Evidence map›Paper›PMID 36239559›Full record

ReviewFEBS letters2023

Dynamical activation of function in metalloenzymes.

Judith P Klinman

Open access · greenAbstract readReview
In one paragraph

Review in FEBS letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
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  9. 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
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

1 author at 1 institution in 1 country.

Judith P KlinmanDepartment of Chemistry, University of California, Berkeley, CA, USA.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
NIGMS NIH HHS R35 GM118117
6 · The paper itself

Abstract

Formulations of hydrogen tunneling in enzyme-catalysed C-H activation reactions indicate enthalpic barriers to reaction that are independent of chemical steps and dependent on the protein scaffold. A tool to identify catalytically relevant site-specific protein thermal networks has emerged from temperature-dependent hydrogen deuterium exchange (TDHDX). Focusing on mutant enzyme forms with altered activation energies for catalysis, TDHDX provides a comparative analysis of the impact of mutation on E

Indexed as

HydrogenProteinsCatalysisKineticsLipoxygenaseModels, MolecularTemperatureThermodynamicsHydrogenLipoxygenaseProteinsC-H activation by tunnelingmetalloenzymesprotein dynamicstemperature-dependent hydrogen deuterium exchangethermal networkstime-resolved protein motions

Identifiers

PMID36239559
PMCPMC9839491
OpenAlexW4306175367

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.