Evidence map›Paper›PMID 34567831›Full record

ArticleACS catalysis2020

What Does the Brønsted Slope Measure in the Phosphoryl Transfer Transition State?

Rui Lai, Qiang Cui

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS catalysis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. The journal of physical chemistry. C, Nanomaterials and interfaces · 2025
    Article
  2. Article
  3. Article
  4. 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

2 authors.

Rui LaiDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215.
Qiang CuiDepartments of Chemistry, Physics and Biomedical Engineering, Boston University, 590 Commonwealth Avenue, Boston, MA 02215.

Funding

Development and application of QM/MM methods for metalloenzymesR01GM106443 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CUI, QIANG · 2013 to 2020
$2.3M
NIGMS NIH HHS R01 GM106443
6 · The paper itself

Abstract

The structural and energetic features of phosphate and phosphonate hydrolysis in Protein Phosphatase-1 (PP1) and water are studied using quantum mechanical (QM) cluster models. The calculations are able to reproduce observed kinetic isotope effects and capture several key trends in the experimental Brønsted plots: the

Indexed as

Brønsted slopefree energy relationphosphoryl transferquantum mechanical cluster modelstransition state

Identifiers

PMID34567831
PMCPMC8457673

What OpenQuestion holds

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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.