Journal of Biological Chemistry, ISSN 0021-9258, 08/2001, Volume 276, Issue 35, pp. 33066 - 33078
We isolated and characterized the gene encoding human transglutaminase (TG)(X) (TGM5) and mapped it to the 15q15.2 region of chromosome 15 by fluorescence in...
TRANSCRIPTION FACTORS | MURINE PALLID MUTATION | AMINO-ACID-SEQUENCE | PROSTATE-SPECIFIC TRANSGLUTAMINASE | KERATINOCYTE TRANSGLUTAMINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FACTOR-XIII | CROSS-LINKING | BLOOD-COAGULATION FACTOR | HUMAN ERYTHROCYTE PROTEIN-4.2 | TISSUE TRANSGLUTAMINASE | Cytoskeletal Proteins | Protein Subunits | Multigene Family | Molecular Weight | Alternative Splicing | Humans | Genomic Library | Molecular Sequence Data | Transglutaminases - genetics | Male | 5' Untranslated Regions - genetics | Phylogeny | Genetic Variation | Blood Proteins - genetics | Base Sequence | Polymerase Chain Reaction | Female | Fetus | Transcription, Genetic | Transglutaminases - chemistry | Amino Acid Sequence | Protein Structure, Secondary | Introns | Isoenzymes - genetics | Chromosome Mapping | Genetic Markers | Membrane Proteins | Vertebrates | Blotting, Northern | Animals | Chromosomes, Human, Pair 15 | Invertebrates | Evolution, Molecular
TRANSCRIPTION FACTORS | MURINE PALLID MUTATION | AMINO-ACID-SEQUENCE | PROSTATE-SPECIFIC TRANSGLUTAMINASE | KERATINOCYTE TRANSGLUTAMINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FACTOR-XIII | CROSS-LINKING | BLOOD-COAGULATION FACTOR | HUMAN ERYTHROCYTE PROTEIN-4.2 | TISSUE TRANSGLUTAMINASE | Cytoskeletal Proteins | Protein Subunits | Multigene Family | Molecular Weight | Alternative Splicing | Humans | Genomic Library | Molecular Sequence Data | Transglutaminases - genetics | Male | 5' Untranslated Regions - genetics | Phylogeny | Genetic Variation | Blood Proteins - genetics | Base Sequence | Polymerase Chain Reaction | Female | Fetus | Transcription, Genetic | Transglutaminases - chemistry | Amino Acid Sequence | Protein Structure, Secondary | Introns | Isoenzymes - genetics | Chromosome Mapping | Genetic Markers | Membrane Proteins | Vertebrates | Blotting, Northern | Animals | Chromosomes, Human, Pair 15 | Invertebrates | Evolution, Molecular
Journal Article
Physiological Reviews, ISSN 0031-9333, 2014, Volume 94, Issue 2, pp. 383 - 417
Transglutaminases (TGs) are multifunctional proteins having enzymatic and scaffolding functions that participate in regulation of cell fate in a wide range of...
