Evidence map›Paper›PMID 31508957›Full record

ArticleJournal of the American Chemical Society2019

Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate Isomerase.

Yashraj S Kulkarni, Tina L Amyes, John P Richard, Shina C L Kamerlin

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2019. 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 22% 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, 23 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

4 authors at 2 institutions in 2 countries.

Yashraj S KulkarniScience for Life Laboratory, Department of Chemistry - BMC , Uppsala University, BMC , Box 576, S-751 23 Uppsala , Sweden.
Tina L AmyesDepartment of Chemistry , University at Buffalo, SUNY , Buffalo , New York 14260-3000 , United States.
John P RichardDepartment of Chemistry , University at Buffalo, SUNY , Buffalo , New York 14260-3000 , United States.ORCID 0000-0002-0440-2387
Shina C L KamerlinScience for Life Laboratory, Department of Chemistry - BMC , Uppsala University, BMC , Box 576, S-751 23 Uppsala , Sweden.ORCID 0000-0002-3190-1173
University at Buffalo, State University of New York · USUppsala University · SE

Funding

REACTIVE INTERMEDIATES OF ENZYMATIC REACTIONSR01GM039754 · NIGMS · UNIVERSITY OF KENTUCKY · PI RICHARD, JOHN P · 1993 to 2012
$3.9M
Activation of Enzymes for Catalysis: The Role of Substrate-Induced Structural ChangesR01GM116921 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI RICHARD, JOHN P · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM039754NIGMS NIH HHS R01 GM116921
6 · The paper itself

Abstract

We report results of detailed empirical valence bond simulations that model the effect of several amino acid substitutions on the thermodynamic (Δ

Indexed as

ProtonsAmino AcidsAmino Acid SubstitutionCatalysisCatalytic DomainDihydroxyacetone PhosphateGlyceraldehyde 3-PhosphateKineticsModels, MolecularMutationThermodynamicsTriose-Phosphate IsomeraseAmino AcidsDihydroxyacetone PhosphateGlyceraldehyde 3-PhosphateProtonsTriose-Phosphate Isomerase

Identifiers

PMID31508957
PMCPMC7032883
OpenAlexW2973182365

What OpenQuestion 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 OpenQuestion graph.