Ste24p mediates proteolysis of both isoprenylated and non-prenylated oligopeptides

Journal of Biological Chemistry

Volumn 291, Issue 27, 2016, Pages 14185-14198

  Hildebrandt, Emily R ^a   Arachea, Buenafe T ^b   Wiene, Michael C ^b   Schmidt, Walter K ^a  

^a University of Georgia   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; ENZYME KINETICS; MASS SPECTROMETRY; PEPTIDES; SUBSTRATES;

CLEAVAGE PREFERENCE; CLEAVAGE SITES; INTEGRAL MEMBRANE PROTEINS; MASS SPECTROSCOPY; METALLOPROTEASES; OLIGOPEPTIDES; SUBSTRATE PROFILE; SUBSTRATE RECOGNITION;

PROTEINS;

AMYLOID BETA PROTEIN; M16A PROTEIN; MEMBRANE PROTEIN; OLIGOPEPTIDE; PROTEINASE; RCE1P PROTEIN; STE24P PROTEIN; UNCLASSIFIED DRUG; METALLOPROTEINASE; SACCHAROMYCES CEREVISIAE PROTEIN; STE24 PROTEIN, S CEREVISIAE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; IN VITRO STUDY; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN FUNCTION; STEADY STATE; STRUCTURE ANALYSIS; METABOLISM; PROTEIN PRENYLATION;

MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; OLIGOPEPTIDES; PROTEIN PRENYLATION; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84976867203     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.718197     Document Type: Article

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