Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52

Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin derives. Family members are found in abundance in virtually all organisms...

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Detalles Bibliográficos
Autores principales: Erlejman, A.G., Lagadari, M., Harris, D.C., Cox, M.B., Galigniana, M.D.
Formato: JOUR
Materias:
FK506
FKBP51
FKBP52
Hsp70
Hsp90
Immunophilin
Peptidylprolyl isomerase
TPR
chaperone
cyclosporin A
fk 506 binding protein
heat shock protein 90
immunophilin
peptidylprolyl isomerase
proline rich protein
protein FKB52
protein FKBP51
protein S 100
rapamycin
tacrolimus
tau protein
unclassified drug
steroid receptor
tacrolimus binding protein 4
tacrolimus binding protein 5
Alzheimer disease
article
breast cancer
cell growth
cell proliferation
complex formation
cytoskeleton
gene expression
gene overexpression
human
nerve cell differentiation
nonhuman
ovary cancer
protein assembly
protein binding
protein domain
protein expression
protein function
protein interaction
protein localization
protein phosphorylation
tetratricopeptide repeat
chemistry
metabolism
protein folding
protein tertiary structure
Humans
Molecular Chaperones
Protein Folding
Protein Structure, Tertiary
Receptors, Steroid
Tacrolimus Binding Proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_13892037_v15_n3_p205_Erlejman
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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