Evidence map›Paper›PMID 33829766›Full record

ArticleBiochemistry2021

Caught in Action: X-ray Structure of Thymidylate Synthase with Noncovalent Intermediate Analog.

Svetlana A Kholodar, Janet S Finer-Moore, Katarzyna Świderek, Kemel Arafet, Vicent Moliner, Robert M Stroud, Amnon Kohen

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 58% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

7 authors at 3 institutions in 2 countries.

Svetlana A KholodarDepartment of Chemistry, The University of Iowa, Iowa City, Iowa 52242, United States.ORCID 0000-0002-4100-1814
Janet S Finer-MooreDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California 94158, United States.ORCID 0000-0001-8172-0998
Katarzyna ŚwiderekDepartament de Química Física i Analítica, Universitat Jaume I, 12071 Castelló, Spain.
Kemel ArafetDepartament de Química Física i Analítica, Universitat Jaume I, 12071 Castelló, Spain.
Vicent MolinerDepartament de Química Física i Analítica, Universitat Jaume I, 12071 Castelló, Spain.ORCID 0000-0002-3665-3391
Robert M StroudDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California 94158, United States.
Amnon KohenDepartment of Chemistry, The University of Iowa, Iowa City, Iowa 52242, United States.ORCID 0000-0001-8793-8939
Universitat Jaume I · ESUniversity of California, San Francisco · USUniversity of Iowa · US

Funding

STRUCTURE/FUNCTION OF PROTEINS AT MOLECULAR LEVELR01GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2024
$7.5M
Tunneling and dynamic studies with DHFRR01GM065368 · NIGMS · UNIVERSITY OF IOWA · PI CHEATUM, CHRISTOPHER M · 2002 to 2017
$3.5M
NIGMS NIH HHS R01 GM024485NIGMS NIH HHS R01 GM065368
6 · The paper itself

Abstract

Methylation of 2-deoxyuridine-5'-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole

Indexed as

Thymidylate SynthaseCatalytic DomainCrystallography, X-RayDeoxyuracil NucleotidesModels, MolecularMolecular Dynamics SimulationProtein ConformationTetrahydrofolatesThymidine Monophosphate2'-deoxyuridylic acid5,10-methylenetetrahydrofolic acidDeoxyuracil NucleotidesTetrahydrofolatesThymidine MonophosphateThymidylate Synthase

Identifiers

PMID33829766
PMCPMC10627423
OpenAlexW3145792952

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.