Evidence map›Paper›PMID 33034833›Full record

ArticleBiomolecular NMR assignments2021

Mary E Cook, Kristen M Varney, Raquel Godoy-Ruiz, David J Weber

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

Article in Biomolecular NMR assignments, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 91% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 1 institution in 1 country.

Mary E CookDepartment of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT), University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA.
Kristen M VarneyDepartment of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT), University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA.
Raquel Godoy-RuizDepartment of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT), University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA.
David J WeberDepartment of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT), University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA. dweber@som.umaryland.edu.ORCID http://orcid.org/0000-0002-8824-1110
University of Maryland, Baltimore · US

Funding

Structure-based targeting of the C. difficile toxin (CDT) from hypervirulent bacterial strainsR56AI152397 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DES GEORGES, AMEDEE, WEBER, DAVID JOSEPH · 2021 to 2021
$522k
600 MHz NMR Spectrometer ConsoleS10RR023447 · NCRR · UNIVERSITY OF MARYLAND BALTIMORE · PI WEBER, DAVID JOSEPH · 2007 to 2007
$362k
NCRR NIH HHS S10 RR023447NIAID NIH HHS R56 AI152397
6 · The paper itself

Abstract

Clostridioides difficile is a bacterial pathogen responsible for the majority of nosocomial infections in the developed world. C. difficile infection (CDI) is difficult to treat in many cases because hypervirulent strains have evolved that contain a third toxin, termed the C. difficile toxin (CDT), in addition to the two enterotoxins TcdA and TcdB. CDT is a binary toxin comprised of an enzymatic, ADP-ribosyltransferase (ART) toxin component, CDTa, and a pore-forming or delivery subunit, CDTb. In the absence of CDTa, CDTb assembles into two distinct di-heptameric states, a symmetric and an asymmetric form with both states having two surface-accessible host cell receptor-binding domains, termed RBD1 and RBD2. RBD1 has a unique amino acid sequence, when aligned to other well-studied binary toxins (i.e., anthrax), and it contains a novel Ca

Indexed as

Clostridioides difficileNuclear Magnetic Resonance, BiomolecularProtein DomainsADP Ribose TransferasesAmino Acid SequenceBacterial ProteinsNitrogen IsotopesADP Ribose TransferasesBacterial ProteinsNitrogen-15Nitrogen IsotopesBinary toxinCDICDTbClostridioides difficile

Identifiers

PMID33034833
PMCPMC7973916
OpenAlexW3092219280

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.