Caged protein prenyltransferase substrates: Tools for understanding protein prenylation

Chemical Biology and Drug Design

Volumn 72, Issue 3, 2008, Pages 171-181

  DeGraw, Amanda J ^a   Hast, Michael A ^b   Xu, Juhua ^a   Mullen, Daniel ^a   Beese, Lorena S ^b   Barany, George ^a   Distefano, Mark D ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

CAAX peptide; Caged substrate; Farnesyl; Isoprenoid diphosphate; Photorelease; Prenyltransferase; Protein prenylation

Indexed keywords

BETA (2 NITROBENZYL)FARNESYL DIPHOSPHATE; BETA 1 (4,5 DIMETHOXYNITROPHENYL)ETHYLFARNESYL DIPHOSPHATE; DIMETHYLALLYLTRANSFERASE; FARNESYL DIPHOSPHATE; GERANYLGERANYL PYROPHOSPHATE; ISOPRENOID DIPHOSPHATE; PROTEIN FARNESYLTRANSFERASE INHIBITOR; PYROPHOSPHATE; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; ARTICLE; CHEMICAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME MECHANISM; ENZYME SUBSTRATE; ENZYME SYNTHESIS; ONCOGENE RAS; PHOTOLYSIS; PRENYLATION; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

ALKYL AND ARYL TRANSFERASES; CRYSTALLOGRAPHY, X-RAY; DIMETHYLALLYLTRANSTRANSFERASE; ENZYME INHIBITORS; FARNESYLTRANSTRANSFERASE; HUMANS; PEPTIDES; POLYISOPRENYL PHOSPHATES; PROTEIN PRENYLATION; SUBSTRATE SPECIFICITY;

EID: 50449094648     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2008.00698.x     Document Type: Article

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