Peptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors

Chemistry and Biology

Volumn 18, Issue 1, 2011, Pages 48-57

  Brown, Christopher M ^a   Ray, Manisha ^a   Eroy Reveles, Aura A ^a   Egea, Pascal ^b,c   Tajon, Cheryl ^a   Craik, Charles S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PEPTIDE HYDROLASE; PHOSPHONIC ACID DERIVATIVE; PROTEINASE INHIBITOR; SERINE PROTEINASE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DESIGN; ENZYME ACTIVE SITE; HUMAN; METABOLISM; STAINING; STRUCTURE ACTIVITY RELATION; SYNTHESIS; TUMOR CELL LINE;

CATALYTIC DOMAIN; CELL LINE, TUMOR; DRUG DESIGN; HUMANS; MODELS, MOLECULAR; PEPTIDE HYDROLASES; PEPTIDES; PHOSPHONIC ACIDS; PROTEASE INHIBITORS; SERINE ENDOPEPTIDASES; SERINE PROTEASES; STAINING AND LABELING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 79251537480     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.11.007     Document Type: Article

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