about
Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cellsERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin familyEndoplasmic reticulum protein BI-1 modulates unfolded protein response signaling and protects against stroke and traumatic brain injuryTwo pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaOxidative protein folding in eukaryotes: mechanisms and consequencesMonitoring protein stability in vivoTargeting the redox balance in inflammatory skin conditionsThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBNovel Covalently Linked Insulin Dimer Engineered to Investigate the Function of Insulin DimerizationCrystal structure of type VI effector Tse1 from Pseudomonas aeruginosaStructural plasticity of 4- -helical bundles exemplified by the puzzle-like molecular assembly of the Rop proteinThe thioredoxin system protects ribosomes against stress-induced aggregationRole of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions.A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum.A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.Cellular disulfide bond formation in bioactive peptides and proteinsFanconi anemia group C protein prevents apoptosis in hematopoietic cells through redox regulation of GSTP1Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatinProgranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteinsCHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulumDifferential cooperative enzymatic activities of protein disulfide isomerase family in protein folding.PDIA3 mRNA expression and IL-2, IL-4, IL-6, and CRP levels of acute kidney allograft rejection in ratCell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunitiesDynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus.DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.Protein disulfide isomerase of Toxoplasma gondii is targeted by mucosal IgA antibodies in humans.The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways.High expression of a cytokeratin-associated protein in many cancers.ROS and protein oxidation in early stages of cytotoxic drug induced apoptosis.Biochemical and structural characterization of mammalian-like purine nucleoside phosphorylase from the Archaeon Pyrococcus furiosus.A Non-Classical Member of the Protein Disulfide Isomerase Family, PDI7 of Arabidopsis thaliana, Localizes to the cis-Golgi and Endoplasmic Reticulum Membranes.Direct identification of the Meloidogyne incognita secretome reveals proteins with host cell reprogramming potential.Peroxicretion: a novel secretion pathway in the eukaryotic cell.Ligand effects on cross-linking support a conformational mechanism for serotonin transport.Kinetics and intracellular location of intramolecular disulfide bond formation mediated by the cytoplasmic redox system encoded by vaccinia virus.The metal nanoparticle-induced inflammatory response is regulated by SIRT1 through NF-κB deacetylation in aseptic loosening.The dual nature of human extracellular superoxide dismutase: one sequence and two structures.Effects of bevacizumab on endoplasmic reticulum stress in hypoxic retinal pigment epithelial cells.
P2860
Q24291018-86FA4EE1-A270-457C-A4F9-8A579FA2E515Q24292308-0A64FE7A-0FBA-4898-8E12-1A7F9C928F87Q24306871-341245BB-F7D5-41D7-A9F3-1684A64F7CA0Q24550637-69C37B14-C570-4414-910D-8B3B4C09AB3CQ24599012-F2A34E6B-64F0-409F-9D78-F06BA6C5E0C3Q24676827-62EE280F-8D41-4A46-B031-167E83E6E024Q24814043-D502E417-135F-481A-8B9D-617ABE4C989AQ27023252-3B485196-0D3C-4C3A-81B5-C26C4392C79EQ27639655-489106C8-FF16-4F7E-962B-AF50976009BDQ27652023-4E0A0938-6BA8-462B-9E33-D09A432B6D57Q27677467-A5401B16-41D8-4DB1-A241-5BADFA93281AQ27681661-9372C200-47B1-44AA-B450-64D4E5483247Q27684684-6F74E200-763E-4104-8E09-D39794C1F4BCQ27935088-CECE4EB4-57A0-442F-8471-4FA56A2B10B3Q27937765-FD56CA19-2F61-4D0F-897E-620B652C65C2Q27939137-3E16B4B3-352A-4043-8DEB-D3A915805F34Q27940305-87708054-E62F-42EE-AFF3-EBF57EB8BC08Q28080871-C70C733D-869F-4156-9D35-3296DC6F45C0Q28204361-DD42F4D1-61C8-44C9-81A0-E700A1B1DCB8Q28242760-43AE2795-214A-4D5A-A065-09996AE631FCQ28477534-1A6DC85C-1882-4142-9407-E30DCCA78888Q28512249-B84E0E4D-947F-4E63-AC13-1FBC75701146Q28570569-48A69352-C37B-47EC-9148-ACEB3852D51CQ28573825-B03B8D26-FF20-46E8-A29A-E06957FEF0FFQ29617768-4AF7B72A-4043-47ED-8B20-BAC336BC82FAQ30443300-CDE34CC5-2682-4DBC-AEE4-5A96C1D167FBQ31583197-80486541-1FD7-4AC3-A923-866128DCEF80Q32147854-ED1B774D-61B6-4423-A3ED-2B7B9AEB6019Q33231814-FEC0BDCE-D1E1-4392-916C-0B8A85B2147BQ33238565-9982FAB4-D09D-4B0C-BB44-B73DEC35A61BQ33260811-5D25F494-94F8-42A2-ADED-70438CF25E80Q33281558-BF7EF0A7-A9C6-4918-81F9-815DD6501E10Q33365290-CA957A34-262A-48D4-B537-EF0B704238CAQ33381586-FC23EDE0-EA91-4F0D-9270-8CA144A7DD80Q33449028-D28BC0D1-03D4-433A-A89C-03C59F0DCFE9Q33553309-F6D39CAC-5792-46DB-BAB6-7BF38F56B026Q33664851-CAF2F045-0C4F-4C38-A093-533665AACF85Q33713171-0C31B9A5-C1F8-4146-A3CF-40CE2BC371DAQ33713531-E99B351C-BA9D-450D-86DE-A89BD3ECA45CQ33773175-3F0F8785-5D35-4D87-A8CB-1FEB8F3B8987
P2860
description
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im Mai 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: May 2000)
@en
vedecký článok (publikovaný 2000-05)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd in 2000-05)
@nl
наукова стаття, опублікована в травні 2000
@uk
مقالة علمية (نشرت في مايو 2000)
@ar
name
Pathways for protein disulphide bond formation
@ast
Pathways for protein disulphide bond formation
@en
Pathways for protein disulphide bond formation
@nl
type
label
Pathways for protein disulphide bond formation
@ast
Pathways for protein disulphide bond formation
@en
Pathways for protein disulphide bond formation
@nl
prefLabel
Pathways for protein disulphide bond formation
@ast
Pathways for protein disulphide bond formation
@en
Pathways for protein disulphide bond formation
@nl
P2093
P1476
Pathways for protein disulphide bond formation
@en
P2093
P304
P356
10.1016/S0962-8924(00)01745-1
P407
P577
2000-05-01T00:00:00Z