Evidence map›Paper›PMID 31353912›Full record

ArticleJournal of proteome research2019

Biochemical Reduction of the Topology of the Diverse WDR76 Protein Interactome.

Gerald Dayebgadoh, Mihaela E Sardiu, Laurence Florens, Michael P Washburn

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  9. The role of WDR76 protein in human diseases.Bosnian journal of basic medical sciences · 2021
    Review
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  11. Article
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  13. Article
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

4 authors at 1 institution in 1 country.

Gerald DayebgadohStowers Institute for Medical Research , Kansas City , Missouri 64110 , United States.
Mihaela E SardiuStowers Institute for Medical Research , Kansas City , Missouri 64110 , United States.
Laurence FlorensStowers Institute for Medical Research , Kansas City , Missouri 64110 , United States.ORCID 0000-0002-9310-6650
Michael P WashburnStowers Institute for Medical Research , Kansas City , Missouri 64110 , United States.ORCID 0000-0001-7568-2585
Stowers Institute for Medical Research · US

Funding

Inhibitor Reprogramming of a Human Histone Deacetylase Protein Interaction NetworkR01GM112639 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI FLORENS, LAURENCE ALEXANDRA · 2016 to 2020
$1.6M
NIGMS NIH HHS R01 GM112639
6 · The paper itself

Abstract

A hub protein in protein interaction networks will typically have a large number of diverse interactions. Determining the core interactions and the function of such a hub protein remains a significant challenge in the study of networks. Proteins with WD40 repeats represent a large class of proteins that can be hub proteins. WDR76 is a poorly characterized WD40 repeat protein with possible involvement in DNA damage repair, cell-cycle progression, apoptosis, gene expression regulation, and protein quality control. WDR76 has a large and diverse interaction network that has made its study challenging. Here we rigorously carry out a series of affinity purification coupled to mass spectrometry (AP-MS) analyses to map out the WDR76 interactome through different biochemical conditions. We apply AP-MS analysis coupled to size-exclusion chromatography to resolve WDR76-based protein complexes. Furthermore, we also show that WDR76 interacts with the CCT complex via its WD40 repeat domain and with DNA-PK-KU, PARP1, GAN, SIRT1, and histones outside of the WD40 domain. An evaluation of the stability of WDR76 interactions led to focused and streamlined reciprocal analyses that validate the interactions with GAN and SIRT1. Overall, the approaches used to study WDR76 would be valuable to study other proteins containing WD40 repeat domains, which are conserved in a large number of proteins in many organisms.

Indexed as

ApoptosisCell Cycle ProteinsCytoskeletal ProteinsDNA-Binding ProteinsDNA DamageDNA RepairGene Expression RegulationHumansMass SpectrometryPoly (ADP-Ribose) Polymerase-1Protein Interaction MapsSirtuin 1WD40 RepeatsCell Cycle ProteinsCytoskeletal ProteinsDNA-Binding ProteinsGAN protein, humanPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1SIRT1 protein, humanSirtuin 1WDR76 protein, humanAlzheimer’scancerchromatinDNA repairhub proteinprotein interaction networktopological scoringWD40 repeatWDR76

Identifiers

PMID31353912
PMCPMC7295179
OpenAlexW2966472327

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.