Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. - Wikidata - awgldk - TriplyDB

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

http://www.wikidata.org/entity/Q34519184

about

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor Antioxidant responses and cellular adjustments to oxidative stress Protein folding and quality control in the ER Endoplasmic reticulum stress and Nox-mediated reactive oxygen species signaling in the peripheral vasculature: potential role in hypertension Oxidative protein folding: selective pressure for prolamin evolution in rice Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways Disulfide bond formation in the mammalian endoplasmic reticulum Protein disulfide isomerase and host-pathogen interaction Orchestration of secretory protein folding by ER chaperones Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4 Crystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic Cycle Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′Peroxiredoxin-1 from the Human Hookworm Ancylostoma ceylanicum Forms a Stable Oxidized Decamer and Is Covalently Inhibited by Conoidin A Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress Identification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testis Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox Disulfide bond formation in prokaryotes: history, diversity and design Suppression of peroxiredoxin 4 in glioblastoma cells increases apoptosis and reduces tumor growth.Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme Approaches to imaging unfolded secretory protein stress in living cells.Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load.Mechanism-based proteomic screening identifies targets of thioredoxin-like proteins A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.Prdx4 is a compartment-specific H2O2 sensor that regulates neurogenesis by controlling surface expression of GDE2.Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides.Balanced Ero1 activation and inactivation establishes ER redox homeostasis Proteostasis and REDOX state in the heart.Peroxiredoxin 4 as an independent prognostic marker for survival in patients with early-stage lung squamous cell carcinoma.Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family Redox reactions in mammalian spermatogenesis and the potential targets of reactive oxygen species under oxidative stress ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding.Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes.TriPer, an optical probe tuned to the endoplasmic reticulum tracks changes in luminal H2O2.Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells.

P2860

Q24295045-37E87975-6149-434F-9D2E-122A5DBB6799 Q26800229-14100CA5-A48D-465B-AEE8-739D149ED212 Q26823157-A9A907F6-F5DF-4CEE-9EBC-EF7830883F14 Q26823318-1733D6BB-0B8C-4E32-815F-CBD641802591 Q26824980-1EF44129-1069-4CA7-AA70-493D3F80D0BA Q26827753-19431503-D930-4B99-B8EC-A5BEE696439A Q26829235-05B0FBC7-EAAD-4EEF-B75F-0F703C249468 Q27005875-0FC63FD7-195B-408F-96C3-FB63F7DDFC17 Q27013551-1FBD8CC2-F16F-4E2F-A634-0A0F84263147 Q27673881-D926A464-6437-4D91-8749-DFEB18561712 Q27675001-0ECCCDE1-8615-45CC-AD6D-C07ED5D249CA Q27675610-8C6AF8E3-4BEF-4BE9-B47D-A1950382C393 Q27679211-037A6588-8965-4E7B-97FA-B014C6A4B534 Q27679694-A6FCBF6F-9ECF-40AB-99A5-A8EAD1C94628 Q28243241-7907A97E-76B9-4873-96FF-BA283B51BCCC Q28244526-46C5774C-B702-4D32-BD42-7B6A9D9C0775 Q28507042-90F76EB5-6001-404E-A3EB-75883FB9C9CC Q28508619-C5F1B70F-1308-4C05-BB66-DB0A261B078F Q28585197-F7692F13-A644-4D09-BF37-8F8FDB819473 Q28591111-8DB2DD45-D83C-492A-BD41-2DCDBE7829B4 Q33723782-DB6D7168-9D6E-4053-8291-AD713B74F065 Q34391054-8F754115-583E-44D4-A219-042BE63B6498 Q34476988-F86BC7A6-C639-45BF-9AC6-F958A41D3784 Q34546956-6E004D5D-AC7A-4C3E-9A12-2F21141E4B89 Q34991338-02284A8A-3C45-4F4C-A857-60A0BE64E10F Q35105380-8A7EF723-0C44-4ADB-82BA-6B7C31FE72A3 Q35126677-7415C018-68BE-472D-AB8E-6B2DDC0C5DB3 Q35227956-BE55C1B8-A338-4710-B6DA-1C5B17B82B01 Q35608957-6C1B9D9B-E5EF-4787-BAEF-40D141E58EDF Q35762914-4749ACB2-0EC8-4DF0-A118-60DC3E2DFB7E Q35841737-1CED0AD4-FDEB-4DF5-A611-14C5F5B60DD9 Q35906430-8F9464CD-37EB-430B-AE21-30B39D5197D2 Q35919069-F073E441-E031-4C0D-A31D-7DC13BCA4FC2 Q35980820-A84F503D-7130-4792-9664-37C6D4F0D00F Q36088073-EFDBAC21-11ED-42AA-BB5E-D382E8C73676 Q36210737-B914FD37-C848-4BB9-B982-0EBB87CBD256 Q36246139-3FB9690B-FF0C-420B-ADAA-8FFA904FFED5 Q36324419-53088A30-0D8B-459A-9123-6E4112259BEC Q36324564-3107D02E-C976-421B-A1CA-ECEC3E3A7013 Q36353820-268BD98D-4C3F-4D54-A2AA-F5E51349F342

