about
Transglutaminase 2 undergoes a large conformational change upon activationSerotonylation of vascular proteins important to contractionCeliac disease: prevalence, diagnosis, pathogenesis and treatmentNon-dietary forms of treatment for adult celiac diseaseCross linking to tissue transglutaminase and collagen favours gliadin toxicity in coeliac diseaseMethods to Design and Synthesize Antibody-Drug Conjugates (ADCs)Microbial transglutaminase and its application in the food industry. A reviewEnvironment, dysbiosis, immunity and sex-specific susceptibility: a translational hypothesis for regressive autism pathogenesisTransglutaminase 2-mediated serotonylation in pulmonary hypertensionStructure of the catalytic domain of theSalmonellavirulence factor SseITransglutaminase 2 has opposing roles in the regulation of cellular functions as well as cell growth and deathMolecular Cues Guiding Matrix Stiffness in Liver FibrosisCharacterization of periphilin, a widespread, highly insoluble nuclear protein and potential constituent of the keratinocyte cornified envelopeCirculating autoantibodies in patients with aspirin-intolerant asthma: an epiphenomenon related to airway inflammationCellular functions of tissue transglutaminasePhysiological, pathological, and structural implications of non-enzymatic protein-protein interactions of the multifunctional human transglutaminase 2Role of transglutaminase 2 in celiac disease pathogenesisActivation and inhibition of transglutaminase 2 in miceUsing FLIM-FRET to measure conformational changes of transglutaminase type 2 in live cellsGliadin peptides induce tissue transglutaminase activation and ER-stress through Ca2+ mobilization in Caco-2 cellsIdentification of a highly reactive substrate peptide for transglutaminase 6 and its use in detecting transglutaminase activity in the skin epidermisA fluorescence-based array screen for transglutaminase substrates.Creating site-specific isopeptide linkages between proteins with the traceless Staudinger ligation.Effects of the regulatory ligands calcium and GTP on the thermal stability of tissue transglutaminase.A novel extracellular role for tissue transglutaminase in matrix-bound VEGF-mediated angiogenesis.Plasma membrane factor XIIIA transglutaminase activity regulates osteoblast matrix secretion and deposition by affecting microtubule dynamics.Site-specific protein propargylation using tissue transglutaminase.Characterization of sea urchin transglutaminase, a protein regulated by guanine/adenine nucleotides.Characterizing monoclonal antibody epitopes by filtered gene fragment phage display.Screening for transglutaminase-catalyzed modifications by peptide mass finger printing using multipoint recalibration on recognized peaks for high mass accuracyScreening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGASE 2 and Factor XIIIA.Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury.Identification of preferred substrate sequences for transglutaminase 1--development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin.Intracellular localization and conformational state of transglutaminase 2: implications for cell death.Identification of a preferred substrate peptide for transglutaminase 3 and detection of in situ activity in skin and hair follicles.Screening of substrate peptide sequences for tissue-type transglutaminase (TGase 2) using T7 phage cDNA library.Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival.Differential alternative splicing of human transglutaminase 4 in benign prostate hyperplasia and prostate cancer.Rapid interactome profiling by massive sequencing
P2860
Q21092747-B01AE012-795B-49A9-98FE-D2C937151E2FQ21562428-5DDEDADD-A790-4109-8462-51E95F60469FQ22305490-83BEA99D-16E7-4070-AFC9-17BAA3074F06Q24602271-CE4F06F4-0C6A-4882-BE8D-0F0CC0944B89Q24680243-73CA2A82-7789-448D-A7B9-71F15E3CB1B5Q26768654-09E7F755-B43E-494F-9217-E10ABED372BFQ26822636-3ABC1F08-BDB4-4B9A-AADC-A34C3F368C10Q27024805-42A1434B-57B0-4339-94DA-64D5619D69AEQ27027862-2EB61FB4-6DFA-4782-BE43-6DD081F4DCF0Q27675137-844CA972-CC1E-48F3-8475-F3837CEDC988Q28069852-43334522-65EB-48D6-89A8-0B332F3632B1Q28077583-511F9A5E-D150-4632-BFAA-4390BB1D604CQ28186267-0BBBA570-FC31-4BD9-AF30-E9E46890296BQ28219147-A1B56315-0EDA-4127-9B67-58D5812ABA67Q28260600-5757617B-F564-4A38-8426-54D258BF85A4Q28261578-C4C3C018-3DE2-42F1-9434-D527BCA3527FQ28262529-69FDCB91-35B7-4B3B-8D9C-6C3D7463E50CQ28480486-148FA46A-195B-4369-8100-AB29930456D1Q28483257-A0652C28-DA44-47CC-BE5F-3FD131048570Q28484010-24BD26B5-21A0-4F48-9367-A3B5986BC313Q28591287-651CB760-667E-4F5A-A0B3-B8D33E4BDEB8Q30316575-E0E553B0-1996-40A9-AEE3-6AD8F45ACEBAQ30371033-AD6C0100-A320-4EAD-9114-4A4C155F8400Q30404253-5B8E094E-71A8-42A6-B6DC-AC06F4268B62Q30547848-1DA93BD4-2708-45B2-AC0F-848679F39D86Q30997344-114433A4-E867-431A-8EAC-4E39A8D5DE7EQ31063390-B237C38C-0122-4E48-936A-85449AAAF7F9Q31114157-76E56E9C-B590-422B-AF5A-2D762351A090Q33212053-3EEDA4EB-02D5-431B-9DE7-B0D8CF77BB9AQ33233251-F3F734C3-F494-4320-960E-79E6CE735655Q33240965-1F239A70-DF6B-44D9-A30A-2011BC9B190FQ33262164-2C1F2C31-951A-421C-8B76-AE40CBD3E6E1Q33325485-7AC478D6-C10F-44D2-9D41-BD98E861ABA7Q33380424-D948116A-4893-472A-B894-BF6CE61C3BFFQ33476870-A3FBCA5F-445D-41FB-BBA4-0C6FD334E6A3Q33660874-8CA51B3E-55CE-4190-8A8A-F262BC26BD9BQ33701867-C969D818-5C3A-4D55-AED2-995CFEF4096BQ33728989-FD10C4A7-A732-49D4-B1D8-08D4E228C2B1Q33809160-7B97314E-CCEF-4951-9BBF-C7C96D4DE88BQ33871179-941AECA7-D796-4743-B0D0-900949100A33
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Transglutaminases: nature's biological glues
@ast
Transglutaminases: nature's biological glues
@en
Transglutaminases: nature's biological glues
@en-gb
Transglutaminases: nature's biological glues
@nl
type
label
Transglutaminases: nature's biological glues
@ast
Transglutaminases: nature's biological glues
@en
Transglutaminases: nature's biological glues
@en-gb
Transglutaminases: nature's biological glues
@nl
prefLabel
Transglutaminases: nature's biological glues
@ast
Transglutaminases: nature's biological glues
@en
Transglutaminases: nature's biological glues
@en-gb
Transglutaminases: nature's biological glues
@nl
P2860
P3181
P356
P1433
P1476
Transglutaminases: nature's biological glues
@en
P2093
Carlo M Bergamini
P2860
P304
P3181
P356
10.1042/BJ20021234
P407
P577
2002-12-01T00:00:00Z