Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme

Biochemical and Biophysical Research Communications

Volumn 339, Issue 2, 2006, Pages 520-525

  Machado, M F M ^a,b   Cunha, F M ^b,c   Berti, D A ^c   Heimann, A S ^d   Klitzke, C F ^e   Rioli, V ^e   Oliveira, V ^a   Ferro, E S ^c  

^a MASTERS AND DOCTORAL PROGRAMS IN PHYSICAL THERAPY   (Brazil)

^b FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^c UNIVERSITY OF SÃO PAULO   (Brazil)

^d Proteimax Biotechnology LTDA   (Brazil)

^e INSTITUTO BUTANTAN   (Brazil)

Author keywords

Intracellular peptide metabolism; Neurolysin; Peptidase; Phosphorylation; Proteasome; Thimet oligopeptidase

Indexed keywords

CELL PROTEIN; DIPEPTIDYL CARBOXYPEPTIDASE; ENZYME INHIBITOR; NEUROLYSIN; PEPTIDE; THIMET OLIGOPEPTIDASE;

ARTICLE; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; HYDROLYSIS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PEPTIDYL-DIPEPTIDASE A; PHOSPHORYLATION; SUBSTRATE SPECIFICITY;

EID: 28444435236     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.11.041     Document Type: Article

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