Evidence map›Paper›PMID 27844185›Full record

ArticleJournal of biomolecular NMR2016

A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.

Eva Rozentur-Shkop, Gil Goobes, Jordan H Chill

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2016. 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
0.3field-weighted citation impact, top 30% 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, 5 citations in OpenAlex.

  1. Review
  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

3 authors at 1 institution in 1 country.

Eva Rozentur-ShkopDepartment of Chemistry, Bar Ilan University, 52900, Ramat Gan, Israel.
Gil GoobesDepartment of Chemistry, Bar Ilan University, 52900, Ramat Gan, Israel.
Jordan H ChillDepartment of Chemistry, Bar Ilan University, 52900, Ramat Gan, Israel. Jordan.Chill@biu.ac.il.ORCID 0000-0002-9518-824X
Bar-Ilan University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are multi-conformational polypeptides that lack a single stable three-dimensional structure. It has become increasingly clear that the versatile IDPs play key roles in a multitude of biological processes, and, given their flexible nature, NMR is a leading method to investigate IDP behavior on the molecular level. Here we present an IDP-tailored J-modulated experiment designed to monitor changes in the conformational ensemble characteristic of IDPs by accurately measuring backbone one- and two-bond J(

Indexed as

Magnetic Resonance SpectroscopyModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationActinsAmino Acid SequenceCytoskeletal ProteinsHumansIntracellular Signaling Peptides and ProteinsIntrinsically Disordered ProteinsIsotope LabelingProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsUbiquitinActinsCytoskeletal ProteinsIntracellular Signaling Peptides and ProteinsIntrinsically Disordered ProteinsRecombinant ProteinsUbiquitinWIPF1 protein, human13C′-detected experimentsActin-binding moduleCrowding effectsIntrinsically disordered proteinsJ-modulated experimentsWASP-interacting protein

Identifiers

PMID27844185
OpenAlexW2552931388

What OpenQuestion holds

Textmetadata
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.