cis -Proline-mediated Ser(P) 5 Dephosphorylation by the RNA Polymerase II C-terminal Domain Phosphatase Ssu72 - Wikidata - wikimedia - TriplyDB

cis -Proline-mediated Ser(P) 5 Dephosphorylation by the RNA Polymerase II C-terminal Domain Phosphatase Ssu72

cis -Proline-mediated Ser(P) 5 Dephosphorylation by the RNA Polymerase II C-terminal Domain Phosphatase Ssu72

http://www.wikidata.org/entity/Q27666319

about

JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins Prolyl isomerase Pin1 in cancer Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity.A Conserved Nuclear Cyclophilin Is Required for Both RNA Polymerase II Elongation and Co-transcriptional Splicing in Caenorhabditis elegans Structural Insights to How Mammalian Capping Enzyme Reads the CTD Code The yeast regulator of transcription protein Rtr1 lacks an active site and phosphatase activity Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72 Specific Interaction of the Transcription Elongation Regulator TCERG1 with RNA Polymerase II Requires Simultaneous Phosphorylation at Ser2, Ser5, and Ser7 within the Carboxyl-terminal Domain Repeat Novel Modifications on C-terminal Domain of RNA Polymerase II Can Fine-tune the Phosphatase Activity of Ssu72 Structural and Kinetic Analysis of Prolyl-isomerization/Phosphorylation Cross-Talk in the CTD Code Rtr1 Is a Dual Specificity Phosphatase That Dephosphorylates Tyr1 and Ser5 on the RNA Polymerase II CTD Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle.Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination.The yeast Ess1 prolyl isomerase controls Swi6 and Whi5 nuclear localization.Protein Phosphatases Involved in Regulating Mitosis: Facts and Hypotheses The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination Regulation of estrogen receptor α N-terminus conformation and function by peptidyl prolyl isomerase Pin1 Threonine-4 of mammalian RNA polymerase II CTD is targeted by Polo-like kinase 3 and required for transcriptional elongation Cell signaling, post-translational protein modifications and NMR spectroscopy RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery.Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p.The interactome of the atypical phosphatase Rtr1 in Saccharomyces cerevisiae The roles of peptidyl-proline isomerases in gene regulation.The RNA polymerase II CTD coordinates transcription and RNA processing.A gene-specific role for the Ssu72 RNAPII CTD phosphatase in HIV-1 Tat transactivation.RNA polymerase II CTD modifications: how many tales from a single tail.TAL effectors target the C-terminal domain of RNA polymerase II (CTD) by inhibiting the prolyl-isomerase activity of a CTD-associated cyclophilin.Rpb4/7 facilitates RNA polymerase II CTD dephosphorylation.Expression, purification, and identification of associated proteins of the full-length hCDK12/CyclinK complex.Vertebrate Ssu72 regulates and coordinates 3'-end formation of RNAs transcribed by RNA polymerase II.Prolyl isomerases in gene transcription Roles of Prolyl Isomerases in RNA-Mediated Gene Expression Emerging Views on the CTD Code The identification of putative RNA polymerase II C-terminal domain associated proteins in red and green algae.p63 threonine phosphorylation signals the interaction with the WW domain of the E3 ligase Itch

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cis -Proline-mediated Ser(P) 5 Dephosphorylation by the RNA Polymerase II C-terminal Domain Phosphatase Ssu72

http://www.wikidata.org/entity/Q27666319

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@ast

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@en

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@nl

type

label

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@ast

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@en

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@nl

prefLabel

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@ast

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@en

cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

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JBC.M110.197129

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Journal of Biological Chemistry

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cis -Proline-mediated Ser(P) 5 ...... minal Domain Phosphatase Ssu72

@en

P2093

Arno L Greenleaf

http://www.w3.org/2001/XMLSchema#string

Chul-Jin Lee

http://www.w3.org/2001/XMLSchema#string

Jon W Werner-Allen

http://www.w3.org/2001/XMLSchema#string

Nathan I Nicely

http://www.w3.org/2001/XMLSchema#string

Pei Zhou

http://www.w3.org/2001/XMLSchema#string

Pengda Liu

http://www.w3.org/2001/XMLSchema#string

Su Wang

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex

A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5

Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate

Structural basis for phosphoserine-proline recognition by group IV WW domains

Determinants for Dephosphorylation of the RNA Polymerase II C-Terminal Domain by Scp1

Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.

The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway

Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends.

Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation.

Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.

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scholarly article

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10.1074/JBC.M110.197129

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7

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286

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2011-02-18T00:00:00Z

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21159777

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