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
Publicado:	2014
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:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman 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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