EPITHELIAL-MESENCHYMAL TRANSITION | GH-ALPHA/TISSUE TRANSGLUTAMINASE-2 | PHYSIOLOGY | GUANINE-NUCLEOTIDE-BINDING | FACTOR-XIII-A | RECESSIVE LAMELLAR ICHTHYOSIS | HEPARAN-SULFATE PROTEOGLYCANS | NF-KAPPA-B | CHONDROCYTE HYPERTROPHIC DIFFERENTIATION | VASCULAR SMOOTH-MUSCLE | TISSUE-TYPE TRANSGLUTAMINASE | Gene Expression Regulation, Enzymologic | Animals | Signal Transduction | Humans | Transglutaminases - metabolism | Neoplasms - enzymology | Transglutaminases - genetics | Transcription, Genetic | Cell Differentiation | Neoplasms - pathology | Cell physiology | Cellular signal transduction | Transglutaminases | Genetic aspects | Research | Analysis | Reviews
EPITHELIAL-MESENCHYMAL TRANSITION | GH-ALPHA/TISSUE TRANSGLUTAMINASE-2 | PHYSIOLOGY | GUANINE-NUCLEOTIDE-BINDING | FACTOR-XIII-A | RECESSIVE LAMELLAR ICHTHYOSIS | HEPARAN-SULFATE PROTEOGLYCANS | NF-KAPPA-B | CHONDROCYTE HYPERTROPHIC DIFFERENTIATION | VASCULAR SMOOTH-MUSCLE | TISSUE-TYPE TRANSGLUTAMINASE | Gene Expression Regulation, Enzymologic | Animals | Signal Transduction | Humans | Transglutaminases - metabolism | Neoplasms - enzymology | Transglutaminases - genetics | Transcription, Genetic | Cell Differentiation | Neoplasms - pathology | Cell physiology | Cellular signal transduction | Transglutaminases | Genetic aspects | Research | Analysis | Reviews
Journal Article
Bioconjugate Chemistry, ISSN 1043-1802, 05/2014, Volume 25, Issue 5, pp. 855 - 862
Although microbial transglutaminases (mTGs) were initially discovered to offset the cost of producing mammalian transglutaminases for food applications, they...
CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CROSS-LINKING | CHEMISTRY, ORGANIC | CHEMICAL-MODIFICATION | STREPTOMYCES-MOBARAENSIS | CHEMISTRY, MULTIDISCIPLINARY | CELIAC-DISEASE | THERAPEUTIC INDEX | HUMAN GROWTH-HORMONE | RECOMBINANT PROTEINS | PROTEIN MODIFICATION | TISSUE TRANSGLUTAMINASE | Neoplasms - metabolism | Biotechnology | Antibodies - metabolism | Antibodies - chemistry | Substrate Specificity | Antineoplastic Agents - therapeutic use | DNA - metabolism | Antineoplastic Agents - chemistry | Neoplasms - drug therapy | Antineoplastic Agents - metabolism | DNA - chemistry | Transglutaminases - metabolism | Polymers - chemistry | Streptomyces - enzymology | Polymers - metabolism | Transglutaminases - chemistry
CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CROSS-LINKING | CHEMISTRY, ORGANIC | CHEMICAL-MODIFICATION | STREPTOMYCES-MOBARAENSIS | CHEMISTRY, MULTIDISCIPLINARY | CELIAC-DISEASE | THERAPEUTIC INDEX | HUMAN GROWTH-HORMONE | RECOMBINANT PROTEINS | PROTEIN MODIFICATION | TISSUE TRANSGLUTAMINASE | Neoplasms - metabolism | Biotechnology | Antibodies - metabolism | Antibodies - chemistry | Substrate Specificity | Antineoplastic Agents - therapeutic use | DNA - metabolism | Antineoplastic Agents - chemistry | Neoplasms - drug therapy | Antineoplastic Agents - metabolism | DNA - chemistry | Transglutaminases - metabolism | Polymers - chemistry | Streptomyces - enzymology | Polymers - metabolism | Transglutaminases - chemistry
Journal Article
Trends in Pharmacological Sciences, ISSN 0165-6147, 2014, Volume 36, Issue 1, pp. 32 - 40
Highlights • Recent irreversible TG2 inhibitors represent privileged ‘warheads’. • Recent reversible TG2 inhibitors are presented according to putative binding...
