Evidence map›Paper›PMID 24055245›Full record

ReviewTrends in biochemical sciences2013

Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.

G Marius Clore, Vincenzo Venditti

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 69 citations in OpenAlex.

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  10. Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020
    Review
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  18. Gut Microbiota Modulates Interactions Between Polychlorinated Biphenyls and Bile Acid Homeostasis.Toxicological sciences : an official journal of the Society of Toxicology · 2018
    Article
  19. Article
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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

2 authors at 2 institutions in 1 country.

G Marius CloreLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. Electronic address: mariusc@mail.nih.gov.
Vincenzo Venditti
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Structure and Dynamics Of Macromolecules In Solution By NMRZIADK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, GIDEON · 2009 to 2025
$41.5M
NMR STUDIES OF THREE-DIMENSIONAL STRUCTURE OF MACROMOLECULES IN SOLUTIONZ01DK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, G. MARIUS · 1988 to 2008
$949k
Intramural NIH HHS Z01 DK029023
6 · The paper itself

Abstract

The bacterial phosphotransferase system (PTS) couples phosphoryl transfer, via a series of bimolecular protein-protein interactions, to sugar transport across the membrane. The multitude of complexes in the PTS provides a paradigm for studying protein interactions, and for understanding how the same binding surface can specifically recognize a diverse array of targets. Fifteen years of work aimed at solving the solution structures of all soluble protein-protein complexes of the PTS has served as a test bed for developing NMR and integrated hybrid approaches to study larger complexes in solution and to probe transient, spectroscopically invisible states, including encounter complexes. We review these approaches, highlighting the problems that can be tackled with these methods, and summarize the current findings on protein interactions.

Indexed as

BacteriaCytoplasmModels, MolecularPhosphoenolpyruvate Sugar Phosphotransferase SystemProtein BindingProtein ConformationPhosphoenolpyruvate Sugar Phosphotransferase Systembacterial phosphotransferase systemencounter complexeshybrid methods in structure determinationNMR spectroscopyprotein–protein recognitionresidual dipolar couplingssignal transductionsolution X-ray scatteringsparsely populated states

Identifiers

PMID24055245
PMCPMC3831880
OpenAlexW2015901189

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.