Evidence map›Paper›PMID 28615448›Full record

ArticleThe Journal of biological chemistry2017

Structural and biochemical analyses reveal insights into covalent flavinylation of the

C A Starbird, Elena Maklashina, Pankaj Sharma, Susan Qualls-Histed, Gary Cecchini, T M Iverson

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Maturation of the respiratory complex II flavoprotein.Current opinion in structural biology · 2019
    Review
  5. The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.Cellular and molecular life sciences : CMLS · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. 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

6 authors at 2 institutions in 1 country.

C A StarbirdGraduate Program in Chemical and Physical Biology, Vanderbilt University, Nashville, Tennessee 37232.
Elena MaklashinaMolecular Biology Division, Veterans Affairs Medical Center, San Francisco, California 94121; Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158.
Pankaj SharmaDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232.
Susan Qualls-HistedDepartments of Cell and Developmental Biology, Vanderbilt University, Nashville, Tennessee 37232.
Gary CecchiniMolecular Biology Division, Veterans Affairs Medical Center, San Francisco, California 94121; Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158. Electronic address: Gary.Cecchini@ucsf.edu.
T M IversonDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232; Department of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232; Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, Tennessee 37232. Electronic address: tina.iverson@vanderbilt.edu.
Vanderbilt University · USSan Francisco VA Medical Center · US

Funding

Vanderbilt/Meharry Initiative for Minority Student DvptR25GM062459 · NIGMS · VANDERBILT UNIVERSITY · PI VELEZ EDWARDS, DIGNA R · 2002 to 2020
$10.4M
Structure/Function of Complex ll OxidoreductasesR01GM061606 · NIGMS · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI CECCHINI, GARY, IVERSON, T M · 2001 to 2022
$9.1M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
A Pixel Array Detector System for Small Angle X-ray ScatteringS10OD018483 · OD · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CLASSEN, SCOTT · 2014 to 2014
$998k
Crystallographic AutomationS10RR026915 · NCRR · VANDERBILT UNIVERSITY · PI IVERSON, T M · 2010 to 2010
$490k
THE ROLE OF ACETYLATION IN MITOCHONDRIAL FUNCTIONI01BX001077 · VA · VETERANS AFFAIRS MED CTR SAN FRANCISCO · PI CECCHINI, GARY · 2011 to 2014
–
BLRD VA I01 BX001077NCRR NIH HHS S10 RR026915NIGMS NIH HHS R01 GM061606NIGMS NIH HHS R01 GM105404NIGMS NIH HHS R25 GM062459NIGMS NIH HHS T32 GM008320NIH HHS S10 OD018483
6 · The paper itself

Abstract

The

Indexed as

Models, MolecularProtein Processing, Post-TranslationalAmino Acid SubstitutionBiocatalysisCrystallography, X-RayEnzyme StabilityEscherichia coliEscherichia coli ProteinsFlavin-Adenine DinucleotideGene DeletionGlutamic AcidHot TemperatureMolecular Docking SimulationMutagenesis, Site-DirectedMutationOxidoreductasesEscherichia coli ProteinsFlavin-Adenine DinucleotideFrdA protein, E coliGlutamic AcidOxidoreductasesProtein SubunitsRecombinant ProteinsSuccinate DehydrogenasebioenergeticsComplex IIflavin adenine dinucleotide (FAD)membrane enzymeoxidation-reduction (redox)protein assemblyprotein structurerespiratory chain

Identifiers

PMID28615448
PMCPMC5546032
OpenAlexW2626200269

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.