9663660

Source:http://linkedlifedata.com/resource/pubmed/id/9663660

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0279266, umls-concept:C0567416, umls-concept:C1314939, umls-concept:C1710082, umls-concept:C1837565
pubmed:issue	4
pubmed:dateCreated	1998-10-14
pubmed:abstractText	TGF-beta superfamily members elicit signals through the stimulation of serine/threonine-kinase receptors. Recently, molecules associated with several TGF-beta family receptors have been cloned. One such molecule, the immunophilin FKBP12, has been reported to interact with TGF-beta family type I receptors. However, the identity of signalling specific molecules interacting with the receptor was unknown.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9607379
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/BMPR1A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein..., http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/TAB1 protein, MAPKKK activator..., http://linkedlifedata.com/resource/pubmed/chemical/TAB1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta, http://linkedlifedata.com/resource/pubmed/chemical/ZMYND11 protein, human
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	1356-9597
pubmed:author	pubmed-author:FujitaTT, pubmed-author:KurozumiKK, pubmed-author:NishitaMM, pubmed-author:ShibuyaHH, pubmed-author:UenoNN, pubmed-author:YamaguchiKK
pubmed:issnType	Print
pubmed:volume	3
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	257-64
pubmed:dateRevised	2011-10-14
pubmed:meshHeading	pubmed-meshheading:9663660-Adaptor Proteins, Signal Transducing, pubmed-meshheading:9663660-Alternative Splicing, pubmed-meshheading:9663660-Bone Morphogenetic Protein Receptors, Type I, pubmed-meshheading:9663660-Bone Morphogenetic Proteins, pubmed-meshheading:9663660-Carrier Proteins, pubmed-meshheading:9663660-Cell Compartmentation, pubmed-meshheading:9663660-Cloning, Molecular, pubmed-meshheading:9663660-DNA, Complementary, pubmed-meshheading:9663660-Humans, pubmed-meshheading:9663660-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:9663660-Peptide Fragments, pubmed-meshheading:9663660-Protein Binding, pubmed-meshheading:9663660-Protein-Serine-Threonine Kinases, pubmed-meshheading:9663660-Receptors, Growth Factor, pubmed-meshheading:9663660-Saccharomyces cerevisiae, pubmed-meshheading:9663660-Signal Transduction, pubmed-meshheading:9663660-Tissue Distribution, pubmed-meshheading:9663660-Transforming Growth Factor beta
pubmed:year	1998
pubmed:articleTitle	BRAM1, a BMP receptor-associated molecule involved in BMP signalling.
pubmed:affiliation	Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't