Evidence map›Paper›PMID 29804834›Full record

ArticleCell2018

Time-Resolved Analysis Reveals Rapid Dynamics and Broad Scope of the CBP/p300 Acetylome.

Brian T Weinert, Takeo Narita, Shankha Satpathy, Balaji Srinivasan, Bogi K Hansen, Christian Schölz, William B Hamilton, Beth E Zucconi, Wesley W Wang, Wenshe R Liu and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 303 papers.

0numbers the graph read from it
0cells of the map it votes in
303citing papers in PubMed
15.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

303 citing papers in PubMed, 521 citations in OpenAlex.

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243 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 6 institutions in 3 countries.

Brian T WeinertDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Takeo NaritaDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Shankha SatpathyDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Balaji SrinivasanDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Bogi K HansenDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Christian SchölzDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark; Max von Pettenkofer Institute, Virology, National Reference Center for Retroviruses, Faculty of Medicine, LMU München, Feodor-Lynen-Str. 23, 81377 Munich, Germany.
William B HamiltonThe Novo Nordisk Foundation Center for Stem Cell Biology-DanStem, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Beth E ZucconiDivision of Genetics, Departments of Medicine and Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Brigham & Women's Hospital, Boston, MA 02115, USA.
Wesley W WangDepartment of Chemistry, Texas A&M University, College Station, TX 77843-3255, USA.
Wenshe R LiuDepartment of Chemistry, Texas A&M University, College Station, TX 77843-3255, USA.
Joshua M BrickmanThe Novo Nordisk Foundation Center for Stem Cell Biology-DanStem, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Edward A KesickiAcylin Therapeutics, Inc., 1616 Eastlake Ave E, #200, Seattle, WA 98102, USA; Petra Pharma Corp., 430 E. 29th St. Suite 835, New York, NY 10016, USA.
Albert LaiDiscovery, Global Pharmaceutical Research and Development, AbbVie, 1 North Waukegan Road, North Chicago, IL 60064, USA.
Kenneth D BrombergDiscovery, Global Pharmaceutical Research and Development, AbbVie, 1 North Waukegan Road, North Chicago, IL 60064, USA.
Philip A ColeDivision of Genetics, Departments of Medicine and Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Brigham & Women's Hospital, Boston, MA 02115, USA.
Chunaram ChoudharyDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark. Electronic address: chuna.choudhary@cpr.ku.dk.
Novo Nordisk Foundation · DKAbbVie (United States) · USBrigham and Women's Hospital · USTexas A&M University · USUniversity of Copenhagen · DKLudwig-Maximilians-Universität München · DE

Funding

Protein Acylation and Methylation Mechanisms_Administrative SupplementR37GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2013 to 2022
$4.1M
p300/CBP and MOZ Acetyltransferase Function and Substrate SelectivityK99GM124357 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ZUCCONI, BETH · 2017 to 2018
$180k
NIGMS NIH HHS K99 GM124357NIGMS NIH HHS R37 GM062437
6 · The paper itself

Abstract

The acetyltransferases CBP and p300 are multifunctional transcriptional co-activators. Here, we combined quantitative proteomics with CBP/p300-specific catalytic inhibitors, bromodomain inhibitor, and gene knockout to reveal a comprehensive map of regulated acetylation sites and their dynamic turnover rates. CBP/p300 acetylates thousands of sites, including signature histone sites and a multitude of sites on signaling effectors and enhancer-associated transcriptional regulators. Time-resolved acetylome analyses identified a subset of CBP/p300-regulated sites with very rapid (<30 min) acetylation turnover, revealing a dynamic balance between acetylation and deacetylation. Quantification of acetylation, mRNA, and protein abundance after CBP/p300 inhibition reveals a kinetically competent network of gene expression that strictly depends on CBP/p300-catalyzed rapid acetylation. Collectively, our in-depth acetylome analyses reveal systems attributes of CBP/p300 targets, and the resource dataset provides a framework for investigating CBP/p300 functions and for understanding the impact of small-molecule inhibitors targeting its catalytic and bromodomain activities.

Indexed as

AcetylationAcetyltransferasesAnimalsCell LineGene Knockout TechniquesHalf-LifeHeterocyclic Compounds, 4 or More RingsHistonesHumansIsotope LabelingKineticsMass SpectrometryMicep300-CBP Transcription FactorsPeptidesReceptors, Aryl HydrocarbonA-485 compoundAcetyltransferasesHeterocyclic Compounds, 4 or More RingsHistonesp300-CBP Transcription FactorsPeptidesReceptors, Aryl HydrocarbonRecombinant ProteinsSmall Molecule LibrariesA-485acetylationacetylation kineticsbromodomainCBPenhancergene transcriptionmass spectrometryp300proteomics

Identifiers

PMID29804834
PMCPMC6078418
OpenAlexW2803754954

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.