P2860

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

http://www.wikidata.org/entity/Q34519184

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@ast

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@en

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@nl

type

label

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@ast

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@en

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@nl

prefLabel

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@ast

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@en

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@nl

P1433

Q34519184-C038EA05-0FB1-4E15-B999-AF9C320BB1FB

P1476

Q34519184-99E3A495-4F72-4B5F-B232-C3B59EFB8686

P2093

Q34519184-28D7A68A-A5B1-49A3-B16C-A728294605A3

Q34519184-95727F2D-E4CC-4D54-82C4-DB9DB8C48CA4

Q34519184-A6484B00-5C27-4A6E-A88C-2A6833CF4ECF

Q34519184-E4E6D313-5B63-4B67-8BBD-FD95F54817EE

P2860

Q34519184-0351E29E-0A31-4499-8DC0-7B9CB6B7BD16

Q34519184-09636530-8A2D-4042-A309-EA4595B2B35A

Q34519184-1FF5F1B3-A968-4495-9676-22A1E068863F

Q34519184-22CA4BB0-286F-41D2-A147-15CD9B07DB89

Q34519184-26D1CC73-8654-440A-902B-A8734B94D00F

Q34519184-280C23D0-5DA9-4D5A-BE16-4192E35B89B1

Q34519184-2DB1DA40-49B4-4AEC-95BF-E9E1EB02373F

Q34519184-2EA643E4-4E34-48A2-B40E-D34AA6BBAB2A

Q34519184-365A0438-F685-4BDA-B865-4039728F9241

Q34519184-3AF7496D-6382-40FB-9C45-68D62E710403

P304

Q34519184-A6B65796-9A57-4F43-B229-E466C5AEC2AC

P31

Q34519184-FF260173-0088-4DBD-9D8B-EA872617E097

P356

Q34519184-927BB327-F2AA-4847-A504-F028A8E73322

P433

Q34519184-3D6B748D-AEC3-473D-8832-62EAF6C62F5E

P478

Q34519184-C398AC66-6A69-4041-BBAD-1AFAF7D19B52

P50

Q34519184-C8BDAA18-696B-4BB4-BF1A-6B8BF1B0D0B0

Q34519184-F2E3706A-FE5E-4732-B812-14DDE6D0BC26

P577

Q34519184-5F3D3AF1-1711-4BEF-AD2E-DAD513864FE0

P5875

Q34519184-D7E275C9-B174-410F-BC8F-B720487E2B95

P698

Q34519184-D43840F0-AE5B-419C-8591-6F4029B14935

P921

Q34519184-4543D62C-9173-49C6-8AEB-20638A00DE20

Q34519184-6ACF9812-539E-4397-8F19-408BA37E688F

P932

Q34519184-166E2DF1-A714-4CAE-9246-2BFAFF2026DD

P356

J.MOLCEL.2010.11.010

P1433

P1476

Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@en

P2093

Ester Zito

http://www.w3.org/2001/XMLSchema#string

Thomas A Neubert

http://www.w3.org/2001/XMLSchema#string

Yun Yang

http://www.w3.org/2001/XMLSchema#string

Åsa Wahlander

http://www.w3.org/2001/XMLSchema#string

P2860

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

An ER-mitochondria tethering complex revealed by a synthetic biology screen

Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

Oxidative protein folding in eukaryotes: mechanisms and consequences

Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments

Structure of a bacterial homologue of vitamin K epoxide reductase

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum.

Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p

P304

787-797

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.MOLCEL.2010.11.010

http://www.w3.org/2001/XMLSchema#string

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

40

http://www.w3.org/2001/XMLSchema#string

P50

Eduardo P. Melo

P577

2010-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

49671445

http://www.w3.org/2001/XMLSchema#string

P698

21145486

http://www.w3.org/2001/XMLSchema#string

P921

endoplasmic reticulum

protein folding

P932

3026605

http://www.w3.org/2001/XMLSchema#string