Evidence map›Paper›PMID 27839951›Full record

ArticleStructure (London, England : 1993)2016

Structure of the NPr:EIN

Madeleine Strickland, Ann Marie Stanley, Guangshun Wang, Istvan Botos, Charles D Schwieters, Susan K Buchanan, Alan Peterkofsky, Nico Tjandra

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 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
1.6field-weighted citation impact, top 16% 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, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Incorporation of residual chemical shift anisotropy into the treatment ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    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

8 authors at 2 institutions in 1 country.

Madeleine StricklandLaboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Ann Marie StanleyLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Guangshun WangDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198, USA.
Istvan BotosLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Charles D SchwietersOffice of Intramural Research, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892, USA.
Susan K BuchananLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Alan PeterkofskyCell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: peterkofsky@nih.gov.
Nico TjandraLaboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: tjandran@nhlbi.nih.gov.
National Institutes of Health · USUniversity of Nebraska Medical Center · US

Funding

Nmr Studies Of The Regulation Of Cell SignalingZIAHL001048 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TJANDRA, NICO · 2009 to 2025
$20.1M
Structural characterization of outer membrane proteins from Yersinia pestisZIADK011011 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.1M
Biomedical ImagingZIACT000090 · CIT · CENTER FOR INFORMATION TECHNOLOGY · PI TRUS, BENES L · 2009 to 2018
$7.8M
NMR STUDIES OF THE REGULATION OF CELL SIGNALINGZ01HL001048 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TJANDRA, NICO · 1998 to 2008
$3.4M
Database designed novel anti-MRSA peptidesR01AI105147 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, GUANGSHUN · 2015 to 2019
$1.9M
Intramural NIH HHS Z01 HL001048
6 · The paper itself

Abstract

Paralogous enzymes arise from gene duplication events that confer a novel function, although it is unclear how cross-reaction between the original and duplicate protein interaction network is minimized. We investigated HPr:EI

Indexed as

Carrier ProteinsCatalytic DomainCrystallography, X-RayEscherichia coli ProteinsModels, MolecularMolecular Docking SimulationMonosaccharidesNitrogenNuclear Magnetic Resonance, BiomolecularPeptide FragmentsPhosphate-Binding ProteinsPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationProtein BindingProtein DomainsStructural Homology, ProteinCarrier ProteinsEIN protein, E coliEscherichia coli ProteinsMonosaccharidesNitrogenNPr protein, E coliPeptide FragmentsPhosphate-Binding ProteinsPhosphoenolpyruvate Sugar Phosphotransferase SystemEnzyme INPrnuclear magnetic resonancephosphotransferase systempseudocontact shiftsresidual dipolar couplingssmall-angle X-ray scatteringspecificitysurface potentialX-ray crystallography

Identifiers

PMID27839951
PMCPMC5143221
OpenAlexW2552109489

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.