The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding

The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding

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http://www.wikidata.org/entity/Q24302291
Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation.The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in HominidaeSmall family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical researchStructural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate bindingThe transcriptional repressor Glis2 is a novel binding partner for p120 cateninParvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Epigenetic investigation of variably X chromosome inactivated genes in monozygotic female twins discordant for primary biliary cirrhosis.Novel targets in drug design: enzymes in the protein ubiquitylation pathway.Identification and characterization of peptides that bind the PPIase domain of Parvulin17.Human DNA-binding peptidyl-prolyl cis/trans isomerase Par14 is cell cycle dependently expressed and associates with chromatin in vivo.Roles of Prolyl Isomerases in RNA-Mediated Gene ExpressionUnraveling the role of peptidyl-prolyl isomerases in neurodegeneration.Par14 protein associates with insulin receptor substrate 1 (IRS-1), thereby enhancing insulin-induced IRS-1 phosphorylation and metabolic actions.Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases.Molecular and biochemical characterization of the parvulin-type PPIases in Lotus japonicus.
P2860

The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding

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http://www.wikidata.org/entity/Q24302291
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2002 nî lūn-bûn
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2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
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2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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The N-terminal basic domain of ...... and high-affinity DNA-binding
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10.1016/S0022-2836(02)00615-0
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