Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex

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Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known. In contrast, the high molecular weight hsp90-binding immunophilins appear to pl...

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Detalles Bibliográficos
Autores principales: Galigniana, M.D., Morishima, Y., Gallay, P.A., Pratt, W.B.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2004
Materias:
Cells
Cytology
Drug products
Immunology
Living systems studies
Molecular weight
Immunophilins
Microtubules
Prolyl isomerase
Protein trafficking
Proteins
cyclophilin
cyclophilin A
cyclosporin A
dynein adenosine triphosphatase
heat shock protein 90
immunophilin
immunosuppressive agent
protein p53
tubulin
animal cell
article
complex formation
controlled study
cytoplasm
cytosol
enzyme activity
in vitro study
in vivo study
microtubule
molecular weight
mouse
nonhuman
priority journal
protein binding
protein domain
protein expression
protein function
protein localization
protein protein interaction
protein synthesis
protein transport
Animals
Cell Line
Cell-Free System
Cyclophilin A
Cyclosporine
Cytoplasm
Fluorescent Antibody Technique, Indirect
Glutathione
HSP90 Heat-Shock Proteins
Immunoblotting
Immunosuppressive Agents
Mice
Microtubule-Associated Proteins
NIH 3T3 Cells
Peptidylprolyl Isomerase
Plasmids
Protein Binding
Protein Structure, Tertiary
Rabbits
Receptors, Glucocorticoid
Tumor Suppressor Protein p53
Animalia
Mammalia
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219258_v279_n53_p55754_Galigniana
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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