Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation (Q27938452)

PubMed

1 December 2016

title

Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation (English)

1 reference

PubMed

Peptidylprolyl isomerase ESS1 YJR017C

1 December 2016

main subject

1 reference

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

D P Morris

series ordinal

1

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H P Phatnani

series ordinal

2

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A L Greenleaf

series ordinal

3

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publication date

29 October 1999

0 references

language of work or name

English

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published in

1 reference

PubMed

Tails of RNA polymerase II.

1 December 2016

volume

274

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issue

44

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page(s)

31583-7

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cites work

1 reference

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A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II.

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RNA polymerase II holoenzymes and subcomplexes.

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RNA polymerase II as a control panel for multiple coactivator complexes

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Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: correlations with gene activity and transcript processing

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Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation

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RNA polymerase II holoenzyme and transcriptional regulation

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mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain

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5′-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II

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Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme

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A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing

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Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA

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A CTD function linking transcription to splicing

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Phosphorylated RNA polymerase II stimulates pre-mRNA splicing

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The C-terminal domain of RNA polymerase II couples mRNA processing to transcription

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RNA polymerase II is an essential mRNA polyadenylation factor

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Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae

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Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae

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All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae

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The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae

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A human peptidyl-prolyl isomerase essential for regulation of mitosis

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Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism

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The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins

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The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1

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Function of WW domains as phosphoserine- or phosphothreonine-binding modules

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The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent cyclin-cyclin-dependent kinase complex

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A protein kinase that phosphorylates the C-terminal repeat domain of the largest subunit of RNA polymerase II

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Assaying CTD Kinasesin Vitroand Phosphorylation-Modulated Properties of RNA Polymerase IIin Vivo

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Interaction of WW Domains with Hematopoietic Transcription Factor p45/NF-E2 and RNA Polymerase II

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Functional domains of the Rsp5 ubiquitin-protein ligase.

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Using Molecular Repertoires to Identify High-Affinity Peptide Ligands of the WW Domain of Human and Mouse YAP

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Identifiers

DOI

10.1074/JBC.274.44.31583

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017