Activation of extracellular transglutaminase 2 by thioredoxin - Wikidata - wikimedia - TriplyDB

Activation of extracellular transglutaminase 2 by thioredoxin

Activation of extracellular transglutaminase 2 by thioredoxin

http://www.wikidata.org/entity/Q24634746

about

Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix Transglutaminase 2-mediated serotonylation in pulmonary hypertension Cellular functions of tissue transglutaminase Role of transglutaminase 2 in celiac disease pathogenesis Astrocyte-derived tissue Transglutaminase affects fibronectin deposition, but not aggregation, during cuprizone-induced demyelination Transglutaminase regulation of cell function.Activity-regulating structural changes and autoantibody epitopes in transglutaminase 2 assessed by hydrogen/deuterium exchange.Thioredoxin is involved in endothelial cell extracellular transglutaminase 2 activation mediated by celiac disease patient IgA.A universal entropy-driven mechanism for thioredoxin-target recognition.P2X7 receptor-mediated TG2 externalization: a link to inflammatory arthritis?Tissue Transglutaminase Mediated Tumor-Stroma Interaction Promotes Pancreatic Cancer Progression P2X7 receptor activation regulates rapid unconventional export of transglutaminase-2.Regulation of the activities of the mammalian transglutaminase family of enzymes.Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.Cell-mediated reduction of human β-defensin 1: a major role for mucosal thioredoxin Secreted CLIC3 drives cancer progression through its glutathione-dependent oxidoreductase activity.Transglutaminase as a therapeutic target for celiac disease.Coeliac disease - from genetic and immunological studies to clinical applications.Polyamines: therapeutic perspectives in oxidative stress and inflammatory diseases.Thioredoxin-1 Selectively Activates Transglutaminase 2 in the Extracellular Matrix of the Small Intestine: IMPLICATIONS FOR CELIAC DISEASE.Epitope-dependent Functional Effects of Celiac Disease Autoantibodies on Transglutaminase 2.Transglutaminase 2 and Transglutaminase 2 Autoantibodies in Celiac Disease: a Review.Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes.Transglutaminase 2 inhibitor abrogates renal cell carcinoma in xenograft models.Interplay between transglutaminases and heparan sulphate in progressive renal scarring.Structural aspects of transglutaminase 2: functional, structural, and regulatory diversity.An unprecedented dual antagonist and agonist of human Transglutaminase 2.Elevated transglutaminase 2 activity is associated with hypoxia-induced experimental pulmonary hypertension in mice.Role of hypoxia-induced transglutaminase 2 in pulmonary artery smooth muscle cell proliferation.Selective inhibition of extracellular thioredoxin by asymmetric disulfides.Endothelial cell-surface tissue transglutaminase inhibits neutrophil adhesion by binding and releasing nitric oxide.Endoplasmic reticulum-resident protein 57 (ERp57) oxidatively inactivates human transglutaminase 2.Polyamines and transglutaminases: future perspectives.An isomerase completes the circuit for a redox switch.Synthesis and Kinetic Characterisation of Water-Soluble Fluorogenic Acyl Donors for Transglutaminase 2.Cystamine and cysteamine as inhibitors of transglutaminase activity

P2860

Q24309155-71479DA5-8733-405F-A487-9232371E16EE Q27027862-53EE71B2-DFFB-482C-AEC1-DF77D20D4FD7 Q28260600-EDC3529B-8C35-44C2-B6F4-64B45C9DAFA0 Q28262529-3539AF28-26F8-4D95-866B-024CB287F9E2 Q29248440-FD2B9545-1391-4120-A988-BF237CFF36D0 Q33707936-38D3B164-E8B4-45A0-88A6-EF078BE7B6F8 Q34661302-D181801D-175A-4860-8BBB-CAEC45BC68A8 Q35018831-A42B9BE8-8CA1-448D-B3DE-B6388180BA52 Q35818808-815411BD-83C0-4511-827B-23EE0867CAEE Q36113827-C03E8220-A3FA-4465-BE23-799F073A4F3F Q36117713-3619B32E-57DA-42AC-B795-E00CC9C82C47 Q36417661-89F77F8B-A05D-437F-A162-9D544CDFCDD9 Q36620140-1E16F923-9AE1-49F4-B3BE-357B893A926A Q36984552-8B2FB9AD-E852-4054-AD48-A68FEC721F57 Q37250664-F12D8220-DFEF-4F35-A632-8300AFC444FA Q37651981-9D46CEC6-8272-431F-9E4D-63C5F8B297EC Q38269678-75AF419B-F00D-40D2-910F-0C75CE74CCA6 Q38408084-3F00AFEE-DB93-4B39-9E5C-CCA0DE9DDA51 Q38653424-58396D0A-AC01-437B-9612-AD2AB5F45AA3 Q38724906-60F890F9-7496-44CF-B9A3-34D89E48C8BF Q38736418-85C3AB4A-B00A-4661-9653-BF887C7DE06F Q38855195-39B2AF9E-7C33-49B8-B00A-061D0CB53823 Q38857583-C1089AD2-85BB-4966-B32D-CB3FE4C98C1F Q39017211-EF59A871-2CEF-4C68-8312-C6ADC5BC6C07 Q39330237-95A9F32B-81F7-4DCD-8068-BD65FBDDA5E4 Q39414447-3E77CE7C-4960-48A1-BAC1-32E9320C62DF Q41810803-0AAE01F2-61BD-4751-9F79-E93508C80379 Q41968228-73D9F537-B6B0-4A98-9E91-85C1E94F41D0 Q42547773-B0B2F8F1-233F-4576-B317-BBFA773AD4DC Q43246200-AB9579C6-F3B7-4CF3-9503-F5B412B66B29 Q47100916-8474D2DE-8E5E-4330-817A-29B9097CCE94 Q47228617-942C42E6-AD8C-40CB-AE60-AE6AA06AFA26 Q50891054-FF2621F4-2211-427C-A6B2-61065F20D609 Q52687745-16F01C64-CDD4-4FD3-B123-3F6E9258A59E Q53764493-848F171C-CADC-4248-ACE4-346164180D74 Q58763905-30FE882A-3CC8-45C5-AC9B-208B7C29C9E9

