Resolving the functions of peptidylprolyl isomerases: insights from the mutagenesis of the nuclear FKBP25 enzyme.
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Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline IsomerizationThe emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's diseaseProlyl isomerases in gene transcriptionMolecular evolution of the vertebrate FK506 binding protein 25.Basic surface features of nuclear FKBPs facilitate chromatin binding.Structure-Function Analysis of the Periplasmic Escherichia coli Cyclophilin PpiA in Relation to Biofilm Formation.Epigenetic mechanisms in development and disease.Structural and functional analysis of cyclophilin PpiB mutants supports an in vivo function not limited to prolyl isomerization activity.The prolyl isomerase FKBP25 regulates microtubule polymerization impacting cell cycle progression and genomic stability.Proteomics and transcriptomics analyses of ataxia telangiectasia cells treated with Dexamethasone.
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Resolving the functions of peptidylprolyl isomerases: insights from the mutagenesis of the nuclear FKBP25 enzyme.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artículo científico
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name
Resolving the functions of pep ...... of the nuclear FKBP25 enzyme.
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type
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Resolving the functions of pep ...... of the nuclear FKBP25 enzyme.
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prefLabel
Resolving the functions of pep ...... of the nuclear FKBP25 enzyme.
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P2093
P2860
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P1476
Resolving the functions of pep ...... of the nuclear FKBP25 enzyme.
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P2093
Christopher J Nelson
Geoff Gudavicius
Heddy Soufari
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P304
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10.1042/BST20130013
P577
2013-06-01T00:00:00Z