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

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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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Autor principal: Erlejman, A.G
Otros Autores: Lagadari, M., Harris, D.C, Cox, M.B, Galigniana, M.D
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Bentham Science Publishers B.V. 2014
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 cas  |a cyclosporin A, 59865-13-3, 63798-73-2; peptidylprolyl isomerase, 95076-93-0; rapamycin, 53123-88-9; tacrolimus, 104987-11-3; Molecular Chaperones; Receptors, Steroid; tacrolimus binding protein 4; tacrolimus binding protein 5; Tacrolimus Binding Proteins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a CPPSC 
100 1 |a Erlejman, A.G. 
245 1 0 |a Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 
260 |b Bentham Science Publishers B.V.  |c 2014 
270 1 0 |m Galigniana, M. D.; IBYME, Vuelta de Obligado 2490, Buenos Aires (C1428ADN), Argentina; email: mgali@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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 and subcellular compartments, and their amino acid sequences are conserved phylogenetically. Immunophilins possess the ability to function as molecular chaperones favoring the proper folding and biological regulation of their biological actions. Their ability to interact via their TPR domains with the 90-kDa heat-shock protein, and through this chaperone, with several signalling cascade factors is of particular importance. Among the family members, the highly homologous proteins FKBP51 and FKBP52 were first characterized due to their ability to interact with steroid hormone receptors. Since then, much progress has been made in understanding the mechanisms by which they regulate receptor signaling and the resulting roles they play not only in endocrine processes, but also in cell architecture, neurodifferentiation, and tumor progression. In this article we review the most relevant features of these two immunophilins and their potential as pharmacologic targets. © 2014 Bentham Science Publishers.  |l eng 
536 |a Detalles de la financiación: National Center for Research Resources, NCRR, 5G12RR008124 
536 |a Detalles de la financiación: National Institute of General Medical Sciences, NIGMS, RP110444-P2 
593 |a Departamento de Química Biológica/IQUIBICEN, Universidad de Buenos Aires, Argentina 
593 |a Instituto de Biología Medicina Experimental/CONICET, Buenos Aires, Argentina 
593 |a The Border Biomedical Research Center and Department of Biological Sciences, University of Texas at El Paso, El Paso, TX, United States 
690 1 0 |a FK506 
690 1 0 |a FKBP51 
690 1 0 |a FKBP52 
690 1 0 |a HSP70 
690 1 0 |a HSP90 
690 1 0 |a IMMUNOPHILIN 
690 1 0 |a PEPTIDYLPROLYL ISOMERASE 
690 1 0 |a TPR 
690 1 0 |a CHAPERONE 
690 1 0 |a CYCLOSPORIN A 
690 1 0 |a FK 506 BINDING PROTEIN 
690 1 0 |a HEAT SHOCK PROTEIN 90 
690 1 0 |a IMMUNOPHILIN 
690 1 0 |a PEPTIDYLPROLYL ISOMERASE 
690 1 0 |a PROLINE RICH PROTEIN 
690 1 0 |a PROTEIN FKB52 
690 1 0 |a PROTEIN FKBP51 
690 1 0 |a PROTEIN S 100 
690 1 0 |a RAPAMYCIN 
690 1 0 |a TACROLIMUS 
690 1 0 |a TAU PROTEIN 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a CHAPERONE 
690 1 0 |a FK 506 BINDING PROTEIN 
690 1 0 |a STEROID RECEPTOR 
690 1 0 |a TACROLIMUS BINDING PROTEIN 4 
690 1 0 |a TACROLIMUS BINDING PROTEIN 5 
690 1 0 |a ALZHEIMER DISEASE 
690 1 0 |a ARTICLE 
690 1 0 |a BREAST CANCER 
690 1 0 |a CELL GROWTH 
690 1 0 |a CELL PROLIFERATION 
690 1 0 |a COMPLEX FORMATION 
690 1 0 |a CYTOSKELETON 
690 1 0 |a GENE EXPRESSION 
690 1 0 |a GENE OVEREXPRESSION 
690 1 0 |a HUMAN 
690 1 0 |a NERVE CELL DIFFERENTIATION 
690 1 0 |a NONHUMAN 
690 1 0 |a OVARY CANCER 
690 1 0 |a PROTEIN ASSEMBLY 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN DOMAIN 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN FUNCTION 
690 1 0 |a PROTEIN INTERACTION 
690 1 0 |a PROTEIN LOCALIZATION 
690 1 0 |a PROTEIN PHOSPHORYLATION 
690 1 0 |a TETRATRICOPEPTIDE REPEAT 
690 1 0 |a CHEMISTRY 
690 1 0 |a METABOLISM 
690 1 0 |a PROTEIN FOLDING 
690 1 0 |a PROTEIN TERTIARY STRUCTURE 
690 1 0 |a HUMANS 
690 1 0 |a MOLECULAR CHAPERONES 
690 1 0 |a PROTEIN FOLDING 
690 1 0 |a PROTEIN STRUCTURE, TERTIARY 
690 1 0 |a RECEPTORS, STEROID 
690 1 0 |a TACROLIMUS BINDING PROTEINS 
700 1 |a Lagadari, M. 
700 1 |a Harris, D.C. 
700 1 |a Cox, M.B. 
700 1 |a Galigniana, M.D. 
773 0 |d Bentham Science Publishers B.V., 2014  |g v. 15  |h pp. 205-215  |k n. 3  |p Curr. Protein Pept. Sci.  |x 13892037  |t Current Protein and Peptide Science 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-84904465108&partnerID=40&md5=d3b6e0b16b92b0cce45c942dba4ccac2  |y Registro en Scopus 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_13892037_v15_n3_p205_Erlejman  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13892037_v15_n3_p205_Erlejman  |y Registro en la Biblioteca Digital 
961 |a paper_13892037_v15_n3_p205_Erlejman  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 85018 

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