P2860

Activation of extracellular transglutaminase 2 by thioredoxin

http://www.wikidata.org/entity/Q24634746

description

2011 nî lūn-bûn

@nan

2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Activation of extracellular transglutaminase 2 by thioredoxin

@ast

Activation of extracellular transglutaminase 2 by thioredoxin

@en

Activation of extracellular transglutaminase 2 by thioredoxin

@nl

type

label

Activation of extracellular transglutaminase 2 by thioredoxin

@ast

Activation of extracellular transglutaminase 2 by thioredoxin

@en

Activation of extracellular transglutaminase 2 by thioredoxin

@nl

prefLabel

Activation of extracellular transglutaminase 2 by thioredoxin

@ast

Activation of extracellular transglutaminase 2 by thioredoxin

@en

Activation of extracellular transglutaminase 2 by thioredoxin

@nl

P1433

Q24634746-BB384CC8-76C8-45A4-B68E-E062C2977897

P1476

Q24634746-36C5CAC5-51E0-4CFB-86C4-05266E9AD35A

P2093

Q24634746-2AAC8896-09F8-46EA-A4AB-0BD0DD15F0BD

Q24634746-43FE74F9-4A0F-420C-81F3-E9E88B5615CE

Q24634746-932EA5AF-C3FF-427B-AEE0-275495DC8D1A

Q24634746-C1208BFB-19D8-40C0-A51E-A8C9EB23B40E

Q24634746-E9E562B7-C840-4580-BFC4-FFE559969BD5

Q24634746-EBB03542-D4FC-48A3-9F8E-E8BE152EF9E4

P2860

Q24634746-00877136-6652-4762-B5F6-630447B1CFA1

Q24634746-0C85D397-CAB3-4017-950F-A6C3B90D3548

Q24634746-1984D6E2-636C-4440-B439-8F973CEBC599

Q24634746-1EF5221F-0F7F-4762-96E2-726A124261EC

Q24634746-208A60F1-8BB1-4595-A3D3-4F5B9676E971

Q24634746-2E3F3BF8-B0C3-4132-B90A-D2BA364C053A

Q24634746-38EA3067-15BC-4B6D-BBF2-439D0CAA4E1A

Q24634746-3A5C90B1-FB29-404D-A4BD-BA2E067A4E9E

Q24634746-3D3BDC3B-7AD3-4664-B6BB-839BF4E62ED2

Q24634746-3DA81C24-5CCC-4F73-AEF6-D107C7783DD5

P304

Q24634746-1EAC6330-62E6-43A1-B2FC-F38AB6E2B3C6

P31

Q24634746-69E36962-E242-4792-8A22-974BD9736F56

P3181

Q24634746-6A7751C3-C338-44EC-B22C-17069A72449F

P356

Q24634746-EA15F5F0-44D9-4248-A648-2BDFC67DAFC2

P407

Q24634746-5F76881D-5C40-4978-820D-9766936CFB28

P433

Q24634746-BD21FEA1-73D9-4BC2-BF1B-1A52DFB3B493

P478

Q24634746-BF32B327-93D3-4FD8-BA48-F8ABD600DD28

P577

Q24634746-FCE5D8E4-89A4-44B2-B7CA-14A2DBECB742

P698

Q24634746-90422B6F-1172-4209-B7C0-46619D984FD7

P921

Q24634746-1EAE25DB-78AD-4702-8D05-06B8A4F0F846

P932

Q24634746-6959F5C9-26FD-4D17-A495-C41A7CB794E4

P3181

P356

JBC.M111.287490

P1433

Journal of Biological Chemistry

P1476

Activation of extracellular transglutaminase 2 by thioredoxin

@en

P2093

Chaitan Khosla

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

Cornelius Klöck

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

Jorunn Stamnaes

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

Ludvig M Sollid

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

Thomas R DiRaimondo

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

Xi Jin

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

P2860

Transglutaminase 2 undergoes a large conformational change upon activation

TRPC channel activation by extracellular thioredoxin

Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity

Transglutaminase 2: an enigmatic enzyme with diverse functions

Structural basis for gluten intolerance in celiac sprue

Mechanism of allosteric regulation of transglutaminase 2 by GTP.

Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif.

The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma

Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.

Identification of human thioredoxin as a novel IFN-gamma-induced factor: mechanism of induction and its role in cytokine production.

P304

37866-73

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

P31

scholarly article

P3181

3179592

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

P356

10.1074/JBC.M111.287490

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

P407

P433

43

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

P478

286

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

P577

2011-10-28T00:00:00Z

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

P698

21908620

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

P921

P932

3199528

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