Evidence map›Paper›PMID 34605436›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis.

Sarah K Alvarado, Mitchell D Miller, Minakshi Bhardwaj, Jon S Thorson, Steven G Van Lanen, George N Phillips

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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.

Sarah K AlvaradoDepartment of BioSciences, Rice University, 6100 Main Street, Houston, TX 77005, USA.ORCID 0000-0002-5653-1578
Mitchell D MillerDepartment of BioSciences, Rice University, 6100 Main Street, Houston, TX 77005, USA.ORCID 0000-0003-1626-4943
Minakshi BhardwajDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, USA.ORCID 0000-0001-6544-7370
Jon S ThorsonDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, USA.ORCID 0000-0002-7148-0721
Steven G Van LanenDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, USA.ORCID 0000-0003-1539-2732
George N PhillipsDepartment of BioSciences, Rice University, 6100 Main Street, Houston, TX 77005, USA.ORCID 0000-0002-4171-4603
Rice University · USUniversity of Kentucky · US

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR001998 · NCATS · UNIVERSITY OF KENTUCKY · PI HARTMANN, KATHERINE E, KERN, PHILIP A · 2016 to 2025
$34.2M
Understanding the role of anti-apolipoprotein A-I antibodies in atherosclerotic cardiovascular diseaseP20GM130456 · NIGMS · UNIVERSITY OF KENTUCKY · PI Jon Scott Thorson · 2020 to 2026
$18.7M
Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
Studies to understand and exploit 10-membered enediyne biosynthesisR01CA217255 · NCI · UNIVERSITY OF KENTUCKY · PI PHILLIPS, GEORGE NEAL, THORSON, JON SCOTT · 2017 to 2021
$2.6M
Platform technologies for understanding and exploiting methylationR01GM115261 · NIGMS · UNIVERSITY OF KENTUCKY · PI PHILLIPS, GEORGE NEAL, THORSON, JON SCOTT · 2016 to 2019
$2.2M
NCATS NIH HHS UL1 TR000117NCATS NIH HHS UL1 TR001998NCI NIH HHS R01 CA217255NIGMS NIH HHS P20 GM130456NIGMS NIH HHS R01 GM115261NIGMS NIH HHS T32 GM008280
6 · The paper itself

Abstract

The 1.5 Å resolution crystal structure of DynU16, a protein identified in the dynemicin-biosynthetic gene cluster, is reported. The structure adopts a di-domain helix-grip fold with a uniquely positioned open cavity connecting the domains. The elongated dimensions of the cavity appear to be compatible with the geometry of a linear polyene, suggesting the involvement of DynU16 in the upstream steps of dynemicin biosynthesis.

Indexed as

Amino Acid SequenceAnthraquinonesAnti-Bacterial AgentsCrystallography, X-RayEnediynesEscherichia coliEscherichia coli ProteinsModels, MolecularMultigene FamilyProtein ConformationAnthraquinonesAnti-Bacterial Agentsdynemicin AEnediynesEscherichia coli ProteinsdynemicinDynU16helix-grip foldSTART/Bet v1 domain

Identifiers

PMID34605436
PMCPMC8488855
OpenAlexW3199583495

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.