scholarly journals Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor

Cell Reports ◽  
2016 ◽  
Vol 16 (2) ◽  
pp. 531-544 ◽  
Author(s):  
Christoph Straub ◽  
Yoav Noam ◽  
Toshihiro Nomura ◽  
Miwako Yamasaki ◽  
Dan Yan ◽  
...  
Keyword(s):  
Kainate Receptor ◽  
Distinct Subunit

Effects of Chronic Alcohol Exposure on Kainate Receptor-Mediated Neurotransmission in the Hippocampus

2002 ◽  
Author(s):  
C. F. Valenzuela ◽  
Daniel D. Savage ◽  
Jeff. L. Weiner
Keyword(s):  
Alcohol Exposure ◽  
Kainate Receptor ◽  
Chronic Alcohol ◽  
Chronic Alcohol Exposure

Association study of polymorphisms in the GluR5 kainate receptor gene (GRIK1) with schizophrenia

2001 ◽  
Vol 11 (3) ◽  
pp. 139-144 ◽  
Author(s):  
Hiroki Shibata ◽  
Akiko Joo ◽  
Yo Fujii ◽  
Ayako Tani ◽  
Chieko Makino ◽  
...  
Keyword(s):  
Association Study ◽  
Receptor Gene ◽  
Kainate Receptor

scholarly journals The kainate receptor antagonist UBP310 but not single deletion of GluK1, GluK2, or GluK3 subunits, inhibits MPTP-induced degeneration in the mouse midbrain

2020 ◽  
Vol 323 ◽  
pp. 113062 ◽  
Author(s):  
Sandy Stayte ◽  
Kathryn J. Laloli ◽  
Peggy Rentsch ◽  
Aimee Lowth ◽  
Kong M. Li ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Kainate Receptor ◽  
Single Deletion

405. Kainate receptor expression in postmortem schizophrenic brain

1998 ◽  
Vol 43 (8) ◽  
pp. S121 ◽  
Author(s):  
O. Cahlon ◽  
V. Haroutunian ◽  
K.L. Davis ◽  
S.J. Watson ◽  
J.H. Meador-Woodruff
Keyword(s):  
Receptor Expression ◽  
Kainate Receptor

scholarly journals Conformational Landscape of an Agonist-Binding Domain of a Full-Length Heteromeric Kainate Receptor Gluk2/K5 Displaying Partial Agonism

2021 ◽  
Vol 120 (3) ◽  
pp. 56a
Author(s):  
Nabina Paudyal ◽  
Elisa Carrillo ◽  
Vladmir Berka ◽  
Vasanthi Jayaraman
Keyword(s):  
Binding Domain ◽  
Full Length ◽  
Kainate Receptor ◽  
Agonist Binding ◽  
Partial Agonism ◽  
Conformational Landscape

scholarly journals Structure And Stability Of Ligand Binding Core Dimer Assembly Controls Desensitization In A Kainate Receptor

2009 ◽  
Vol 96 (3) ◽  
pp. 491a
Author(s):  
Charu Chaudhry ◽  
Matthew C. Weston ◽  
Peter Schuck ◽  
Christian Rosenmund ◽  
Mark L. Mayer
Keyword(s):  
Ligand Binding ◽  
Kainate Receptor ◽  
Structure And Stability ◽  
Binding Core

scholarly journals Single Molecule FRET Studies into the Effects of Sodium on Kainate Receptor Dynamics

2018 ◽  
Vol 114 (3) ◽  
pp. 125a
Author(s):  
Douglas Litwin ◽  
Sana Shaikh ◽  
Vladimir Berka ◽  
Vasanthi Jayaraman
Keyword(s):  
Single Molecule ◽  
Kainate Receptor ◽  
Single Molecule Fret ◽  
Receptor Dynamics

scholarly journals Two related ARID family proteins are alternative subunits of human SWI/SNF complexes

2004 ◽  
Vol 383 (2) ◽  
pp. 319-325 ◽  
Author(s):  
Xiaomei WANG ◽  
Norman G. NAGL ◽  
Deborah WILSKER ◽  
Michael VAN SCOY ◽  
Stephen PACCHIONE ◽  
...  
Keyword(s):  
Dna Binding ◽  
Direct Evidence ◽  
Potential Interaction ◽  
Atpase Subunit ◽  
Reading Frame ◽  
Atpase Subunits ◽  
A Subunit ◽  
Distinct Subunit ◽  
Binding Behaviour

p270 (ARID1A) is a member of the ARID family of DNA-binding proteins and a subunit of human SWI/SNF-related complexes, which use the energy generated by an integral ATPase subunit to remodel chromatin. ARID1B is an independent gene product with an open reading frame that is more than 60% identical with p270. We have generated monoclonal antibodies specific for either p270 or ARID1B to facilitate the investigation of ARID1B and its potential interaction with human SWI/SNF complexes in vivo. Immunocomplex analysis provides direct evidence that endogenous ARID1B is associated with SWI/SNF-related complexes and indicates that p270 and ARID1B, similar to the ATPase subunits BRG1 and hBRM, are alternative, mutually exclusive subunits of the complexes. The ARID-containing subunits are not specific to the ATPases. Each associates with both BRG1 and hBRM, thus increasing the number of distinct subunit combinations known to be present in cells. Analysis of the panels of cell lines indicates that ARID1B, similar to p270, has a broad tissue distribution. The ratio of p270/ARID1B in typical cells is approx. 3.5:1, and BRG1 is distributed proportionally between the two ARID subunits. Analysis of DNA-binding behaviour indicates that ARID1B binds DNA in a non-sequence-specific manner similar to p270.

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