Evidence map›Paper›PMID 37414058›Full record

ArticleJournal of the American Chemical Society2023

Nuclear Resonance Vibrational Spectroscopy Definition of Peroxy Intermediates in Catechol Dioxygenases: Factors that Determine Extra- versus Intradiol Cleavage.

Jeffrey T Babicz, Melanie S Rogers, Dory E DeWeese, Kyle D Sutherlin, Rahul Banerjee, Lars H Böttger, Yoshitaka Yoda, Nobumoto Nagasawa, Makina Saito, Shinji Kitao and 6 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. 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

16 authors at 7 institutions in 2 countries.

Jeffrey T BabiczDepartment of Chemistry, Stanford University, 380 Roth Way, Stanford, California 94305, United States.ORCID 0000-0002-1476-8390
Melanie S RogersDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55391, United States.ORCID 0000-0002-2657-7065
Dory E DeWeeseDepartment of Chemistry, Stanford University, 380 Roth Way, Stanford, California 94305, United States.
Kyle D SutherlinDepartment of Chemistry, Stanford University, 380 Roth Way, Stanford, California 94305, United States.
Rahul BanerjeeDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55391, United States.
Lars H BöttgerDepartment of Chemistry, Stanford University, 380 Roth Way, Stanford, California 94305, United States.ORCID 0000-0003-3436-3451
Yoshitaka YodaJapan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Nobumoto NagasawaJapan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Makina SaitoDepartment of Physics, Tohoku University, Sendai, Miyagi 980-8578, Japan.
Shinji KitaoInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.
Masayuki KurokuzuInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.
Yasuhiro KobayashiInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.
Kenji TamasakuRIKEN SPring-8 Center, RIKEN, Sayo, Hyogo 679-5148, Japan.
Makoto SetoInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.
John D LipscombDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55391, United States.ORCID 0000-0002-8158-5594
Edward I SolomonDepartment of Chemistry, Stanford University, 380 Roth Way, Stanford, California 94305, United States.ORCID 0000-0003-0291-3199
Kyoto University · JPStanford University · USUniversity of Minnesota · USJapan Synchrotron Radiation Research Institute · JPSLAC National Accelerator Laboratory · USSPring-8 · JPTohoku University · JP

Funding

OXYGENASE ENZYME MECHANISMR01GM024689 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI LIPSCOMB, JOHN D · 1985 to 2016
$3.8M
Intermediates in O2 Activation by Oxygenases at Non-heme Iron CentersR35GM118030 · NIGMS · UNIVERSITY OF MINNESOTA · PI LIPSCOMB, JOHN D · 2016 to 2020
$2.7M
Spectroscopic Characterization of Oxygen Intermediates in Non-heme and Heme Iron EnzymesR35GM145202 · NIGMS · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 2022 to 2026
$2.0M
OXYGENASE ENZYME MECHANISMR37GM024689 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI LIPSCOMB, JOHN D · 1994 to 2003
$1.1M
NIGMS NIH HHS R01 GM024689NIGMS NIH HHS R35 GM118030NIGMS NIH HHS R35 GM145202NIGMS NIH HHS R37 GM024689
6 · The paper itself

Abstract

The extradiol dioxygenases (EDOs) and intradiol dioxygenases (IDOs) are nonheme iron enzymes that catalyze the oxidative aromatic ring cleavage of catechol substrates, playing an essential role in the carbon cycle. The EDOs and IDOs utilize very different Fe

Indexed as

DioxygenasesCatecholsFerric CompoundsFerrous CompoundsSpectrum AnalysiscatecholCatecholsDioxygenasesFerric CompoundsFerrous Compounds

Identifiers

PMID37414058
PMCPMC10804917
OpenAlexW4383312814

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.