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dc.contributor.author
Guy, Naihsuan C.
dc.contributor.author
Garcia, Yenni A.
dc.contributor.author
Sivils, Jeffrey
dc.contributor.author
Galigniana, Mario Daniel
dc.contributor.author
Cox, Marc B.
dc.contributor.other
Blatch, Gregory L.
dc.contributor.other
Edkins, A. L.
dc.date.available
2020-07-17T13:29:11Z
dc.date.issued
2015
dc.identifier.citation
Guy, Naihsuan C.; Garcia, Yenni A.; Sivils, Jeffrey; Galigniana, Mario Daniel; Cox, Marc B.; Functions of Hsp90-Binding FKBP immunophilins; Springer; 78; 2015; 35-68
dc.identifier.isbn
978-0-387-49310-7
dc.identifier.uri
http://hdl.handle.net/11336/109524
dc.description.abstract
Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90- binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
FKBP51
dc.subject
FKBP52
dc.subject
HSP90
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TPR
dc.subject.classification
Bioquímica y Biología Molecular
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Medicina Básica
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CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Functions of Hsp90-Binding FKBP immunophilins
dc.type
info:eu-repo/semantics/publishedVersion
dc.type
info:eu-repo/semantics/bookPart
dc.type
info:ar-repo/semantics/parte de libro
dc.date.updated
2020-06-23T15:50:12Z
dc.journal.volume
78
dc.journal.pagination
35-68
dc.journal.pais
Estados Unidos
dc.journal.ciudad
New York
dc.description.fil
Fil: Guy, Naihsuan C.. University of Texas at El Paso; Estados Unidos
dc.description.fil
Fil: Garcia, Yenni A.. University of Texas at El Paso; Estados Unidos
dc.description.fil
Fil: Sivils, Jeffrey. University of Texas at El Paso; Estados Unidos
dc.description.fil
Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Cox, Marc B.. University of Texas at El Paso; Estados Unidos
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/chapter/10.1007/978-3-319-11731-7_2
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/978-3-319-11731-7_2
dc.source.titulo
The Networking of chaperones by Co-chaperones
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