Detalhe da pesquisa
1.
Spt5 C-terminal repeat domain phosphorylation and length negatively regulate heterochromatin through distinct mechanisms.
PLoS Genet
; 19(11): e1010492, 2023 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-37939109
2.
Gßγ subunits colocalize with RNA polymerase II and regulate transcription in cardiac fibroblasts.
J Biol Chem
; 299(4): 103064, 2023 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-36841480
3.
A Cdk9-PP1 switch regulates the elongation-termination transition of RNA polymerase II.
Nature
; 558(7710): 460-464, 2018 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-29899453
4.
Lipidated peptides derived from intracellular loops 2 and 3 of the urotensin II receptor act as biased allosteric ligands.
J Biol Chem
; 297(3): 101057, 2021 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-34389356
5.
Cdk9 and H2Bub1 signal to Clr6-CII/Rpd3S to suppress aberrant antisense transcription.
Nucleic Acids Res
; 48(13): 7154-7168, 2020 07 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-32496538
6.
High-Content Single-Cell Förster Resonance Energy Transfer Imaging of Cultured Striatal Neurons Reveals Novel Cross-Talk in the Regulation of Nuclear Signaling by Protein Kinase A and Extracellular Signal-Regulated Kinase 1/2.
Mol Pharmacol
; 100(6): 526-539, 2021 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-34503973
7.
New connections between ubiquitylation and methylation in the co-transcriptional histone modification network.
Curr Genet
; 67(5): 695-705, 2021 Oct.
Artigo
em Inglês
| MEDLINE | ID: mdl-34089069
8.
Therapeutic Targeting of the General RNA Polymerase II Transcription Machinery.
Int J Mol Sci
; 21(9)2020 May 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-32397434
9.
A nucleosome turnover map reveals that the stability of histone H4 Lys20 methylation depends on histone recycling in transcribed chromatin.
Genome Res
; 25(6): 872-83, 2015 Jun.
Artigo
em Inglês
| MEDLINE | ID: mdl-25778913
10.
Functional interaction of Rpb1 and Spt5 C-terminal domains in co-transcriptional histone modification.
Nucleic Acids Res
; 43(20): 9766-75, 2015 Nov 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-26275777
11.
The PAF complex and Prf1/Rtf1 delineate distinct Cdk9-dependent pathways regulating transcription elongation in fission yeast.
PLoS Genet
; 9(12): e1004029, 2013.
Artigo
em Inglês
| MEDLINE | ID: mdl-24385927
12.
A positive feedback loop links opposing functions of P-TEFb/Cdk9 and histone H2B ubiquitylation to regulate transcript elongation in fission yeast.
PLoS Genet
; 8(8): e1002822, 2012.
Artigo
em Inglês
| MEDLINE | ID: mdl-22876190
13.
The Rtf1/Prf1-dependent histone modification axis counteracts multi-drug resistance in fission yeast.
Life Sci Alliance
; 7(6)2024 Jun.
Artigo
em Inglês
| MEDLINE | ID: mdl-38514187
14.
Histone H2B ubiquitylation promotes activity of the intact Set1 histone methyltransferase complex in fission yeast.
J Biol Chem
; 287(23): 19040-7, 2012 Jun 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-22505722
15.
Comparing the signaling and transcriptome profiling landscapes of human iPSC-derived and primary rat neonatal cardiomyocytes.
Sci Rep
; 13(1): 12248, 2023 07 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-37507481
16.
Decoding histone ubiquitylation.
Front Cell Dev Biol
; 10: 968398, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-36105353
17.
A role for BET proteins in regulating basal, dopamine-induced and cAMP/PKA-dependent transcription in rat striatal neurons.
Cell Signal
; 91: 110226, 2022 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-34974082
18.
Differential Activation of P-TEFb Complexes in the Development of Cardiomyocyte Hypertrophy following Activation of Distinct G Protein-Coupled Receptors.
Mol Cell Biol
; 40(14)2020 06 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-32341082
19.
Dopamine D1 receptor signalling in dyskinetic Parkinsonian rats revealed by fiber photometry using FRET-based biosensors.
Sci Rep
; 10(1): 14426, 2020 09 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-32879346
20.
Spt5 Phosphorylation and the Rtf1 Plus3 Domain Promote Rtf1 Function through Distinct Mechanisms.
Mol Cell Biol
; 40(15)2020 07 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-32366382