Advanced Basic Science | irreversible inhibitor | enzyme inhibition | reversible inhibitor | tissue transglutaminase | TG2 | cross-link | Enzyme inhibition | Tissue transglutaminase | Irreversible inhibitor | Cross-link | Reversible inhibitor | IRREVERSIBLE INHIBITORS | ACTIVE-SITE | BETA-AMINOETHYL KETONES | ALPHA,BETA-UNSATURATED AMIDES | CELIAC-DISEASE | GAMMA-GLUTAMYL-TRANSPEPTIDASE | CONFORMATIONAL-CHANGES | PIG LIVER TRANSGLUTAMINASE | PHARMACOLOGY & PHARMACY | CATALYZED CROSS-LINKING | HUNTINGTONS-DISEASE | Animals | Humans | Transglutaminases - metabolism | Enzyme Inhibitors - pharmacology | Protein Conformation | Enzyme Inhibitors - therapeutic use | Transglutaminases - antagonists & inhibitors | Transglutaminases - chemistry
Advanced Basic Science | irreversible inhibitor | enzyme inhibition | reversible inhibitor | tissue transglutaminase | TG2 | cross-link | Enzyme inhibition | Tissue transglutaminase | Irreversible inhibitor | Cross-link | Reversible inhibitor | IRREVERSIBLE INHIBITORS | ACTIVE-SITE | BETA-AMINOETHYL KETONES | ALPHA,BETA-UNSATURATED AMIDES | CELIAC-DISEASE | GAMMA-GLUTAMYL-TRANSPEPTIDASE | CONFORMATIONAL-CHANGES | PIG LIVER TRANSGLUTAMINASE | PHARMACOLOGY & PHARMACY | CATALYZED CROSS-LINKING | HUNTINGTONS-DISEASE | Animals | Humans | Transglutaminases - metabolism | Enzyme Inhibitors - pharmacology | Protein Conformation | Enzyme Inhibitors - therapeutic use | Transglutaminases - antagonists & inhibitors | Transglutaminases - chemistry
Journal Article
Autoimmunity Reviews, ISSN 1568-9972, 2016, Volume 15, Issue 12, pp. 1111 - 1119
Abstract Microbial transglutaminase (mTg) is capable of cross-linking numerous molecules. It is a family member of human tissue transglutaminase (tTg),...
Allergy and Immunology | Celiac disease | Microbial transglutaminase | Immunogenic | Tissue transglutaminase | Antibodies | Immunoreactivity | Food additive | Food processing | AUTOANTIBODIES | ANTIGLIADIN | DIAGNOSIS | GLIADIN | IGA | IMMUNOLOGY | GLUTEN | ENDOMYSIAL ANTIBODIES | Viral antibodies | Enzymes | Analysis | Food additives | Antigenic determinants | Monoglycerides
Allergy and Immunology | Celiac disease | Microbial transglutaminase | Immunogenic | Tissue transglutaminase | Antibodies | Immunoreactivity | Food additive | Food processing | AUTOANTIBODIES | ANTIGLIADIN | DIAGNOSIS | GLIADIN | IGA | IMMUNOLOGY | GLUTEN | ENDOMYSIAL ANTIBODIES | Viral antibodies | Enzymes | Analysis | Food additives | Antigenic determinants | Monoglycerides
Journal Article
2012, International Review of Cell and Molecular Biology, ISBN 9780123943057, Volume 294, 97
Transglutaminase 2 (TG2 or tissue transglutaminase) is a highly complex multifunctional protein that acts as transglutaminase, GTPase/ATPase, protein disulfide...
