Evidence map›Paper›PMID 39366370›Full record

ArticleStructure (London, England : 1993)2024

Probing hot spots of protein-protein interactions mediated by the safety-belt region of REV7.

Radha Charan Dash, Gianluca A Arianna, Seema M Patel, Alessandro A Rizzo, Noah J Harrahill, Dmitry M Korzhnev, M Kyle Hadden

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

7 authors.

Radha Charan DashDepartment of Pharmaceutical Sciences, University of Connecticut, 69 N Eagleville Rd, Unit 3092, Storrs, CT 06269-3092, USA.
Gianluca A AriannaDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA.
Seema M PatelDepartment of Pharmaceutical Sciences, University of Connecticut, 69 N Eagleville Rd, Unit 3092, Storrs, CT 06269-3092, USA.
Alessandro A RizzoDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA.
Noah J HarrahillDepartment of Pharmaceutical Sciences, University of Connecticut, 69 N Eagleville Rd, Unit 3092, Storrs, CT 06269-3092, USA.
Dmitry M KorzhnevDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA. Electronic address: korzhniev@uchc.edu.
M Kyle HaddenDepartment of Pharmaceutical Sciences, University of Connecticut, 69 N Eagleville Rd, Unit 3092, Storrs, CT 06269-3092, USA. Electronic address: kyle.hadden@uconn.edu.

Funding

Inhibition of Translesion Synthesis as a Novel Strategy for Cancer ChemotherapyR01CA233959 · NCI · UNIVERSITY OF CONNECTICUT STORRS · PI HADDEN, MATTHEW KYLE, KORZHNEV, DMITRY M. · 2019 to 2023
$2.5M
NCI NIH HHS R01 CA233959
6 · The paper itself

Abstract

REV7 is a HORMA (Hop1, Rev7, Mad2) family adaptor protein best known as an accessory subunit of the translesion synthesis (TLS) DNA polymerase ζ (Polζ). In this role, REV7 binds REV3, the catalytic subunit of Polζ, by locking REV7-binding motifs (RBMs) in REV3 underneath the REV7 safety-belt loop. The same mechanism is used by REV7 to interact with RBMs from other proteins in DNA damage response (DDR) and mitosis. Because of the importance of REV7 for TLS and other DDR pathways, targeting REV7:RBM protein-protein interactions (PPIs) with small molecules has emerged as a strategy to enhance cancer response to genotoxic chemotherapy. To identify druggable pockets at the REV7:RBM interface, we performed computational analyses of REV7 complexed with several RBM partners. The contributions of different interface regions to REV7:RBM stabilization were corroborated experimentally. These studies provide insights into key intermolecular interactions and establish targetable regions of REV7 for the design of REV7:RBM PPI inhibitors.

Indexed as

DNA-Directed DNA PolymeraseMad2 ProteinsProtein BindingBinding SitesDNA-Binding ProteinsHumansModels, MolecularProtein Interaction Domains and MotifsDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA polymerase zetaMAD2L2 protein, humanMad2 Proteinsenergy decompositionsfluorescence polarizationmolecular dynamicsprotein-protein interactionREV3REV7translesion synthesis

Identifiers

PMID39366370
PMCPMC11631137

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Registered trials

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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.