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Mutation of calmodulin-binding site renders the Na+/H+ exchanger (NHE1) highly H+-sensitive and Ca2+ regulation-defective

Author
WAKABAYASHI, S1 ; BERTRAND, B; IKEDA, T1 ; POUYSSEGUR, J2 ; SHIGEKAWA, M1
[1] National cardiovascular cent. res. inst., dep. molecular physiology, Suita, Osaka 565, Japan
[2] CNRS Univ. Nice, cent. biochimie, 06108 Nice, France
Source

The Journal of biological chemistry (Print). 1994, Vol 269, Num 18, pp 13710-13715 ; ref : 34 ref

CODEN
JBCHA3
ISSN
0021-9258
Scientific domain
Biochemistry, molecular biology, biophysics; Biotechnology
Publisher
American Society for Biochemistry and Molecular Biology, Bethesda, MD
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Calmoduline Mutagenèse dirigée Proton Relation structure activité Sodium Séquence régulatrice Transduction signal Calcium Protéine liaison Protéine transport Transport ion
Keyword (en)
Calmodulin Site directed mutagenesis Proton Structure activity relation Sodium Regulatory sequence Signal transduction Calcium Binding protein Carrier protein Ion transport
Keyword (es)
Calmodulina Mutagénesis dirigida Protón Relación estructura actividad Sodio Secuencia reguladora Transducción señal Calcio Proteína enlace Proteína transportador Transporte iónica
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02D Proteins / 002A02D08 Binding and carrier proteins

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
4167008

Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS

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