Structural elements responsible for transglutaminase activity of protein disulphide isomerases and thioredoxins

Journal of Biological Regulators and Homeostatic Agents

Volumn 18, Issue 1, 2004, Pages 1-8

  Blasko B ^a   Madi A ^b   Fésüs, László ^a,b  

^a UNIVERSITY OF DEBRECEN   (Hungary)

^b UNIVERSITY OF DEBRECEN   (Hungary)

Author keywords

3D structure; Catalytic residues; Protein disulphide isomerase; Thioredoxin; Transglutaminase

Indexed keywords

AMINE; AMINO ACID; ASPARAGINE; CYSTEINE; GLUTAMINE; HISTIDINE; PROTEIN DISULFIDE ISOMERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; THIOREDOXIN;

AMINO ACID SEQUENCE; ARTICLE; CAENORHABDITIS ELEGANS; CELL FUNCTION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENETIC CONSERVATION; HUMAN; MOLECULAR BIOLOGY; NONHUMAN; PROTEIN BINDING; PROTEIN FAMILY; REGULATORY MECHANISM; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 4444365411     PISSN: 0393974X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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