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BIN1 gene

Known as: BRIDGING INTEGRATOR 1, AMPHIPHYSIN II, SH3P9 
This gene is involved in signal transduction and cell differentiation.
National Institutes of Health

Related topics

Related topics

6 relations
BIN1 proteinIntracellular Signaling ProcessLiver carcinomaSignal Transduction

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BIN1 wt Allele

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Bioinformatics strategy to advance the interpretation of Alzheimer's disease GWAS discoveries: The roads from association to causation
2013
2013
The N-BAR domain protein, Bin3, regulates Rac1- and Cdc42-dependent processes in myogenesis.
Review
2012
Review
2012
This month in archives of neurology.
Q ureshi and Mehler (page 294) complete their 3-part series with this review in which they survey the therapeutic potential of… 
2009
2009
The c-MYC-interacting proapoptotic tumor suppressor BIN1 is a transcriptional target for E2F1 in response to DNA damage
The E2F1 transcription factor, which was originally identified as a cell-cycle initiator, mediates apoptosis in response to DNA… 
Highly Cited
2006
Highly Cited
2006
Identification of VCP/p97, Carboxyl Terminus of Hsp70-interacting Protein (CHIP), and Amphiphysin II Interaction Partners Using Membrane-based Human Proteome Arrays*S
Proteins mediate their biological function through interactions with other proteins. Therefore, the systematic identification and… 
Highly Cited
2003
Highly Cited
2003
Expression of a MYCN-interacting isoform of the tumor suppressor BIN1 is reduced in neuroblastomas with unfavorable biological features.
PURPOSE Amplification of the MYCN proto-oncogene is strongly correlated with poor outcome in neuroblastoma (NB), although… 
Highly Cited
2003
Highly Cited
2003
Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.
The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be… 
Highly Cited
2001
Highly Cited
2001
Interaction of Two Structurally Distinct Sequence Types with the Clathrin Terminal Domain β-Propeller*
The amino-terminal domain of the clathrin heavy chain, which folds into a seven-bladed β-propeller, binds directly to several… 
Highly Cited
1997
Highly Cited
1997
Clathrin interacts specifically with amphiphysin and is displaced by dynamin 1
Highly Cited
1997
Highly Cited
1997
cDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants.
Amphiphysin, an SH3-domain containing protein concentrated in nerve terminals, is believed to be involved in the synaptic vesicle… 
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