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Substitution of glutamine for arginine 1131 : a newly identified mutation in the catalytic loop of the tyrosine kinase domain of the human insulin receptor

Author
KISHIMOTO, M1 ; HASHIRAMOTO, M1 ; YONEZAWA, K1 ; SHII, K; KAZUMI, T; KASUGA, M1
[1] Kobe univ. school medicine, second dep. internal medicine, Chuo-ku, Kobe 650, Japan
Source

The Journal of biological chemistry (Print). 1994, Vol 269, Num 15, pp 11349-11355 ; ref : 48 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)
Autophosphorylation Homme Insuline Protein-tyrosine kinase Relation structure activité Réaction chaîne polymérase Site catalytique Transduction signal Enzyme Hormone protéine Mutation Récepteur hormonal Transferases
Keyword (en)
Autophosphorylation Human Insulin Protein-tyrosine kinase Structure activity relation Polymerase chain reaction Catalytic site Signal transduction Enzyme Protein hormone Mutation Hormonal receptor Transferases
Keyword (es)
Autofosforilación Hombre Insulina Protein-tyrosine kinase Relación estructura actividad Reacción cadena polimerasa Sitio catalítico Transducción señal Enzima Hormona proteina Mutación Receptor hormonal Transferases
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A04 Molecular and cellular biology / 002A04F Cell structures and functions / 002A04F03 Cell receptors / 002A04F03A Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors

Discipline
Molecular and cell biology
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
4182951

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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