Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-7-18
pubmed:abstractText
Src homology 2 (SH2) domain is a conserved module involved in various biological processes. Tensin family member was reported to be involved in tumor suppression by interacting with DLC-1 (deleted-in-liver-cancer-1) via its SH2 domain. We explore here the important questions that what the structure of tensin2 SH2 domain is, and how it binds to DLC-1, which might reveal a novel binding mode.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-10320398, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-11809769, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-11823424, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-12920122, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-14592531, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-14987415, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-15680235, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-1689011, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-1691440, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-16951145, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-17190795, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-17517630, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-17846036, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-17979893, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19194507, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19214987, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19440389, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19487278, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19548092, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19580545, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-19732724, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-20457744, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-2153914, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-3025655, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-7511210, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-7536927, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-7680959, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-8520220, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-8730509, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-9367762, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-9774102, http://linkedlifedata.com/resource/pubmed/commentcorrection/21765928-9817027
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1932-6203
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
e21965
pubmed:meshHeading
pubmed-meshheading:21765928-Amino Acid Sequence, pubmed-meshheading:21765928-Circular Dichroism, pubmed-meshheading:21765928-Humans, pubmed-meshheading:21765928-Kinetics, pubmed-meshheading:21765928-Ligands, pubmed-meshheading:21765928-Magnetic Resonance Spectroscopy, pubmed-meshheading:21765928-Microfilament Proteins, pubmed-meshheading:21765928-Models, Molecular, pubmed-meshheading:21765928-Molecular Sequence Data, pubmed-meshheading:21765928-Peptides, pubmed-meshheading:21765928-Phosphoric Monoester Hydrolases, pubmed-meshheading:21765928-Phosphorylation, pubmed-meshheading:21765928-Phosphotyrosine, pubmed-meshheading:21765928-Protein Binding, pubmed-meshheading:21765928-Protein Structure, Secondary, pubmed-meshheading:21765928-Sequence Alignment, pubmed-meshheading:21765928-Solutions, pubmed-meshheading:21765928-Structure-Activity Relationship, pubmed-meshheading:21765928-Surface Plasmon Resonance, pubmed-meshheading:21765928-Tumor Suppressor Proteins, pubmed-meshheading:21765928-src Homology Domains
pubmed:year
2011
pubmed:articleTitle
Solution structure of tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1.
pubmed:affiliation
Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't