Stem cells | Transamidation | Transglutaminase | GTPase | Cell signaling | Therapeutic target | Protein cross-linking | GTP-BINDING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDUCED NEURONAL DIFFERENTIATION | HUMAN-ERYTHROCYTE TRANSGLUTAMINASE | VASCULAR SMOOTH-MUSCLE | CELL BIOLOGY | GH-ALPHA/TISSUE TRANSGLUTAMINASE-2 | GUANINE-NUCLEOTIDE-BINDING | EPIDERMAL-GROWTH-FACTOR | HEPARAN-SULFATE PROTEOGLYCANS | CHONDROCYTE HYPERTROPHIC DIFFERENTIATION | PANCREATIC-CANCER CELLS | Humans | Transglutaminases - genetics | Cell Enlargement | Gene Expression Regulation, Enzymologic - physiology | Cell Movement - physiology | Cell Compartmentation - physiology | Extracellular Matrix - enzymology | Animals | Cell Adhesion - physiology | Transglutaminases - metabolism | Apoptosis - physiology | GTP-Binding Proteins | Cell Differentiation - physiology | Cell Survival - physiology
Stem cells | Transamidation | Transglutaminase | GTPase | Cell signaling | Therapeutic target | Protein cross-linking | GTP-BINDING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDUCED NEURONAL DIFFERENTIATION | HUMAN-ERYTHROCYTE TRANSGLUTAMINASE | VASCULAR SMOOTH-MUSCLE | CELL BIOLOGY | GH-ALPHA/TISSUE TRANSGLUTAMINASE-2 | GUANINE-NUCLEOTIDE-BINDING | EPIDERMAL-GROWTH-FACTOR | HEPARAN-SULFATE PROTEOGLYCANS | CHONDROCYTE HYPERTROPHIC DIFFERENTIATION | PANCREATIC-CANCER CELLS | Humans | Transglutaminases - genetics | Cell Enlargement | Gene Expression Regulation, Enzymologic - physiology | Cell Movement - physiology | Cell Compartmentation - physiology | Extracellular Matrix - enzymology | Animals | Cell Adhesion - physiology | Transglutaminases - metabolism | Apoptosis - physiology | GTP-Binding Proteins | Cell Differentiation - physiology | Cell Survival - physiology
Book Chapter
Journal of Medicinal Chemistry, ISSN 0022-2623, 05/2018, Volume 61, Issue 10, pp. 4528 - 4560
Transglutaminase 2 (TGase 2)-catalyzed transamidation represents an important post-translational mechanism for protein modification with implications in...
CHEMISTRY, MEDICINAL | COVALENT INHIBITORS | HYDROGEN-BOND BASICITY | PIG LIVER TRANSGLUTAMINASE | IN-VITRO MODEL | STEM-CELL SURVIVAL | HUMAN TISSUE TRANSGLUTAMINASE | DRUG-LIKE MOLECULES | MESENCHYMAL TRANSITION | KINETIC CHARACTERIZATION | CELIAC-DISEASE | Lysine - analogs & derivatives | Catalytic Domain | GTP-Binding Proteins - antagonists & inhibitors | Humans | Enzyme Inhibitors - pharmacology | Models, Molecular | Structure-Activity Relationship | Pyridazines - chemistry | Tissue Distribution | Animals | Lysine - pharmacokinetics | Lysine - pharmacology | Enzyme Inhibitors - pharmacokinetics | Microsomes, Liver - drug effects | Protein Conformation | Mice | Microsomes, Liver - enzymology | Molecular Structure | Catalysis | Kinetics | Transglutaminases - antagonists & inhibitors
CHEMISTRY, MEDICINAL | COVALENT INHIBITORS | HYDROGEN-BOND BASICITY | PIG LIVER TRANSGLUTAMINASE | IN-VITRO MODEL | STEM-CELL SURVIVAL | HUMAN TISSUE TRANSGLUTAMINASE | DRUG-LIKE MOLECULES | MESENCHYMAL TRANSITION | KINETIC CHARACTERIZATION | CELIAC-DISEASE | Lysine - analogs & derivatives | Catalytic Domain | GTP-Binding Proteins - antagonists & inhibitors | Humans | Enzyme Inhibitors - pharmacology | Models, Molecular | Structure-Activity Relationship | Pyridazines - chemistry | Tissue Distribution | Animals | Lysine - pharmacokinetics | Lysine - pharmacology | Enzyme Inhibitors - pharmacokinetics | Microsomes, Liver - drug effects | Protein Conformation | Mice | Microsomes, Liver - enzymology | Molecular Structure | Catalysis | Kinetics | Transglutaminases - antagonists & inhibitors
Journal Article
BBA - Molecular Cell Research, ISSN 0167-4889, 02/2012, Volume 1823, Issue 2, pp. 406 - 419
Transglutaminase 2 (TG2) is the most widely distributed member of the transglutaminase family with almost all cell types in the body expressing TG2 to varying...
