Hsp90-binding immunophilins as a potential new platform for drug treatment
Immunophilins are proteins that contain a PPIase domain as a family signature. Low-molecular-weight immunophilins were first described associated to immunosuppressive action and protein folding. Recent studies of other members of the family have led to the identification of their participation in ba...
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paper:paper_17568919_v5_n5_p591_Erlejman2023-06-08T16:28:56Z Hsp90-binding immunophilins as a potential new platform for drug treatment Lagadari, Mariana alisporivir apolipoprotein E corticosteroid receptor cyclin D1 cyclosporin A fk 506 binding protein glucocorticoid receptor heat shock protein 90 immunophilin rapamycin tacrolimus transcription factor YY1 Alzheimer disease amino acid sequence apoptosis breast carcinoma cell activity cell cycle progression cell differentiation cell metabolism chromatin assembly and disassembly chromatin structure colorectal carcinoma genetic transcription hepatitis C human immunoreactivity metastatic melanoma molecular weight nerve cell differentiation neuroprotection neurotropism nonhuman pathophysiology phase 3 clinical trial (topic) priority journal prostate carcinoma protein folding protein motif protein protein interaction protein transport review signal transduction tetratricopeptide repeat transcription initiation transcription regulation Animals Drug Discovery HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms Neurogenesis Protein Binding Protein Transport Transcriptional Activation Immunophilins are proteins that contain a PPIase domain as a family signature. Low-molecular-weight immunophilins were first described associated to immunosuppressive action and protein folding. Recent studies of other members of the family have led to the identification of their participation in basic processes such as protein-protein interactions, signal transduction cascades, cell differentiation, cell cycle progression, metabolic activity, apoptosis mechanisms, microorganisms infection, cancer, neurotrophism and neuroprotection, among several other physiological and pathophysiological processes. Due to all these emerging features, the development of specific ligands for immunophilins appears to have promising perspectives, in particular in the fields of cancer biology and neuroregeneration fields. We review the emerging role of immunophilins in protein transport, transcription regulation, malignancies development and neurotrophic action, in addition to a number of biological properties that transform these proteins in potential targets for novel therapeutic strategies. © 2013 Future Science Ltd. Fil:Lagadari, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_17568919_v5_n5_p591_Erlejman http://hdl.handle.net/20.500.12110/paper_17568919_v5_n5_p591_Erlejman |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
alisporivir apolipoprotein E corticosteroid receptor cyclin D1 cyclosporin A fk 506 binding protein glucocorticoid receptor heat shock protein 90 immunophilin rapamycin tacrolimus transcription factor YY1 Alzheimer disease amino acid sequence apoptosis breast carcinoma cell activity cell cycle progression cell differentiation cell metabolism chromatin assembly and disassembly chromatin structure colorectal carcinoma genetic transcription hepatitis C human immunoreactivity metastatic melanoma molecular weight nerve cell differentiation neuroprotection neurotropism nonhuman pathophysiology phase 3 clinical trial (topic) priority journal prostate carcinoma protein folding protein motif protein protein interaction protein transport review signal transduction tetratricopeptide repeat transcription initiation transcription regulation Animals Drug Discovery HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms Neurogenesis Protein Binding Protein Transport Transcriptional Activation |
spellingShingle |
alisporivir apolipoprotein E corticosteroid receptor cyclin D1 cyclosporin A fk 506 binding protein glucocorticoid receptor heat shock protein 90 immunophilin rapamycin tacrolimus transcription factor YY1 Alzheimer disease amino acid sequence apoptosis breast carcinoma cell activity cell cycle progression cell differentiation cell metabolism chromatin assembly and disassembly chromatin structure colorectal carcinoma genetic transcription hepatitis C human immunoreactivity metastatic melanoma molecular weight nerve cell differentiation neuroprotection neurotropism nonhuman pathophysiology phase 3 clinical trial (topic) priority journal prostate carcinoma protein folding protein motif protein protein interaction protein transport review signal transduction tetratricopeptide repeat transcription initiation transcription regulation Animals Drug Discovery HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms Neurogenesis Protein Binding Protein Transport Transcriptional Activation Lagadari, Mariana Hsp90-binding immunophilins as a potential new platform for drug treatment |
topic_facet |
alisporivir apolipoprotein E corticosteroid receptor cyclin D1 cyclosporin A fk 506 binding protein glucocorticoid receptor heat shock protein 90 immunophilin rapamycin tacrolimus transcription factor YY1 Alzheimer disease amino acid sequence apoptosis breast carcinoma cell activity cell cycle progression cell differentiation cell metabolism chromatin assembly and disassembly chromatin structure colorectal carcinoma genetic transcription hepatitis C human immunoreactivity metastatic melanoma molecular weight nerve cell differentiation neuroprotection neurotropism nonhuman pathophysiology phase 3 clinical trial (topic) priority journal prostate carcinoma protein folding protein motif protein protein interaction protein transport review signal transduction tetratricopeptide repeat transcription initiation transcription regulation Animals Drug Discovery HSP90 Heat-Shock Proteins Humans Immunophilins Neoplasms Neurogenesis Protein Binding Protein Transport Transcriptional Activation |
description |
Immunophilins are proteins that contain a PPIase domain as a family signature. Low-molecular-weight immunophilins were first described associated to immunosuppressive action and protein folding. Recent studies of other members of the family have led to the identification of their participation in basic processes such as protein-protein interactions, signal transduction cascades, cell differentiation, cell cycle progression, metabolic activity, apoptosis mechanisms, microorganisms infection, cancer, neurotrophism and neuroprotection, among several other physiological and pathophysiological processes. Due to all these emerging features, the development of specific ligands for immunophilins appears to have promising perspectives, in particular in the fields of cancer biology and neuroregeneration fields. We review the emerging role of immunophilins in protein transport, transcription regulation, malignancies development and neurotrophic action, in addition to a number of biological properties that transform these proteins in potential targets for novel therapeutic strategies. © 2013 Future Science Ltd. |
author |
Lagadari, Mariana |
author_facet |
Lagadari, Mariana |
author_sort |
Lagadari, Mariana |
title |
Hsp90-binding immunophilins as a potential new platform for drug treatment |
title_short |
Hsp90-binding immunophilins as a potential new platform for drug treatment |
title_full |
Hsp90-binding immunophilins as a potential new platform for drug treatment |
title_fullStr |
Hsp90-binding immunophilins as a potential new platform for drug treatment |
title_full_unstemmed |
Hsp90-binding immunophilins as a potential new platform for drug treatment |
title_sort |
hsp90-binding immunophilins as a potential new platform for drug treatment |
publishDate |
2013 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_17568919_v5_n5_p591_Erlejman http://hdl.handle.net/20.500.12110/paper_17568919_v5_n5_p591_Erlejman |
work_keys_str_mv |
AT lagadarimariana hsp90bindingimmunophilinsasapotentialnewplatformfordrugtreatment |
_version_ |
1768545575309934592 |