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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2004-7-9
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pubmed:abstractText |
Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes. The fast growing number of research reports on protein phosphorylation points to a general need for an accurate database dedicated to phosphorylation to provide easily retrievable information on phosphoproteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-10600390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-10647936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-11283593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-11911893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-11988757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-12471243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-12520052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-12824381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-12923550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-14681407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-14755292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15212693-9847189
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1471-2105
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
22
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
79
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15212693-Animals,
pubmed-meshheading:15212693-Binding Sites,
pubmed-meshheading:15212693-Databases, Protein,
pubmed-meshheading:15212693-Humans,
pubmed-meshheading:15212693-Mice,
pubmed-meshheading:15212693-Phosphorylation,
pubmed-meshheading:15212693-Protein Processing, Post-Translational,
pubmed-meshheading:15212693-Proteins,
pubmed-meshheading:15212693-Rats,
pubmed-meshheading:15212693-Research Design,
pubmed-meshheading:15212693-Software
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pubmed:year |
2004
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pubmed:articleTitle |
Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins.
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pubmed:affiliation |
Cellzome AG, Heidelberg, Germany. diella@embl.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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