Removal of acidic residues of the prodomain of PCSK9 increases its activity towards the LDL receptor

Biochemical and Biophysical Research Communications

Volumn 406, Issue 2, 2011, Pages 234-238

  Holla, Øystein L ^a   Laerdahl, Jon K ^b   Strøm, Thea Bismo ^a   Tveten, Kristian ^a   Cameron, Jamie ^a   Berge, Knut Erik ^a   Leren, Trond P ^a  

^a UNIVERSITY OF OSLO   (Norway)

^b OSLO UNIVERSITY HOSPITAL   (Norway)

Author keywords

Cholesterol; LDL receptor; Mutagenesis; PCSK9; Prodomain

Indexed keywords

AMINO ACID; HISTIDINE; LOW DENSITY LIPOPROTEIN RECEPTOR; PROPROTEIN CONVERTASE SUBTILISIN KEXIN TYPE 9; SERINE PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; HUMAN; HUMAN CELL; INHIBITION KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE; CONSERVED SEQUENCE; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, LDL; SEQUENCE DELETION; SERINE ENDOPEPTIDASES;

EID: 79952454325     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.02.023     Document Type: Article

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