GTP | Transamidase | Calcium | Cell death | Transglutaminase 2 | Transcription regulation | GTP-BINDING PROTEIN | PROTEIN DISULFIDE-ISOMERASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | FACTOR-KAPPA-B | CELL BIOLOGY | RESPONSE ELEMENT | RETINOIC ACID | NEUROBLASTOMA SH-SY5Y CELLS | HUNTINGTONS-DISEASE | TISSUE-TYPE TRANSGLUTAMINASE | PANCREATIC-CANCER CELLS | Gene Duplication | Catalytic Domain | Cell Proliferation | GTP-Binding Proteins - chemistry | Cell Survival | Humans | Models, Molecular | Transglutaminases - genetics | Structure-Activity Relationship | GTP-Binding Proteins - genetics | GTP Phosphohydrolases - chemistry | Animals | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Transglutaminases - metabolism | Protein Conformation | Transcription, Genetic | Transglutaminases - chemistry | GTP-Binding Proteins - metabolism | Mitochondrial DNA | Cells
GTP | Transamidase | Calcium | Cell death | Transglutaminase 2 | Transcription regulation | GTP-BINDING PROTEIN | PROTEIN DISULFIDE-ISOMERASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | FACTOR-KAPPA-B | CELL BIOLOGY | RESPONSE ELEMENT | RETINOIC ACID | NEUROBLASTOMA SH-SY5Y CELLS | HUNTINGTONS-DISEASE | TISSUE-TYPE TRANSGLUTAMINASE | PANCREATIC-CANCER CELLS | Gene Duplication | Catalytic Domain | Cell Proliferation | GTP-Binding Proteins - chemistry | Cell Survival | Humans | Models, Molecular | Transglutaminases - genetics | Structure-Activity Relationship | GTP-Binding Proteins - genetics | GTP Phosphohydrolases - chemistry | Animals | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Transglutaminases - metabolism | Protein Conformation | Transcription, Genetic | Transglutaminases - chemistry | GTP-Binding Proteins - metabolism | Mitochondrial DNA | Cells
Journal Article
Cell Death and Disease, ISSN 2041-4889, 08/2015, Volume 6, Issue 8, pp. e1868 - e1868
Differentiation of preadipocytes to lipid storing adipocytes involves extracellular signaling pathways, matrix remodeling and cytoskeletal changes. A number of...
ACTIVATED RECEPTOR-GAMMA | FACTOR-I PREF-1 | INSULIN-RESISTANCE | GENE-EXPRESSION | DOWN-REGULATION | ADIPOCYTE DIFFERENTIATION | PPAR-GAMMA | CELL-ADHESION | TISSUE TRANSGLUTAMINASE | MECHANISMS LINKING OBESITY | CELL BIOLOGY | Phosphorylation | Embryo, Mammalian | GTP-Binding Proteins - deficiency | Actins - metabolism | Adipose Tissue, White - metabolism | Transglutaminases - genetics | Adipocytes - cytology | PPAR gamma - metabolism | GTP-Binding Proteins - genetics | Proto-Oncogene Proteins c-akt - genetics | Actins - genetics | Intercellular Signaling Peptides and Proteins - metabolism | Adipose Tissue, White - cytology | rho-Associated Kinases - metabolism | Cell Differentiation | CCAAT-Enhancer-Binding Proteins - genetics | Proto-Oncogene Proteins c-akt - metabolism | Adipogenesis - genetics | Fibroblasts - metabolism | PPAR gamma - genetics | CCAAT-Enhancer-Binding Proteins - metabolism | Signal Transduction | Gene Expression Regulation | Intercellular Signaling Peptides and Proteins - genetics | rho-Associated Kinases - genetics | Transglutaminases - deficiency | beta Catenin - metabolism | beta Catenin - genetics | Mice, Knockout | Protein Transport | Animals | Adipocytes - metabolism | Fibroblasts - cytology | Mice | Original
