Evidence map›Paper›PMID 26086954›Full record

ArticleThe journal of physical chemistry. B2015

Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy.

Eduardo F Vicente, Indra D Sahu, Antonio J Costa-Filho, Eduardo M Cilli, Gary A Lorigan

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2015. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. Pinholin SBiochimica et biophysica acta. Biomembranes · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Biophysical EPR Studies Applied to Membrane Proteins.Journal of physical chemistry & biophysics
    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

5 authors.

Eduardo F Vicente†UNESP - Univ Estadual Paulista, Campus de Tupã, 17602-496, Tupã, SP Brazil.
Indra D Sahu‡Department of Chemistry and Biochemistry, Miami University, 45056, Oxford, Ohio United States.
Antonio J Costa-Filho§Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo - USP,14040-901, Ribeirão Preto, SP Brazil.
Eduardo M Cilli∥Departamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista, 14800-900, Araraquara, SP Brazil.
Gary A Lorigan‡Department of Chemistry and Biochemistry, Miami University, 45056, Oxford, Ohio United States.

Funding

EPR Structural Studies of KCNE1/KCNQ1R01GM108026 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM108026
6 · The paper itself

Abstract

The human enzyme dihydroorotate dehydrogenase (HsDHODH) has been studied for being a target for development of new antineoplasic and antiproliferative drugs. The synthetic peptide N-t(DH) represents the N-terminal microdomain of this enzyme, responsible for anchoring it to the inner mitochondrial membrane. Also, it is known to harbor quinones that are essential for enzyme catalysis. Here we report structural features of the peptide/membrane interactions obtained by using CD and DEER spectroscopic techniques, both in micelles and in lipid vesicles. The data revealed different peptide conformational states in micelles and liposomes, which could suggest that this microdomain acts in specific regions or areas of the mitochondria, which can be related with the control of the quinone access to the HsDHODH active site. This is the first study to report on conformational changes of the HsDHODH N-terminal microdomain through a combination of CD and DEER spectroscopic techniques.

Indexed as

Amino Acid SequenceCatalytic DomainCircular DichroismDihydroorotate DehydrogenaseHumansMolecular Sequence DataOxidoreductases Acting on CH-CH Group DonorsProtein ConformationSpectrum AnalysisDihydroorotate DehydrogenaseOxidoreductases Acting on CH-CH Group Donors

Identifiers

PMID26086954
PMCPMC4814773

What OpenQuestion holds

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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.