Subcellular rearrangement of hsp90-binding immunophilins accompanies neuronal differentiation and neurite outgrowth

Mostrar todas las versiones(3)

FKBP51 and FKBP52 (FK506-binding protein 51 and 52) are tetratricopeptide repeat-domain immunophilins belonging to the tetratricopeptide- protein•hsp90•hsp70•p23 heterocomplex bound to steroid receptors. Immunophilins are related to receptor folding, subcellular localization, and hormonedependent tr...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Quintá, H.R., Maschi, D., Gomez-Sanchez, C., Piwien-Pilipuk, G., Galigniana, M.D.
Formato:	JOUR
Materias:	Chaperones FKBP Hippocampus P23 Tau Tetratricopeptide proteins beta tubulin beta3 tubulin fk 506 binding protein fk 506 binding protein 51 fk 506 binding protein 52 heat shock protein 70 heat shock protein 90 heat shock protein 90 binding immunophilin immunophilin messenger RNA microtubule associated protein 2 protein p23 tau 1 protein tau protein unclassified drug animal cell article brain nerve cell cell nucleus cell stimulation cellular distribution complex formation controlled study cytoplasm embryo gene overexpression gene silencing hippocampus intermediate filament microtubule mouse nerve cell differentiation nerve ending nerve fiber growth neuroblastoma cell nonhuman phenotype priority journal protein analysis protein assembly protein binding protein expression protein function protein transport rat transcription initiation Animals Cell Differentiation Cell Line, Tumor Female Fluorescent Antibody Technique, Indirect HSP90 Heat-Shock Proteins Immunophilins Immunosuppressive Agents Neurites Neuroblastoma Neurons Pregnancy Rats RNA, Messenger Signal Transduction Subcellular Fractions Tacrolimus Tacrolimus Binding Proteins Transfection Uridine Triphosphate
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00223042_v115_n3_p716_Quinta
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

Ejemplares similares

Subcellular rearrangement of hsp90-binding immunophilins accompanies neuronal differentiation and neurite outgrowth
por: Maschi, Darío
Publicado: (2010)

Subcellular rearrangement of hsp90-binding immunophilins accompanies neuronal differentiation and neurite outgrowth
por: Quintá, H.R., et al.
Publicado: (2010)

Subcellular rearrangement of hsp90-binding immunophilins accompanies neuronal differentiation and neurite outgrowth
por: Quintá, H.R., et al.
Publicado: (2010)

Management of cytoskeleton architecture by molecular chaperones and immunophilins
por: Lagadari, Mariana
Publicado: (2011)

Management of cytoskeleton architecture by molecular chaperones and immunophilins
por: Quintá, H.R., et al.

Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52
Publicado: (2014)

Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52
por: Erlejman, A.G., et al.

Regulation of NF-κB signalling cascade by immunophilins
Publicado: (2015)

Regulation of NF-κB signalling cascade by immunophilins
por: Lagadari, M., et al.

Hsp90-binding immunophilin FKBP51 forms complexes with hTERT enhancing telomerase activity
por: Lagadari, Mariana, et al.
Publicado: (2016)

Hsp90-binding immunophilin FKBP51 forms complexes with hTERT enhancing telomerase activity
por: Lagadari, M., et al.

The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
por: Monte, Martín
Publicado: (2010)

The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
por: Galigniana, M.D., et al.
Publicado: (2010)

The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
por: Galigniana, M.D., et al.
Publicado: (2010)

The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
por: Galigniana, M.D., et al.

Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore
por: Echeverría, Pablo Christian
Publicado: (2010)

Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore
por: Galigniana, M.D., et al.

The activity of the glucocorticoid receptor is regulated by SUMO conjugation to FKBP51
por: Druker, Jimena Paola, et al.
Publicado: (2016)

The activity of the glucocorticoid receptor is regulated by SUMO conjugation to FKBP51
por: Antunica-Noguerol, M., et al.

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus
Publicado: (2004)

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus
por: Galigniana, M.D., et al.
Publicado: (2004)

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus
por: Galigniana, M.D., et al.
Publicado: (2004)

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus
por: Galigniana, M.D., et al.

The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress
por: Gallo, Luciana Inés, et al.
Publicado: (2011)

The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress
por: Gallo, L.I., et al.
Publicado: (2011)

The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress
por: Gallo, L.I., et al.
Publicado: (2011)

The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress
por: Gallo, L.I., et al.

Immunophilins, protein chemistry and cell biology of a promising new class of drug targets – Part II
Publicado: (2015)

Immunophilins, protein chemistry and cell biology of a promising new class of drug targets – Part II
por: Galigniana, M.D.

Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
por: Echeverría, Pablo Christian
Publicado: (2009)

Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
por: Echeverría, P.C., et al.
Publicado: (2009)

Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
por: Echeverría, P.C., et al.
Publicado: (2009)

Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
por: Echeverría, P.C., et al.

Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
Publicado: (2004)

Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
por: Galigniana, M.D., et al.
Publicado: (2004)

Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
por: Galigniana, M.D., et al.
Publicado: (2004)

Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
por: Galigniana, M.D., et al.

NF-κB transcriptional activity is modulated by FK506-Binding proteins FKBP51 and FKBP52:A role for peptidyl-prolyl isomerase activity
por: Fontana, Vanina Andrea
Publicado: (2014)

NF-κB transcriptional activity is modulated by FK506-Binding proteins FKBP51 and FKBP52:A role for peptidyl-prolyl isomerase activity
por: Erlejman, A.G., et al.

Interaction of the stress protein p8 with Jab1 is required for Jab1-dependent p27 nuclear-to-cytoplasm translocation
por: Moreno de Colonna, Silvia
Publicado: (2006)