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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2011-2-23
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pubmed:abstractText |
PH domains represent one of the most common domains in the human proteome. These domains are recognized as important mediators of protein-phosphoinositide and protein-protein interactions. Phosphoinositides are lipid components of the membrane that function as signaling molecules by targeting proteins to their sites of action. Phosphoinositide based signaling pathways govern a diverse range of important cellular processes including membrane remodeling, differentiation, proliferation and survival. Myo-Inositol phosphates are soluble signaling molecules that are structurally similar to the head groups of phosphoinositides. These molecules have been proposed to function, at least in part, by regulating PH domain-phosphoinositide interactions. Given the structural similarity of inositol phosphates we were interested in examining the specificity of PH domains towards the family of myo-inositol pentakisphosphate isomers.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-10320401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-10834940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-10983984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-10983985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-11331907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-11384737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-12614874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-14594214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-14755253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-15698571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-16166311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-16381859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-16510979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-17692025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-18034889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-18288939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-19675354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-20364126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-2171926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-2469189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-2550825,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21310079-9804818
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/inositol pentaphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol receptors,
http://linkedlifedata.com/resource/pubmed/chemical/platelet protein P47
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pubmed:status |
MEDLINE
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pubmed:issn |
1472-6807
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11
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pubmed:dateRevised |
2011-7-25
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pubmed:meshHeading |
pubmed-meshheading:21310079-Binding Sites,
pubmed-meshheading:21310079-Blood Proteins,
pubmed-meshheading:21310079-Inositol Phosphates,
pubmed-meshheading:21310079-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:21310079-Isomerism,
pubmed-meshheading:21310079-Phosphatidylinositols,
pubmed-meshheading:21310079-Phosphoproteins,
pubmed-meshheading:21310079-Protein Binding,
pubmed-meshheading:21310079-Protein Interaction Domains and Motifs,
pubmed-meshheading:21310079-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:21310079-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:21310079-Signal Transduction
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pubmed:year |
2011
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pubmed:articleTitle |
Inositol pentakisphosphate isomers bind PH domains with varying specificity and inhibit phosphoinositide interactions.
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pubmed:affiliation |
Department of Biochemistry and Biomedical Sciences, McMaster University, 1200 Main Street West, Hamilton, ON, L8N 3Z5, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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