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Journal Article
Journal Article
Amino Acids, ISSN 0939-4451, 3/2017, Volume 49, Issue 3, pp. 605 - 614
... structure and increase protein stability. These clusters are located in intrinsically disordered regions and via short linear motifs influence interactions with TGM2 partners directly, or through post-translation modification... 
Life Sciences | Biochemistry, general | Analytical Chemistry | Life Sciences, general | Novel amino acid clusters | Biochemical Engineering | Proteomics | Neurobiology | Intrinsically disordered regions | Short linear motifs | Protein stability | Transglutaminase 2 | LOCALIZATION | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE | PREDICTION | SEQUENCE | REGIONS | PROTEIN-PHOSPHORYLATION | TISSUE TRANSGLUTAMINASE | BINDING | Phosphorylation | Humans | Amino Acids - chemistry | Crystallography, X-Ray | Isoenzymes - chemistry | Amino Acids - metabolism | Thermodynamics | Isoenzymes - metabolism | Databases, Protein | Protein Interaction Domains and Motifs | Transglutaminases - chemistry | Protein Structure, Tertiary | Protein Conformation, alpha-Helical | Catalytic Domain | GTP-Binding Proteins - chemistry | Models, Molecular | Glycosylation | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Protein Conformation, beta-Strand | Intrinsically Disordered Proteins - chemistry | Transglutaminases - metabolism | Protein Binding | Protein Processing, Post-Translational | Evolution, Molecular | GTP-Binding Proteins - metabolism | Intrinsically Disordered Proteins - metabolism | Enzymes | Analysis | Stem cells | Physiological aspects | Amino acids | Phylogeny | Molecular biology
Journal Article
Bioinformatics, ISSN 1367-4803, 4/2007, Volume 23, Issue 8, pp. 950 - 956
Journal Article
Journal Article