Electron avenue: pathways of disulfide bond formation and isomerization.
about
ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin familyTwo pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumFunctional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1aShedding light on disulfide bond formation: engineering a redox switch in green fluorescent proteinThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Coordinate gene regulation by fimbriae-induced signal transductionCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsThe dithiol:disulfide oxidoreductases DsbA and DsbB of Rhodobacter capsulatus are not directly involved in cytochrome c biogenesis, but their inactivation restores the cytochrome c biogenesis defect of CcdA-null mutantsDsbD-catalyzed transport of electrons across the membrane of Escherichia coli.Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coliGenes required for cytochrome c synthesis in Bacillus subtilis.Computation-directed identification of OxyR DNA binding sites in Escherichia coli.Native disulfide bond formation in proteinsComplete pathway for protein disulfide bond formation encoded by poxvirusesFormation and transfer of disulphide bonds in living cells.An attractive surface: gram-negative bacterial biofilms.Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.Genome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDIRoles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.Towards clinical development of a Pfs48/45-based transmission blocking malaria vaccine.Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli.DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa.Just toothpicks and logic: how some labs succeed at solving complex problems.Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function.Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase.Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B.FAD transport and FAD-dependent protein thiol oxidation in rat liver microsomes.Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili.Hemextin AB complex, a unique anticoagulant protein complex from Hemachatus haemachatus (African Ringhals cobra) venom that inhibits clot initiation and factor VIIa activity.Isolation and characterization of a chromosomally encoded disulphide oxidoreductase from Salmonella enterica serovar Typhimurium.
P2860
Q24292308-CBE44E42-02B6-479C-A0A0-637D45FB918EQ24550637-81CC6361-0BFB-4023-835E-90EF900B69DAQ27631272-7F38515C-D52D-4F83-8C4E-161F5C69F3FEQ27635911-9E238B53-FF4E-44B1-9651-8FB528C385E0Q27639655-73FB0C2A-C983-4E18-81D8-B44438810AF1Q28366798-7EDD1E44-DADB-4A76-98D6-3225FF7DC4E7Q29999427-AAE33894-12F5-45A0-AF7A-B2116A4C5DDBQ30932970-9BF1E8C1-9AF5-4C88-B3D0-FD929924777FQ31583197-23924868-EE4B-4137-A4DB-4238B6F644E4Q33211413-5F3FEC7E-19FA-4009-AE0E-310DC1D0296BQ33904926-27B4AA9C-19C2-409C-A38B-844B9C4119BFQ33996659-03B7D061-390D-4495-BC36-75233752BE37Q34046362-455438D2-C9F2-4C91-9C9C-96D83002AFB2Q34067229-BD8D4125-D137-47C2-B800-95D9A8CB3D7CQ34157680-E4228FAF-B3DE-49AE-BFDE-D6E7E9DFE3C8Q34637794-24BCE93E-FE41-454B-AD19-A56C0B999E49Q34828345-E3DEC173-67B5-4B53-8D18-7D94F34B662AQ35713362-0003E552-41B0-42E1-BDC4-43E6B648FE1DQ37264681-20CE0B31-66D4-4218-8C0F-A64CEB331E59Q38289355-B8D80263-FF49-4AEF-89F9-6F8121CBF5B0Q38775588-3B25B90B-7E2A-4C7E-80BA-B0E3C20211B8Q39487446-958950BF-3FCB-49F2-9E24-81BADF5D0E32Q39501974-3B371B90-EDE9-42BA-AEE2-A4FEE9036E71Q39714223-F41B4622-89D8-4BDD-9EA9-DFC27BBC5F17Q39714839-A5D5372D-2F66-4C77-99FB-E1FBBA677889Q40739794-09C8DD7C-8A4C-46C4-9B4B-8F234DAC2A41Q41982341-45254662-292D-4803-8B96-0EDD7065F6A8Q43792245-EE9DCA68-B543-454C-A475-A793BE4783C0Q44652130-86CAC438-3010-424E-AE7D-34BF45708CC8Q44856945-5453D228-ACAB-4A45-8576-3405FE517B37Q46583622-82CFCDBD-F35D-45DF-B78A-F31AF1E4822EQ48341081-D5EB36A3-EDB0-49D0-B762-54C504CB65F8
P2860
Electron avenue: pathways of disulfide bond formation and isomerization.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Electron avenue: pathways of disulfide bond formation and isomerization.
@ast
Electron avenue: pathways of disulfide bond formation and isomerization.
@en
type
label
Electron avenue: pathways of disulfide bond formation and isomerization.
@ast
Electron avenue: pathways of disulfide bond formation and isomerization.
@en
prefLabel
Electron avenue: pathways of disulfide bond formation and isomerization.
@ast
Electron avenue: pathways of disulfide bond formation and isomerization.
@en
P1433
P1476
Electron avenue: pathways of disulfide bond formation and isomerization.
@en
P2093
Beckwith J
Debarbieux L
P304
P356
10.1016/S0092-8674(00)81642-6
P407
P577
1999-10-01T00:00:00Z