Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-9-7
pubmed:abstractText
dHAND is a transcription factor belonging to the class B basic helix-loop-helix protein family and is expressed during embryogenesis in the heart, branchial arches, limb buds, and neural crest derivatives. Despite much study, the molecular mechanisms involved in the regulation of dHAND activity are not well understood. We therefore carried out yeast two-hybrid screening using full-length dHAND as bait, which led to identification of several dHAND-binding proteins, including three E-proteins: E2A, ME2, and ALF1. Subsequent analysis revealed that although their heterodimerization and transcriptional activities were similar, dHAND/E-protein heterodimers bind to an E-box element with differing affinities, suggesting they have distinct DNA binding specificities. Moreover, in situ hybridization showed that E-protein genes are expressed fairly ubiquitously among embryonic tissues, including the branchial arches and limb buds. By contrast, little signal was detected in the heart, suggesting that dHAND complexes with partners other than E-proteins in cardiac tissue.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Basic Helix-Loop-Helix Leucine..., http://linkedlifedata.com/resource/pubmed/chemical/Basic Helix-Loop-Helix..., http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/HAND2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Hand2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/Myelin Basic Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TCF Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/TCF3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Tcf12 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Tcf3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Tcf4 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins, http://linkedlifedata.com/resource/pubmed/chemical/hand2 protein, zebrafish
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Elsevier Inc.
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
323
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
168-74
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:15351717-Animals, pubmed-meshheading:15351717-Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, pubmed-meshheading:15351717-Basic Helix-Loop-Helix Transcription Factors, pubmed-meshheading:15351717-Blotting, Western, pubmed-meshheading:15351717-Cell Line, pubmed-meshheading:15351717-DNA, pubmed-meshheading:15351717-DNA, Complementary, pubmed-meshheading:15351717-DNA-Binding Proteins, pubmed-meshheading:15351717-Dimerization, pubmed-meshheading:15351717-Gene Library, pubmed-meshheading:15351717-Genes, Reporter, pubmed-meshheading:15351717-Glutathione Transferase, pubmed-meshheading:15351717-Helix-Loop-Helix Motifs, pubmed-meshheading:15351717-Humans, pubmed-meshheading:15351717-In Situ Hybridization, pubmed-meshheading:15351717-Luciferases, pubmed-meshheading:15351717-Mice, pubmed-meshheading:15351717-Models, Biological, pubmed-meshheading:15351717-Myelin Basic Proteins, pubmed-meshheading:15351717-Nerve Tissue Proteins, pubmed-meshheading:15351717-Protein Binding, pubmed-meshheading:15351717-Signal Transduction, pubmed-meshheading:15351717-TCF Transcription Factors, pubmed-meshheading:15351717-Time Factors, pubmed-meshheading:15351717-Transcription, Genetic, pubmed-meshheading:15351717-Transcription Factors, pubmed-meshheading:15351717-Transfection, pubmed-meshheading:15351717-Two-Hybrid System Techniques, pubmed-meshheading:15351717-Zebrafish Proteins
pubmed:year
2004
pubmed:articleTitle
Differential cooperation between dHAND and three different E-proteins.
pubmed:affiliation
Division of Integrative Cell Biology, Department of Embryogenesis, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Kumamoto, Kumamoto 860-0811, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't