title: The muscle-specific beta m protein is functionally different from other members of the X,K-ATPase beta-subunit family.
authors.affiliation: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia. korn@mail.ibch.ru
authors.forename: Nikolay B
authors.initials: NB
authors.lastname: Pestov
authors.forename: Gilles
authors.initials: G
authors.lastname: Crambert
authors.forename: Hao
authors.initials: H
authors.lastname: Zhao
authors.forename: Tatyana V
authors.initials: TV
authors.lastname: Korneenko
authors.forename: Mikhail I
authors.initials: MI
authors.lastname: Shakhparonov
authors.forename: Käthi
authors.initials: K
authors.lastname: Geering
authors.forename: Nikolai N
authors.initials: NN
authors.lastname: Modyanov
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D027682:Cation Transport Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D018482:Muscle, Skeletal / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology; D021122:Protein Subunits / Q000378:metabolism; D051381:Rats; D013552:Swine
chemical_list: D027682:Cation Transport Proteins; D021122:Protein Subunits; D000251:Adenosine Triphosphatases