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8/22/2014 11:42:00 AM | Browse: 757 | Download: 635
Publication Name World Journal of Biological Chemistry
Manuscript ID 7729
Country/Territory Germany
Received
2013-11-30 11:39
Peer-Review Started
2013-11-30 23:17
To Make the First Decision
2014-02-27 11:32
Return for Revision
2014-03-03 17:42
Revised
2014-03-13 06:08
Second Decision
2014-04-11 18:49
Accepted by Journal Editor-in-Chief
Accepted by Company Editor-in-Chief
2014-04-11 19:09
Articles in Press
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript
2014-05-22 14:39
Publish the Manuscript Online
2014-06-11 10:30
ISSN 1949-8454 (online)
Open Access
Copyright
Article Reprints For details, please visit: http://www.wjgnet.com/bpg/gerinfo/247
Permissions For details, please visit: http://www.wjgnet.com/bpg/gerinfo/207
Publisher Baishideng Publishing Group Inc, 7041 Koll Center Parkway, Suite 160, Pleasanton, CA 94566, USA
Website http://www.wjgnet.com
Category Biochemistry & Molecular Biology
Manuscript Type Autobiography
Article Title Functional analysis of human Na+/K+-ATPase familial or sporadic hemiplegic migraine mutations expressed in Xenopus oocytes
Manuscript Source Invited Manuscript
All Author List Susan Spiller and Thomas Friedrich
Funding Agency and Grant Number
Funding Agency Grant Number
German Research Foundation (Cluster of Excellence “Unifying Concepts in Catalysis”)
Corresponding Author Thomas Friedrich, Professor, Institute of Chemistry, Technical University of Berlin, Sekr. PC-14, Straβe des 17. Juni 135, D-10623 Berlin, Germany. friedrich@chem.tu-berlin.de
Key Words Na+/K+-ATPase; Electrophysiology; Voltage dependence; Familial hemiplegic migraine; C-terminus; β-subunit
Core Tip Mutations of the human ATP1A2 gene, which encodes the Na+/K+-ATPase α2-subunit, are associated with familial hemiplegic migraine (FHM2) that is inherited in an autosomal dominant fashion. We studied seven ATP1A2 mutations related to FHM2 or sporadic hemiplegic migraine by electrophysiological and biochemical methods to characterize functional impairments. The mutations G855R, G900R, E902K, L994del, D999H, K1003E and Y1009X were selected according to their structural importance: in putative interaction sites between α- and β-subunit and in the α-subunit’s C-terminal region. Some of these mutations showed a severe loss of function, and we discuss the functional and physiological consequences in order to better understand the molecular basis for neurological impairments.
Publish Date 2014-06-11 10:30
Citation Spiller S, Friedrich T. Functional analysis of human Na+/K+-ATPase familial or sporadic hemiplegic migraine mutations expressed in Xenopus oocytes. World J Biol Chem 2014; 5(2): 240-253
URL http://www.wjgnet.com/1949-8454/full/v5/i2/240.htm
DOI http://dx.doi.org/10.4331/wjbc.v5.i2.240
Full Article (PDF) wjbc-5-240.pdf
Full Article (Word) wjbc-5-240.doc
Manuscript File 7729-Review.docx
Answering Reviewers 7729-Answering reviewers.pdf
Copyright License Agreement 7729-Copyright assignment.pdf
Peer-review Report 7729-Peer review(s).pdf
Scientific Editor Work List 7729-Scientific editor work list.doc