Evidence map›Paper›PMID 28108356›Full record

ReviewBiochimica et biophysica acta. Molecular and cell biology of lipids2017

Lipid A structural modifications in extreme conditions and identification of unique modifying enzymes to define the Toll-like receptor 4 structure-activity relationship.

Alison J Scott, Benjamin L Oyler, David R Goodlett, Robert K Ernst

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

47 citing papers in PubMed, 66 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

4 authors at 2 institutions in 1 country.

Alison J ScottDepartment of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, MD 21201, United States.
Benjamin L OylerInstitute of Marine & Environmental Technology, University of Maryland Center for Environmental Science, Baltimore, MD 21202, United States.
David R GoodlettDepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD 21201, United States.
Robert K ErnstDepartment of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, MD 21201, United States. Electronic address: rkernst@umaryland.edu.
University of Maryland, Baltimore · USUniversity of Maryland Center for Environmental Science · US

Funding

IMMUNITY AND INFECTIONT32AI007540 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI KAPER, JAMES B · 1998 to 2018
$2.2M
Protection Against Gram-Negative Sepsis Conferred by Lipid A-Based Structural VariantsR01AI123820 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI ERNST, ROBERT K, GOODLETT, DAVID ROBINSON · 2016 to 2019
$1.5M
MS diagnostic bacterial identification libraryR01GM111066 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI ERNST, ROBERT K, GOODLETT, DAVID ROBINSON · 2014 to 2017
$1.2M
Immunotherapeutic Potential of Modified Lipooligosaccharides and Lipid A'sR21AI101685 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI ERNST, ROBERT K · 2013 to 2014
$411k
NIAID NIH HHS R01 AI123820NIAID NIH HHS R21 AI101685NIAID NIH HHS T32 AI007540NIGMS NIH HHS R01 GM111066
6 · The paper itself

Abstract

Strategies utilizing Toll-like receptor 4 (TLR4) agonists for treatment of cancer, infectious diseases, and other targets report promising results. Potent TLR4 antagonists are also gaining attention as therapeutic leads. Though some principles for TLR4 modulation by lipid A have been described, a thorough understanding of the structure-activity relationship (SAR) is lacking. Only through a complete definition of lipid A-TLR4 SAR is it possible to predict TLR4 signaling effects of discrete lipid A structures, rendering them more pharmacologically relevant. A limited 'toolbox' of lipid A-modifying enzymes has been defined and is largely composed of enzymes from mesophile human and zoonotic pathogens. Expansion of this 'toolbox' will result from extending the search into lipid A biosynthesis and modification by bacteria living at the extremes. Here, we review the fundamentals of lipid A structure, advances in lipid A uses in TLR4 modulation, and the search for novel lipid A-modifying systems in extremophile bacteria. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.

Indexed as

Drug DesignAnimalsBacteriaBacterial ProteinsEnzymesHumansLipid ALipogenesisProtein ConformationSignal TransductionStructure-Activity RelationshipToll-Like Receptor 4Bacterial ProteinsEnzymesLipid AToll-Like Receptor 4Lipid A modifying enzymesLipid A structureMarine bacteriaTLR4 agonistsTLR4 antagonistsTLR4 immunomodulation

Identifiers

PMID28108356
PMCPMC5513793
OpenAlexW2576519196

What OpenQuestion 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 OpenQuestion graph.