Evidence map›Paper›PMID 32133840›Full record

ArticleBiochemistry2020

Comparative Analysis of CPI-Motif Regulation of Biochemical Functions of Actin Capping Protein.

Patrick McConnell, Marlene Mekel, Alexander G Kozlov, Olivia L Mooren, Timothy M Lohman, John A Cooper

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 20 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Patrick McConnellDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.
Marlene MekelDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.
Alexander G KozlovDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.
Olivia L MoorenDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.
Timothy M LohmanDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.
John A CooperDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.ORCID 0000-0002-0933-4571
Washington University in St. Louis · US

Funding

SSB PROTEIN/DNA INTERACTIONSR01GM030498 · NIGMS · WASHINGTON UNIVERSITY · PI LOHMAN, TIMOTHY M · 1985 to 2019
$7.4M
ACTIN ASSEMBLY AND CELL MOTILITY: MECHANISMS AND REGULATIONR35GM118171 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2016 to 2020
$2.8M
NIGMS NIH HHS R01 GM030498NIGMS NIH HHS R35 GM118171
6 · The paper itself

Abstract

The heterodimeric actin capping protein (CP) is regulated by a set of proteins that contain CP-interacting (CPI) motifs. Outside of the CPI motif, the sequences of these proteins are unrelated and distinct. The CPI motif and surrounding sequences are conserved within a given protein family, when compared to those of other CPI-motif protein families. Using biochemical assays with purified proteins, we compared the ability of CPI-motif-containing peptides from different protein families (a) to bind to CP, (b) to allosterically inhibit barbed-end capping by CP, and (c) to allosterically inhibit interaction of CP with V-1, another regulator of CP. We found large differences in potency among the different CPI-motif-containing peptides, and the different functional assays showed different orders of potency. These biochemical differences among the CPI-motif peptides presumably reflect interactions between CP and CPI-motif peptides involving amino acid residues that are conserved but are not part of the strictly defined consensus, as it was originally identified in comparisons of sequences of CPI motifs across all protein families [Hernandez-Valladares, M., et al. (2010) Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.

Indexed as

ActinsAllosteric RegulationAmino Acid MotifsAnimalsCapZ Actin Capping ProteinDimerizationEukaryotaHumansKineticsPeptidesPhylogenyProtein BindingProtein ConformationProtein Interaction Domains and MotifsActinsCapza1 protein, mouseCapZ Actin Capping ProteinCAPZB protein, mousePeptides

Identifiers

PMID32133840
PMCPMC7301643
OpenAlexW3010275022

What OpenQuestion holds

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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.