB94-7CE5A9459FFFQ54618987-6116BF53-23FD-425D-962E-AB39D4B325CFQ56038109-A147A00E-6A00-45E5-B1F6-7636B50051E7
P2860
The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
The reactivities and ionizatio ...... n protein disulphide-isomerase
@en
The reactivities and ionizatio ...... n protein disulphide-isomerase
@nl
type
label
The reactivities and ionizatio ...... n protein disulphide-isomerase
@en
The reactivities and ionizatio ...... n protein disulphide-isomerase
@nl
prefLabel
The reactivities and ionizatio ...... n protein disulphide-isomerase
@en
The reactivities and ionizatio ...... n protein disulphide-isomerase
@nl
P2860
P356
P1433
P1476
The reactivities and ionizatio ...... n protein disulphide-isomerase
@en
P2093
Freedman RB
Hawkins HC
P2860
P304
P356
10.1042/BJ2750335
P407
P478
275 ( Pt 2)
P577
1991-04-01T00:00:00Z