Evidence map›Paper›PMID 32374983›Full record

ArticleBiochemistry2020

Orotidine 5'-Monophosphate Decarboxylase: The Operation of Active Site Chains Within and Across Protein Subunits.

Tiago A S Brandão, John P Richard

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

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 44% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Uridine as a hub in cancer metabolism and RNA biology.Experimental & molecular medicine · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Review
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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

2 authors at 2 institutions in 2 countries.

Tiago A S BrandãoDepartment of Chemistry, ICEx, Federal University of Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, Brazil.ORCID 0000-0002-7783-3014
John P RichardDepartment of Chemistry, University at Buffalo, The State University of New York, Buffalo, New York 14260-3000, United States.ORCID 0000-0002-0440-2387
Universidade Federal de Minas Gerais · BRUniversity at Buffalo, State University of New York · US

Funding

Studies on Enzyme Activation and Novel Modes of Inhibition. Administrative Supplement for EquipmentR35GM134881 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI John P Richard · 2020 to 2026
$2.5M
Activation of Enzymes for Catalysis: The Role of Substrate-Induced Structural ChangesR01GM116921 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI RICHARD, JOHN P · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM116921NIGMS NIH HHS R35 GM134881
6 · The paper itself

Abstract

The D37 and T100' side chains of orotidine 5'-monophosphate decarboxylase (OMPDC) interact with the C-3' and C-2' ribosyl hydroxyl groups, respectively, of the bound substrate. We compare the intra-subunit interactions of D37 with the inter-subunit interactions of T100' by determining the effects of the D37G, D37A, T100'G, and T100'A substitutions on the following: (a)

Indexed as

Binding SitesBiocatalysisModels, MolecularOrotidine-5'-Phosphate DecarboxylaseProtein SubunitsSaccharomyces cerevisiaeUridine MonophosphateOrotidine-5'-Phosphate Decarboxylaseorotidylic acidProtein SubunitsUridine Monophosphate

Identifiers

PMID32374983
PMCPMC7476526
OpenAlexW3021991525

What OpenQuestion holds

Textmetadata
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.