Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-1-16
pubmed:abstractText
Pleckstrin homology (PH) domains are one of the most prevalent domains in the human proteome and represent the major phosphoinositide-binding module. These domains are often found in signaling proteins and function predominately by targeting their host proteins to the cell membrane. Inositol phosphates, which are structurally similar to phosphoinositides, are not only known to play a role as signaling molecules but are also capable of being bound by PH domains.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-10196129, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-10497244, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-10983984, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-10995449, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-11136447, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-11331907, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-11384737, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-12401198, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-12434012, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-12434013, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-1329895, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-13678580, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-14594214, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-14755253, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15247908, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15274927, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15299374, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15299926, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15493994, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15572765, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-15698571, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-16166311, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-16381859, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-16500648, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-16510979, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-1660712, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-17115053, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-1850990, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-2768345, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-2897630, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-3178774, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-7782310, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-8070814, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-8381210, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-8497315, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-8500161, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-8810277, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-8999861, http://linkedlifedata.com/resource/pubmed/commentcorrection/18034889-9060471
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1472-6807
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
80
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Structural analysis of the carboxy terminal PH domain of pleckstrin bound to D-myo-inositol 1,2,3,5,6-pentakisphosphate.
pubmed:affiliation
Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Canada. jacksosg@mcmaster.ca
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't