Evidence map›Paper›PMID 38456823›Full record

ArticleJournal of the American Chemical Society2024

Flexibility of Binding Site is Essential to the Ca

Rui Lai, Guohui Li, Qiang Cui

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

8 citing papers in PubMed, 12 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

3 authors at 2 institutions in 2 countries.

Rui LaiDalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023, China.ORCID 0000-0003-1300-8039
Guohui LiDalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023, China.ORCID 0000-0001-8223-705X
Qiang CuiDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States.ORCID 0000-0001-6214-5211
Boston University · USDalian Institute of Chemical Physics · CN

Funding

Computational Analysis of Enzyme Catalysis and RegulationR35GM141930 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI Qiang Cui · 2021 to 2026
$2.7M
NIGMS NIH HHS R35 GM141930
6 · The paper itself

Abstract

High binding affinity and selectivity of metal ions are essential to the function of metalloproteins. Thus, understanding the factors that determine these binding characteristics is of major interest for both fundamental mechanistic investigations and guiding of the design of novel metalloproteins. In this work, we perform QM cluster model calculations and quantum mechanics/molecular mechanics (QM/MM) free energy simulations to understand the binding selectivity of Ca

Indexed as

Calcium-Binding ProteinsMetalloproteinsBinding SitesIonsProtein BindingCalcium-Binding ProteinsIonsMetalloproteins

Identifiers

PMID38456823
PMCPMC11102802
OpenAlexW4392600298

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.