Evidence map›Paper›PMID 35948076›Full record

ArticleMolecular pharmaceutics2022

NMR Reveals Functionally Relevant Thermally Induced Structural Changes within the Native Ensemble of G-CSF.

Mark-Adam W Kellerman, Teresa Almeida, Timothy R Rudd, Paul Matejtschuk, Paul A Dalby

Open access · hybridAbstract read
In one paragraph

Article in Molecular pharmaceutics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

5 authors at 3 institutions in 1 country.

Mark-Adam W KellermanDepartment of Biochemical Engineering, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Teresa AlmeidaMedicines & Healthcare Products Regulatory Agency, National Institute for Biological Standards and Control (NIBSC), Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, United Kingdom.
Timothy R RuddMedicines & Healthcare Products Regulatory Agency, National Institute for Biological Standards and Control (NIBSC), Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, United Kingdom.ORCID 0000-0003-4434-0333
Paul MatejtschukMedicines & Healthcare Products Regulatory Agency, National Institute for Biological Standards and Control (NIBSC), Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, United Kingdom.
Paul A DalbyDepartment of Biochemical Engineering, University College London, Gower Street, London WC1E 6BT, United Kingdom.ORCID 0000-0002-0980-8167
National Institute for Biological Standards and Control · GBUniversity College London · GBUniversity of Liverpool · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structure-function relationships in proteins refer to a trade-off between stability and bioactivity, molded by evolution of the molecule. Identifying which protein amino acid residues jeopardize global or local stability for the benefit of bioactivity would reveal residues pivotal to this structure-function trade-off. Here, we use

Indexed as

Granulocyte Colony-Stimulating FactorProteinsMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein ConformationGranulocyte Colony-Stimulating FactorProteinsaggregationdenaturationremodelingstructure−function“switch”

Identifiers

PMID35948076
PMCPMC9449972
OpenAlexW4292606846

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.