Palmitoylation and depalmitoylation dynamics at a glance
Author(s) -
Elizabeth Conibear,
Nicholas G. Davis
Publication year - 2010
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.059287
Subject(s) - biology , palmitoylation , dynamics (music) , microbiology and biotechnology , biochemistry , physics , cysteine , enzyme , acoustics
Protein palmitoylation, the thioester linkage of fatty acyl moieties (typically, saturated 16C palmitate) to cysteine, is a lipid modification that serves both to tether proteins to membranes and to direct their localization to membrane microdomains. Unlike the two other types of lipid modification
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