Evidence map›Paper›PMID 26332992›Full record

ArticleAngewandte Chemie (International ed. in English)2015

Resolution of Stepwise Cooperativities of Copper Binding by the Homotetrameric Copper-Sensitive Operon Repressor (CsoR): Impact on Structure and Stability.

Alexander D Jacobs, Feng-Ming James Chang, Lindsay Morrison, Jonathan M Dilger, Vicki H Wysocki, David E Clemmer, David P Giedroc

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 19 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

7 authors at 2 institutions in 1 country.

Alexander D JacobsDepartment of Chemistry, Indiana University, Bloomington, IN 47405-7102 (USA).
Feng-Ming James ChangDepartment of Chemistry, Indiana University, Bloomington, IN 47405-7102 (USA).
Lindsay MorrisonDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210 (USA).
Jonathan M DilgerDepartment of Chemistry, Indiana University, Bloomington, IN 47405-7102 (USA).
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210 (USA).
David E ClemmerDepartment of Chemistry, Indiana University, Bloomington, IN 47405-7102 (USA).
David P GiedrocDepartment of Chemistry, Indiana University, Bloomington, IN 47405-7102 (USA). giedroc@indiana.edu.
Indiana University Bloomington · USThe Ohio State University · US

Funding

ZINC COORDINATION AND REGULATION OF ZINC METALLOPROTEINSR01GM042569 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 1996 to 2015
$4.9M
NIGMS NIH HHS R01 GM042569
6 · The paper itself

Abstract

The cooperativity of ligand binding is central to biological regulation and new approaches are needed to quantify these allosteric relationships. Herein, we exploit a suite of mass spectrometry (MS) experiments to provide novel insights into homotropic Cu-binding cooperativity, gas-phase stabilities and conformational ensembles of the D2 -symmetric, homotetrameric copper-sensitive operon repressor (CsoR) as a function of Cu(I) ligation state. Cu(I) binding is overall positively cooperative, but is characterized by distinct ligation state-specific cooperativities. Structural transitions occur upon binding the first and fourth Cu(I) , with the latter occurring with significantly higher cooperativity than previous steps; this results in the formation of a holo-tetramer that is markedly more resistant than apo-, and partially ligated CsoR tetramers toward surface-induced dissociation (SID).

Indexed as

CopperGeobacillusModels, MolecularOperonProtein ConformationProtein MultimerizationProtein StabilityRepressor ProteinsCopperRepressor Proteinsallosterycoppermetalloproteinsmetalloregulationsurface-induced dissociation

Identifiers

PMID26332992
PMCPMC4673887
OpenAlexW2097995578

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.