Evidence map›Paper›PMID 34639146›Full record

ArticleInternational journal of molecular sciences2021

Residual Helicity at the Active Site of the Histidine Phosphocarrier, HPr, Modulates Binding Affinity to Its Natural Partners.

José L Neira, David Ortega-Alarcón, Bruno Rizzuti, Martina Palomino-Schätzlein, Adrián Velázquez-Campoy, Alberto Falcó

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 29% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
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

6 authors at 3 institutions in 2 countries.

José L NeiraIDIBE, Universidad Miguel Hernández, 03202 Elche, Spain.ORCID 0000-0002-4933-0428
David Ortega-AlarcónJoint Units IQFR-CSIC-BIFI, and GBsC-CSIC-BIFI, Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Universidad de Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0003-1885-4365
Bruno RizzutiJoint Units IQFR-CSIC-BIFI, and GBsC-CSIC-BIFI, Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Universidad de Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0003-1110-764X
Martina Palomino-SchätzleinCentro de Investigación Príncipe Felipe, Calle Eduardo Primo Yufera 3, 46022 Valencia, Spain.ORCID 0000-0001-7303-0743
Adrián Velázquez-CampoyJoint Units IQFR-CSIC-BIFI, and GBsC-CSIC-BIFI, Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Universidad de Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0001-5702-4538
Alberto FalcóIDIBE, Universidad Miguel Hernández, 03202 Elche, Spain.ORCID 0000-0001-7726-6577
Universidad de Zaragoza · ESUniversitat de Miguel Hernández d'Elx · ESCentro de Investigacion Principe Felipe · ES

Funding

Ministry of Economy, Industry and Competitiveness BES-2017-080739Ministry of Economy, Industry and Competitiveness BFU2016-78232-PMinistry of Economy, Industry and Competitiveness RTI2018-097991-B-I00Ministry of Economy, Industry and Competitiveness RTI2018-101969-J-I00
6 · The paper itself

Abstract

The phosphoenolpyruvate-dependent phosphotransferase system (PTS) modulates the preferential use of sugars in bacteria. The first proteins in the cascade are common to all organisms (EI and HPr). The active site of HPr involves a histidine (His15) located immediately before the beginning of the first α-helix. The regulator of sigma D (Rsd) protein also binds to HPr. The region of HPr comprising residues Gly9-Ala30 (HPr

Indexed as

MutationAnti-Bacterial AgentsBacterial ProteinsBinding SitesCatalytic DomainHistidinePeptide FragmentsPhosphoenolpyruvate Sugar Phosphotransferase SystemStaphylococcus aureusAnti-Bacterial AgentsBacterial ProteinsHistidinePeptide Fragmentsphosphocarrier protein HPrPhosphoenolpyruvate Sugar Phosphotransferase Systembindingcircular dichroismfluorescenceisothermal titration calorimetryNMRpeptides

Identifiers

PMID34639146
PMCPMC8509676
OpenAlexW3202567961

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.