Evidence map›Paper›PMID 31315931›Full record

ArticleThe Journal of biological chemistry2019

The active site of the

Ghader Bashiri, Tyler L Grove, Subray S Hegde, Thomas Lagautriere, Gary J Gerfen, Steven C Almo, Christopher J Squire, John S Blanchard, Edward N Baker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 20 citations in OpenAlex.

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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

9 authors at 2 institutions in 2 countries.

Ghader BashiriMaurice Wilkins Center for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand.
Tyler L GroveDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10805.
Subray S HegdeDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10805.
Thomas LagautriereMaurice Wilkins Center for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand.
Gary J GerfenDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10805.
Steven C AlmoDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10805.
Christopher J SquireMaurice Wilkins Center for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand.
John S BlanchardDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10805.
Edward N BakerMaurice Wilkins Center for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand. Electronic address: ted.baker@auckland.ac.nz.
Albert Einstein College of Medicine · USUniversity of Auckland · NZ

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI CRONAN, JOHN E. · 2010 to 2015
$34.6M
The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SEIDEL, RONALD D · 2010 to 2014
$32.6M
Protein/Structure CoreP01GM118303 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GERLT, JOHN A · 2016 to 2020
$11.4M
Function and Mechanism of Viperin, a radical SAM antiviral proteinR21AI133329 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI ALMO, STEVEN C., GROVE, TYLER L · 2017 to 2018
$459k
NIAID NIH HHS R21 AI133329NIGMS NIH HHS P01 GM118303NIGMS NIH HHS U54 GM093342NIGMS NIH HHS U54 GM094662
6 · The paper itself

Abstract

Iron-sulfur clusters are protein cofactors with an ancient evolutionary origin. These clusters are best known for their roles in redox proteins such as ferredoxins, but some iron-sulfur clusters have nonredox roles in the active sites of enzymes. Such clusters are often prone to oxidative degradation, making the enzymes difficult to characterize. Here we report a structural and functional characterization of dihydroxyacid dehydratase (DHAD) from

Indexed as

Amino Acids, Branched-ChainBinding SitesHydro-LyasesIron-Sulfur ProteinsModels, MolecularMolecular ConformationMycobacterium tuberculosisAmino Acids, Branched-Chaindihydroxyacid dehydrataseHydro-LyasesIron-Sulfur Proteinsbiosynthesiscrystal structuredihydroxyacid dehydrataseiron–sulfur proteinMycobacterium tuberculosisprotein stabilityprotein structure

Identifiers

PMID31315931
PMCPMC6721945
OpenAlexW2956977177

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.