Evidence map›Paper›PMID 28866776›Full record

ArticleBiomolecular NMR assignments2017

Zhalgas Serimbetov, Nicola J Baxter, Matthew J Cliff, Jonathan P Waltho

Open access · hybridAbstract read
In one paragraph

Article in Biomolecular NMR assignments, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 54% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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 2 institutions in 1 country.

Zhalgas SerimbetovManchester Institute of Biotechnology and School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Nicola J BaxterManchester Institute of Biotechnology and School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. n.j.baxter@sheffield.ac.uk.
Matthew J CliffManchester Institute of Biotechnology and School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. matthew.cliff@manchester.ac.uk.
Jonathan P WalthoManchester Institute of Biotechnology and School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. j.waltho@manchester.ac.uk.
University of Manchester · GBUniversity of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council (GB) BB/M021637/1European Commission Marie Curie Fellowship PITN-GA-2013-ITN 606831
6 · The paper itself

Abstract

Human phosphoglycerate kinase (PGK) is an energy generating glycolytic enzyme that catalyses the transfer of a phosphoryl group from 1,3-bisphosphoglycerate (BPG) to ADP producing 3-phosphoglycerate (3PG) and ATP. PGK is composed of two α/β Rossmann-fold domains linked by a central α-helix and the active site is located in the cleft formed between the N-domain which binds BPG or 3PG, and the C-domain which binds the nucleotides ADP or ATP. Domain closure is required to bring the two substrates into close proximity for phosphoryl transfer to occur, however previous structural studies involving a range of native substrates and substrate analogues only yielded open or partly closed PGK complexes. X-ray crystallography using magnesium trifluoride (MgF

Indexed as

Nuclear Magnetic Resonance, BiomolecularAdenosine DiphosphateFluoridesGlyceraldehyde 3-PhosphateHumansMagnesium CompoundsModels, MolecularPhosphoglycerate KinaseProtein BindingProtein Conformation, alpha-HelicalAdenosine DiphosphateFluoridesGlyceraldehyde 3-PhosphateMagnesium Compoundsmagnesium fluoridePhosphoglycerate KinaseBackbone resonance assignmentMagnesium trifluoridePhosphoryl transfer enzymeTransition state analogueTransverse relaxation optimised spectroscopy

Identifiers

PMID28866776
PMCPMC5594045
OpenAlexW2752230173

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.