ACTIVATED RECEPTOR-GAMMA | FACTOR-I PREF-1 | INSULIN-RESISTANCE | GENE-EXPRESSION | DOWN-REGULATION | ADIPOCYTE DIFFERENTIATION | PPAR-GAMMA | CELL-ADHESION | TISSUE TRANSGLUTAMINASE | MECHANISMS LINKING OBESITY | CELL BIOLOGY | Phosphorylation | Embryo, Mammalian | GTP-Binding Proteins - deficiency | Actins - metabolism | Adipose Tissue, White - metabolism | Transglutaminases - genetics | Adipocytes - cytology | PPAR gamma - metabolism | GTP-Binding Proteins - genetics | Proto-Oncogene Proteins c-akt - genetics | Actins - genetics | Intercellular Signaling Peptides and Proteins - metabolism | Adipose Tissue, White - cytology | rho-Associated Kinases - metabolism | Cell Differentiation | CCAAT-Enhancer-Binding Proteins - genetics | Proto-Oncogene Proteins c-akt - metabolism | Adipogenesis - genetics | Fibroblasts - metabolism | PPAR gamma - genetics | CCAAT-Enhancer-Binding Proteins - metabolism | Signal Transduction | Gene Expression Regulation | Intercellular Signaling Peptides and Proteins - genetics | rho-Associated Kinases - genetics | Transglutaminases - deficiency | beta Catenin - metabolism | beta Catenin - genetics | Mice, Knockout | Protein Transport | Animals | Adipocytes - metabolism | Fibroblasts - cytology | Mice | Original
Journal Article
Amino Acids, ISSN 0939-4451, 1/2015, Volume 47, Issue 1, pp. 19 - 26
Neuroinflammatory processes seem to play a pivotal role in various chronic neurodegenerative diseases, characterized also by the pathogenetic accumulation of...
Life Sciences | Biochemistry, general | NF-κB | Analytical Chemistry | Life Sciences, general | Biochemical Engineering | Proteomics | Neurobiology | Neuroinflammation | Transglutaminase 2 | Microglia | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | AMYOTROPHIC-LATERAL-SCLEROSIS | IN-VITRO | NF-kappa B | TNF-ALPHA | NF-KAPPA-B | TISSUE TRANSGLUTAMINASE | HUNTINGTONS-DISEASE | EXPRESSION | BRAIN | Nervous System Diseases - enzymology | GTP-Binding Proteins - immunology | Humans | Microglia - enzymology | Transglutaminases - genetics | NF-kappa B - metabolism | Astrocytes - enzymology | Nervous System Diseases - genetics | GTP-Binding Proteins - genetics | Transglutaminases - immunology | Animals | Microglia - immunology | Astrocytes - immunology | NF-kappa B - genetics | Nervous System Diseases - immunology | Enzymes | Nervous system diseases | Crosslinked polymers | Multiple sclerosis | Alzheimer's disease | Neurological diseases | Proteins | Central nervous system | Amino acids | Activation | Stimuli
Life Sciences | Biochemistry, general | NF-κB | Analytical Chemistry | Life Sciences, general | Biochemical Engineering | Proteomics | Neurobiology | Neuroinflammation | Transglutaminase 2 | Microglia | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | AMYOTROPHIC-LATERAL-SCLEROSIS | IN-VITRO | NF-kappa B | TNF-ALPHA | NF-KAPPA-B | TISSUE TRANSGLUTAMINASE | HUNTINGTONS-DISEASE | EXPRESSION | BRAIN | Nervous System Diseases - enzymology | GTP-Binding Proteins - immunology | Humans | Microglia - enzymology | Transglutaminases - genetics | NF-kappa B - metabolism | Astrocytes - enzymology | Nervous System Diseases - genetics | GTP-Binding Proteins - genetics | Transglutaminases - immunology | Animals | Microglia - immunology | Astrocytes - immunology | NF-kappa B - genetics | Nervous System Diseases - immunology | Enzymes | Nervous system diseases | Crosslinked polymers | Multiple sclerosis | Alzheimer's disease | Neurological diseases | Proteins | Central nervous system | Amino acids | Activation | Stimuli
Journal Article