A molecular dynamics study of catestatin docked on nicotinic acetylcholine receptors to identify amino acids potentially involved in the binding of chromogranin A fragments. Issue 26 (14th July 2015)

Record Type:: Journal Article
Title:: A molecular dynamics study of catestatin docked on nicotinic acetylcholine receptors to identify amino acids potentially involved in the binding of chromogranin A fragments. Issue 26 (14th July 2015)
Main Title:: A molecular dynamics study of catestatin docked on nicotinic acetylcholine receptors to identify amino acids potentially involved in the binding of chromogranin A fragments
Authors:: Kraszewski, Sebastian
Drabik, Dominik
Langner, Marek
Ramseyer, Christophe
Kembubpha, Sineenat
Yasothornsrikul, Sukkid
Abstract:: <abstract abstract-type="toc"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <graphic position="anchor" id="ga" xlink:href="ark:/27927/pgj1c6nq4tk" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" />Human catestatin, representing potential to regulate nicotinic signal transduction, can bind onto nAChR-β subunits indicating a novel mode of action.</p> </abstract>
Is Part Of:: Physical chemistry chemical physics. Volume 17:Issue 26(2015)
Journal:: Physical chemistry chemical physics
Issue:: Volume 17:Issue 26(2015)
Issue Display:: Volume 17, Issue 26 (2015)
Year:: 2015
Volume:: 17
Issue:: 26
Issue Sort Value:: 2015-0017-0026-0000
Page Start:: 17454
Page End:: 17460
Publication Date:: 2015-07-14
Subjects:: Chemistry, Physical and theoretical -- Periodicals
541.3
Journal URLs:: http://pubs.rsc.org/en/journals/journalissues/cp#!issueid=cp016040&type=current&issnprint=1463-9076 ↗
http://www.rsc.org/ ↗
DOI:: 10.1039/c4cp02491e ↗
Languages:: English
ISSNs:: 1463-9076
Deposit Type:: Legaldeposit
View Content:: Available online (eLD content is only available in our Reading Rooms) ↗
Physical Locations:: British Library DSC - 6475.306000
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Ingest File:: 3200.xml