Evidence map›Paper›PMID 38501487›Full record

ArticleProtein science : a publication of the Protein Society2024

Calcium mediated static and dynamic allostery in S100A12: Implications for target recognition by S100 proteins.

Qian Wang, Christopher DiForte, Aleksey Aleshintsev, Gianna Elci, Shibani Bhattacharya, Angelo Bongiorno, Rupal Gupta

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 at 3 institutions in 1 country.

Qian WangDepartment of Chemistry, College of Staten Island, City University of New York, New York, United States.
Christopher DiForteDepartment of Chemistry, College of Staten Island, City University of New York, New York, United States.
Aleksey AleshintsevDepartment of Chemistry, College of Staten Island, City University of New York, New York, United States.
Gianna ElciDepartment of Chemistry, College of Staten Island, City University of New York, New York, United States.
Shibani BhattacharyaNew York Structural Biology Center, New York, New York, United States.ORCID 0000-0002-7706-9167
Angelo BongiornoDepartment of Chemistry, College of Staten Island, City University of New York, New York, United States.
Rupal GuptaDepartment of Chemistry, College of Staten Island, City University of New York, New York, United States.ORCID 0000-0001-8637-6129
The Graduate Center, CUNY · USCollege of Staten Island · USNew York Structural Biology Center · US

Funding

TR&D4: Integrated pipeline for data analysisP41GM118302 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI PALMER, ARTHUR G · 2017 to 2021
$8.5M
RM1 Center on Macromolecular Dynamics by NMR Spectroscopy at the New York Structural Biology Center (CoMD/NMR)- Equipment Supplement RequestRM1GM145397 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI ARTHUR G PALMER · 2022 to 2026
$8.3M
Interdependence of Antimicrobial and Pro-inflammatory Activities Mediated byS100A12 in the Innate Immune ResponseR15GM131338 · NIGMS · COLLEGE OF STATEN ISLAND · PI GUPTA, RUPAL · 2019 to 2022
$936k
NIGMS NIH HHS P41 GM118302NIGMS NIH HHS R15 GM131338NIGMS NIH HHS RM1 GM145397NIH HHS
6 · The paper itself

Abstract

Structure and functions of S100 proteins are regulated by two distinct calcium binding EF hand motifs. In this work, we used solution-state NMR spectroscopy to investigate the cooperativity between the two calcium binding sites and map the allosteric changes at the target binding site. To parse the contribution of the individual calcium binding events, variants of S100A12 were designed to selectively bind calcium to either the EF-I (N63A) or EF-II (E31A) loop, respectively. Detailed analysis of the backbone chemical shifts for wildtype protein and its mutants indicates that calcium binding to the canonical EF-II loop is the principal trigger for the conformational switch between 'closed' apo to the 'open' Ca

Indexed as

S100A12 ProteinS100 ProteinsCalciumCalcium-Binding ProteinsEF Hand MotifsPeptidesProtein ConformationCalciumCalcium-Binding ProteinsPeptidesS100A12 ProteinS100 Proteinscalcium binding proteinsmolecular dynamics simulationsNMR spectroscopyS100 proteins

Identifiers

PMID38501487
PMCPMC10949321
OpenAlexW4392956460

What Socratic holds

Textmetadata
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 Socratic graph.