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Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

Author
HARRISON, C. J1 ; HAYER-HARTL, M; DI LIBERTO, M; HARTL, F.-U; KURIYAN, J1
Cellular Biochemistry and Biophysics Program, Howard Hughes Medical Institute, New York, NY 10021, United States
Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, United States
[1] Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, United States
Source

Science (Washington, D.C.). 1997, Vol 276, Num 5311, pp 431-435

CODEN
SCIEAS
ISSN
0036-8075
Scientific domain
Multidisciplinary
Publisher
American Association for the Advancement of Science, Washington, DC
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Adenosinetriphosphatase Chaperon Complexe moléculaire Conformation Escherichia coli Interaction moléculaire Maturation moléculaire Protéine liaison Repliement Structure cristalline Structure moléculaire Protéine DnaK Protéine GrpE Bactérie Enterobacteriaceae Enzyme Hydrolases
Keyword (en)
Adenosinetriphosphatase Chaperone Molecular complex Conformation Escherichia coli Molecular interaction Molecular processing Binding protein Refolding Crystalline structure Molecular structure Bacteria Enterobacteriaceae Enzyme Hydrolases
Keyword (es)
Adenosinetriphosphatase Complejo molecular Conformación Escherichia coli Interacción molecular Maduración molecular Proteína enlace Repliegue Estructura cristalina Estructura molecular Bacteria Enterobacteriaceae Enzima Hydrolases
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
2641025

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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