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FEBS Journal, ISSN 1742-464X, 12/2009, Volume 276, Issue 23, pp. 7083 - 7096
Journal Article
Cancer research, ISSN 0008-5472, 05/2018, Volume 78, Issue 10, pp. 2775 - 2775
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2640 - 2649
Transglutaminase 2 (TG2) is a ubiquitously expressed, intracellular as well as extracellular protein with multiple modes of post-translational regulation,... 
SELECTIVE-INHIBITION | HUMAN THIOREDOXIN-1 | ACTIVE-SITE | THROMBUS FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISOMERASE | THIOL-DISULFIDE EXCHANGE | EXTRACELLULAR-MATRIX | QUIESCIN-SULFHYDRYL OXIDASE | TISSUE TRANSGLUTAMINASE | CELIAC-DISEASE | Enzymes, Immobilized - metabolism | Oxidants - pharmacology | Human Umbilical Vein Endothelial Cells - metabolism | Membrane Glycoproteins - metabolism | Glutathione - metabolism | Protein Disulfide-Isomerases - metabolism | GTP-Binding Proteins - antagonists & inhibitors | Humans | Membrane Glycoproteins - chemistry | Oxidants - metabolism | Extracellular Matrix - metabolism | Transglutaminases - genetics | Protein Disulfide-Isomerases - antagonists & inhibitors | Protein Transport - drug effects | GTP-Binding Proteins - genetics | Thioredoxins - genetics | Oxidoreductases Acting on Sulfur Group Donors - chemistry | Protein Processing, Post-Translational - drug effects | RNA Interference | Biocatalysis - drug effects | Human Umbilical Vein Endothelial Cells - cytology | Thioredoxins - metabolism | Peptide Fragments - genetics | Transglutaminases - antagonists & inhibitors | Transglutaminases - chemistry | Allosteric Regulation - drug effects | Oxidoreductases Acting on Sulfur Group Donors - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | GTP-Binding Proteins - chemistry | Oxidation-Reduction | Extracellular Matrix - drug effects | Cells, Cultured | Hydrogen Peroxide - pharmacology | Recombinant Proteins - chemistry | Membrane Glycoproteins - genetics | Extracellular Matrix - enzymology | Peptide Fragments - chemistry | Protein Disulfide-Isomerases - genetics | Human Umbilical Vein Endothelial Cells - enzymology | Cystine - metabolism | Transglutaminases - metabolism | Oxidoreductases Acting on Sulfur Group Donors - genetics | Enzymes, Immobilized - antagonists & inhibitors | GTP-Binding Proteins - metabolism | Index Medicus | Editors' Picks | post-translational modification (PTM) | PDIA3 | transglutaminase | thioredoxin | disulfide | oxidation-reduction (redox) | ERp57 | redox switch | celiac disease | transglutaminase 2 | protein disulfide isomerase family A member 3
Journal Article
Food Research International, ISSN 0963-9969, 11/2019, Volume 125, p. 108577
were encapsulated by complex coacervation followed by transglutaminase crosslinking, aiming to improve the resistance of the microcapsules and improve the... 
Probiotics | Microencapsulation | Transglutaminase
Journal Article
Oncogene, ISSN 0950-9232, 05/2017, Volume 36, Issue 21, pp. 2981 - 2990
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 48, pp. 17146 - 17151
The multifunctional enzyme transglutaminase 2 (TG2) is the target of autoantibodies in the gluten-sensitive enteropathy celiac disease. In addition, the enzyme... 
Proteins | Deuterium | Celiac disease | Enzymes | Autoantibodies | Active sites | Disulfides | Antibodies | Oxidation | Epitopes | celiac disease | transglutaminase 2 | autoantibodies | hydrogen/deuterium exchange | CALCIUM-IONS | MULTIDISCIPLINARY SCIENCES | BINDING-PROTEIN | CROSS-LINKING | GTP-BINDING | CELIAC-DISEASE | PROTEIN DYNAMICS | FIBRONECTIN | TISSUE TRANSGLUTAMINASE | HYDROGEN-EXCHANGE | APOPTOSIS IN-VITRO | Disulfides - metabolism | Autoantibodies - metabolism | Epitopes - metabolism | Calcium - metabolism | Humans | Molecular Sequence Data | Transglutaminases - genetics | Intestines - metabolism | Calcium - chemistry | GTP-Binding Proteins - genetics | Intestines - immunology | Transglutaminases - immunology | Epitopes - immunology | Celiac Disease - immunology | Disulfides - chemistry | Epitope Mapping - methods | Plasma Cells - metabolism | Transglutaminases - chemistry | Protein Structure, Tertiary | Intestines - pathology | GTP-Binding Proteins - chemistry | GTP-Binding Proteins - immunology | Electrophoresis, Polyacrylamide Gel | Models, Molecular | Binding Sites - genetics | Deuterium Exchange Measurement - methods | Celiac Disease - pathology | Autoantibodies - immunology | Protein Binding | Epitopes - chemistry | Mutation | Mass Spectrometry - methods | Celiac Disease - metabolism | Plasma Cells - immunology | Transglutaminases | Hydrogen | Health aspects | Molecules | Peptides | Pathogenesis | T cell receptors | Mass spectrometry | Index Medicus | Biological Sciences | hydrogen | deuterium exchange
Journal Article
JAMA Pediatrics, ISSN 2168-6203, 05/2018, Volume 172, Issue 5, pp. 497 - 497
Journal Article
Journal Article