Structure, biological activity and membrane partitioning of analogs of the isoprenylated a-factor mating peptide of Saccharomyces cerevisiae

Journal of Peptide Research

Volumn 55, Issue 5, 2000, Pages 372-383

  Xie, H ^a   Becker, J M ^b   Gibbs, R A ^c   Naider, F ^a  

^a CITY UNIVERSITY OF NEW YORK   (United States)

^b UNIVERSITY OF TENNESSEE   (United States)

^c WAYNE STATE UNIVERSITY   (United States)

Author keywords

A factor; Farnesylation; Lipopeptide; Membrane partitioning; Peptide pheromones

Indexed keywords

LIPOPEPTIDE; MATING HORMONE ALPHA FACTOR; PHEROMONE; SYNTHETIC PEPTIDE;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SACCHAROMYCES CEREVISIAE; YEAST;

CELL DIVISION; CELL MEMBRANE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; MODELS, CHEMICAL; PEPTIDE BIOSYNTHESIS; PEPTIDES; PHEROMONES; PROTEIN BINDING; PROTEIN ISOPRENYLATION; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

EID: 0034070171     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2000.00705.x     Document Type: Article

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