| pubmed-article:15902274 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C0001461 | lld:lifeskim |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:15902274 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15902274 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:15902274 | pubmed:dateCreated | 2005-6-1 | lld:pubmed |
| pubmed-article:15902274 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15902274 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15902274 | pubmed:abstractText | The ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose. | lld:pubmed |
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| pubmed-article:15902274 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15902274 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15902274 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15902274 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15902274 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15902274 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:15902274 | pubmed:author | pubmed-author:LadurnerAndre... | lld:pubmed |
