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Phosphorylation Control of Nuclear Receptors | SpringerLink
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Most transcription factors including nuclear receptors (NRs) act as sensors of the extracellular and intracellular compartments. As such, NRs serve as integrating platforms for a variety of stimuli and are targets for Post-translational modifications such as...
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Keywords {🔍}
google, scholar, pubmed, article, cas, phosphorylation, receptor, biol, mol, nuclear, protein, estrogen, cell, alpha, methods, receptors, transcription, rochetteegly, endocrinol, acid, activation, function, analysis, activity, res, human, information, biochem, steroid, retinoic, kinase, chem, site, nrs, mass, sites, signaling, binding, embo, interactions, serine, cancer, privacy, cookies, content, data, publish, factors, protocol, prediction,
Topics {✒️}
peptidyl-prolyl cis/trans isomerases christine ferry & cécile rochette-egly understand oestrogen-receptor-mediated transcription retinoic acid receptor-alpha glucocorticoid receptor phospho-isoforms phospho-specific antibodies allowed hormone-dependent nuclear export phosphate-modified nucleotides ubiquitin-proteasome pathway polices nuclear receptor-dependent transcription nuclear receptor-directed initiation p38mapk/msk1 directs raralpha alpha-helix stability mitogen-activated protein kinase represses rargamma-mediated transcription serine/threonine-rich motif high confidence determination site-specific phosphorylation dynamics phosphorylation site-specific antibodies large-scale phosphorylation analysis specific protein-protein interactions regulates estrogen sensitivity cécile rochette-egly oestrogen receptor-alpha n-terminal domain estrogen receptor alpha privacy choices/manage cookies receptor alpha loses phosphorylated af-1 domain breast cancer cells ligand-dependent phosphorylation phosphoproteomics toolbox human oestrogen receptor post-translational modifications proteolytic peptide mapping phosphoamino acid composition nuclear receptors protocol synergy control motif quantitative mass spectrometry nuclear localization signals estrogen receptor beta study steroid receptor nuclear receptor factsbook retinoic acid ligand-dependent interaction human progesterone receptor steroid receptor phosphorylation probability-based approach estrogen receptor isolated glucocorticoid-induced genes
Questions {❓}
- Shaw PE (2007) Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?
Schema {🗺️}
ScholarlyArticle:
headline:Phosphorylation Control of Nuclear Receptors
pageEnd:266
pageStart:251
image:https://media.springernature.com/w153/springer-static/cover/book/978-1-60761-738-9.jpg
genre:
Springer Protocols
isPartOf:
name:Transcription Factors
isbn:
978-1-60761-738-9
978-1-60761-737-2
type:Book
publisher:
name:Humana Press
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Sébastien Lalevée
affiliation:
name:Institut de Genetique et de Biologie Molecularie et Cellulaire
address:
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
type:PostalAddress
type:Organization
type:Person
name:Christine Ferry
affiliation:
name:Institut de Genetique et de Biologie Molecularie et Cellulaire
address:
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
type:PostalAddress
type:Organization
type:Person
name:Cécile Rochette-Egly
affiliation:
name:Institut de Genetique et de Biologie Molecularie et Cellulaire
address:
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
type:PostalAddress
type:Organization
email:[email protected]
type:Person
keywords:Phosphorylation, Nuclear receptors, Phosphoproteomics, Mass spectrometry, Phosphorylation sites databases, Phosphorylation site-specific antibodies, FRAP, ChIP
description:Most transcription factors including nuclear receptors (NRs) act as sensors of the extracellular and intracellular compartments. As such, NRs serve as integrating platforms for a variety of stimuli and are targets for Post-translational modifications such as phosphorylations. During the last decade, knowledge of NRs phosphorylation advanced considerably because of the emergence of new technologies. Indeed, the development of a wide range of phosphorylation site databases, high accuracy mass spectrometry, and phospho-specific antibodies allowed the identification of multiple novel phosphorylation sites in NRs. New and improved methods also emerge to connect these data with the downstream consequences of phosphorylation on NRs structure (computational prediction, NMR), intracellular localization (FRAP), interaction with coregulators (proteomics, FRET, FLIM), and affinity for DNA (ChIP, ChIP-seq, FRAP). In the future, such integrated strategies should provide data with a treasure-trove of information about the integration of numerous signaling events by NRs.
datePublished:2010
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isbn:
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978-1-60761-737-2
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name:Institut de Genetique et de Biologie Molecularie et Cellulaire
address:
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
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name:Institut de Genetique et de Biologie Molecularie et Cellulaire
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address:
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
type:PostalAddress
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name:Cécile Rochette-Egly
affiliation:
name:Institut de Genetique et de Biologie Molecularie et Cellulaire
address:
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
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name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
name:Department of Functional Denomics, Institut de Genetique et de Biologie Molecularie et Cellulaire, Strasbourg, France
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