Evidence map›Paper›PMID 26990667›Full record

ArticleChemMedChem2016

Characterization of the Binding of Hydroxyindole, Indoleacetic acid, and Morpholinoaniline to the Salmonella Type III Secretion System Proteins SipD and SipB.

Andrew C McShan, Asokan Anbanandam, Sikta Patnaik, Roberto N De Guzman

Abstract read
In one paragraph

Article in ChemMedChem, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Infection biology ofEcoSal Plus · 2024
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019
    Review
  9. Review
  10. Frontiers in cellular and infection microbiology · 2019
    Review
  11. Article
  12. 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

4 authors at 1 institution in 1 country.

Andrew C McShanDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Ave., Lawrence, KS, 66045, USA.
Asokan AnbanandamBiomolecular NMR Core Facility, University of Kansas, Lawrence, KS, 66045, USA.
Sikta PatnaikDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Ave., Lawrence, KS, 66045, USA.
Roberto N De GuzmanDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Ave., Lawrence, KS, 66045, USA. rdguzman@ku.edu.ORCID 0000-0003-1172-2917
University of Kansas · US

Funding

U of Kansas/Haskell Indian Nations U.IRACDA ProjectK12GM063651 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI DE GUZMAN, ROBERTO N · 2002 to 2022
$10.0M
Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
PHARMACEUTICAL ASPECTS OF BIOTECHNOLOGY TRAININGT32GM008359 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SIAHAAN, TERUNA J., VOLKIN, DAVID · 1989 to 2018
$5.0M
NMR studies of bacterial needle and tip proteinsR01AI074856 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI DE GUZMAN, ROBERTO N · 2008 to 2018
$3.6M
NIAID NIH HHS R01 AI074856NIGMS NIH HHS K12 GM063651NIGMS NIH HHS P30 GM110761NIGMS NIH HHS T32 GM008359
6 · The paper itself

Abstract

Many Gram-negative bacteria require the type III secretion system (T3SS) to cause infectious diseases in humans. A looming public health problem is that all bacterial pathogens that require the T3SS to cause infectious diseases in humans have developed multidrug resistance to current antibiotics. The T3SS is an attractive target for the development of new antibiotics because of its critical role in virulence. An initial step in developing anti-T3SS-based therapeutics is the identification of small molecules that can bind to T3SS proteins. Currently, the only small molecules that are known to bind to the Salmonella T3SS proteins SipD and SipB are bile salts (to SipD) and sphingolipids and cholesterol (to SipB). Herein we report the results of a surface plasmon resonance screen of 288 compounds wherein the binding of 4-morpholinoaniline to SipD, 3-indoleacetic acid to SipB, and 5-hydroxyindole to both SipD and SipB were identified. We also identified by NMR the SipD surfaces involved in binding. These three compounds represent a new class of molecules that can bind to T3SS tip (SipD) and translocon (SipB) proteins that could find use in future drug design.

Indexed as

Aniline CompoundsAntigens, BacterialBacterial ProteinsIndoleacetic AcidsIndolesMembrane ProteinsNuclear Magnetic Resonance, BiomolecularProtein BindingSalmonellaSurface Plasmon ResonanceType III Secretion Systems5-hydroxyindoleanilineAniline CompoundsAntigens, BacterialBacterial Proteinsindoleacetic acidIndoleacetic AcidsIndolesinvasion protein B, Salmonella typhimuriumMembrane ProteinsSspD protein, Salmonella typhimuriumType III Secretion SystemsantibioticsSipBSipDSTD NMRsurface plasmon resonancetranslocontype III secretion system

Identifiers

PMID26990667
PMCPMC5010876
OpenAlexW2297766526

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.