| pubmed-article:1534749 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1534749 | lifeskim:mentions | umls-concept:C0068563 | lld:lifeskim |
| pubmed-article:1534749 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:1534749 | lifeskim:mentions | umls-concept:C1537044 | lld:lifeskim |
| pubmed-article:1534749 | lifeskim:mentions | umls-concept:C0598435 | lld:lifeskim |
| pubmed-article:1534749 | lifeskim:mentions | umls-concept:C0332206 | lld:lifeskim |
| pubmed-article:1534749 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:1534749 | pubmed:dateCreated | 1992-7-14 | lld:pubmed |
| pubmed-article:1534749 | pubmed:abstractText | The addition of palmitate to cysteine residues enhances the hydrophobicity of proteins, and consequently their membrane association. Here we have investigated whether this type of fatty acylation also regulates protein-protein interactions. GAP-43 is a neuronal protein that increases guanine nucleotide exchange by heterotrimeric G proteins. Two cysteine residues near the N-terminus of GAP-43 are subject to palmitoylation, and are necessary for membrane binding as well as for G(o) activation. N-terminal peptides, which include these cysteines, stimulate G(o). Monopalmitoylation reduces, and dipalmitoylation abolishes the activity of the peptides. The activity of GAP-43 protein purified from brain also is reversibly blocked by palmitoylation. This suggests that palmitoylation controls a cycle of GAP-43 between an acylated, membrane-bound reservoir of inactive GAP-43, and a depalmitoylated, active pool of protein. | lld:pubmed |
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| pubmed-article:1534749 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1534749 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1534749 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1534749 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1534749 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1534749 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1534749 | pubmed:author | pubmed-author:ValenzuelaDD | lld:pubmed |
| pubmed-article:1534749 | pubmed:author | pubmed-author:FishmanM CMC | lld:pubmed |
| pubmed-article:1534749 | pubmed:author | pubmed-author:SudoYY | lld:pubmed |
| pubmed-article:1534749 | pubmed:author | pubmed-author:Beck-Sickinge... | lld:pubmed |
| pubmed-article:1534749 | pubmed:author | pubmed-author:StrittmatterS... | lld:pubmed |
| pubmed-article:1534749 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1534749 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1534749 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1534749 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1534749 | pubmed:pagination | 2095-102 | lld:pubmed |
| pubmed-article:1534749 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
| pubmed-article:1534749 | pubmed:meshHeading | pubmed-meshheading:1534749-... | lld:pubmed |
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| pubmed-article:1534749 | pubmed:meshHeading | pubmed-meshheading:1534749-... | lld:pubmed |
| pubmed-article:1534749 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1534749 | pubmed:articleTitle | Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP-43. | lld:pubmed |
| pubmed-article:1534749 | pubmed:affiliation | Developmental Biology Laboratory, Massachusetts General Hospital, Charlestown. | lld:pubmed |
| pubmed-article:1534749 | pubmed:publicationType | Journal Article | lld:pubmed |
