Evidence map›Paper›PMID 33395523›Full record

ArticleJournal of the American Chemical Society2021

Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase.

Emily J Thompson, Adhayana Paul, Anthony T Iavarone, Judith P Klinman

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023
    Review
  12. Article
  13. Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Review
  15. Article
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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 1 institution in 1 country.

Emily J ThompsonDepartment of Chemistry, University of California, Berkeley, California 94720, United States.ORCID 0000-0003-4624-7239
Adhayana PaulDepartment of Chemistry, University of California, Berkeley, California 94720, United States.
Anthony T IavaroneDepartment of Chemistry, University of California, Berkeley, California 94720, United States.
Judith P KlinmanDepartment of Chemistry, University of California, Berkeley, California 94720, United States.ORCID 0000-0001-5734-2843
QB3 · US

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
High Definition Ion Mobility SpectrometerS10OD020062 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2015 to 2015
$590k
Acquisition of a Cryoprobe and Related Accessories for a 600 MHz NMR Spectrometer to Support Health Research Activities at the University of California, BerkeleyS10OD024998 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI HARTWIG, JOHN F · 2018 to 2018
$265k
Linking specific macromolecular motions to enzyme rate acceleration in the TIM barrelsuperfamily of proteinsF32GM130031 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THOMPSON, EMILY JORDAN · 2019 to 2020
$78k
NIGMS NIH HHS F32 GM130031NIGMS NIH HHS R35 GM118117NIH HHS S10 OD020062NIH HHS S10 OD024998
6 · The paper itself

Abstract

We report here on the salient role of protein mobility in accessing conformational landscapes that enable efficient enzyme catalysis. We are focused on yeast enolase, a highly conserved lyase with a TIM barrel domain and catalytic loop, as part of a larger study of the relationship of site selective protein motions to chemical reactivity within superfamilies. Enthalpically hindered variants were developed by replacement of a conserved hydrophobic side chain (Leu 343) with smaller side chains. Leu343 is proximal to the active site base in enolase, and comparative pH rate profiles for the valine and alanine variants indicate a role for side chain hydrophobicity in tuning the p

Indexed as

TemperatureBinding SitesBiocatalysisKineticsLyasesModels, MolecularMutationSaccharomyces cerevisiaeWaterLyasesWater

Identifiers

PMID33395523
PMCPMC7908892
OpenAlexW3118887487

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.