Autor/Autorin: Gatta Nicola Gaetano
Dr. Gentile is a recognized expert in the Transglutaminase (TG) enzymes research area and has a strong background in the molecular biology and biochemical aspects of the TG enzymes expression, activity and function. Part of his work has been focused to the TG2 characterization in normal and pathological cellular events.
Transglutaminase 2 (TG2, "tissue” TG) belongs to the family of the Transglutaminase (TG) enzymes, which catalyse post-translational modifications of proteins, such as the cross linking of a glutaminyl residue of a protein/peptide substrate to a lysyl residue of a protein/peptide co-substrate with the formation of an N-gamma-(epsilon-L-glutamyl)-L-lysine [GGEL] cross link (isopeptidic bond) and the concomitant release of ammonia.
Transglutaminase 2 (TG2, "tissue" TG) belongs to the family of the Transglutaminase (TG) enzymes, which catalyse post-translational modifications of proteins, such as the cross linking of a glutaminyl residue of a protein/peptide substrate to a lysyl residue of a protein/peptide co-substrate with the formation of an N-gamma-(epsilon-L-glutamyl)-L-lysine [GGEL] cross link (isopeptidic bond) and the concomitant release of ammonia.
Gatta, Nicola Gaetano
Dr. Gentile is a recognized expert in the Transglutaminase (TG) enzymes research area and has a strong background in the molecular biology and biochemical aspects of the TG enzymes expression, activity and function. Part of his work has been focused to the TG2 characterization in normal and pathological cellular events.
Über den Autor
Dr. Gentile is a recognized expert in the Transglutaminase (TG) enzymes research area and has a strong background in the molecular biology and biochemical aspects of the TG enzymes expression, activity and function. Part of his work has been focused to the TG2 characterization in normal and pathological cellular events.
Klappentext
Transglutaminase 2 (TG2, ¿tissue¿ TG) belongs to the family of the Transglutaminase (TG) enzymes, which catalyse post-translational modifications of proteins, such as the cross linking of a glutaminyl residue of a protein/peptide substrate to a lysyl residue of a protein/peptide co-substrate with the formation of an N-gamma-(epsilon-L-glutamyl)-L-lysine [GGEL] cross link (isopeptidic bond) and the concomitant release of ammonia.
