Evidence map›Paper›PMID 31676138›Full record

ArticleBiophysical journal2019

Assessing Structural Preferences of Unstructured Protein Regions by NMR.

Azzurra Carlon, Lucia Gigli, Enrico Ravera, Giacomo Parigi, Angela M Gronenborn, Claudio Luchinat

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2019. 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
0.2field-weighted citation impact, top 47% 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, 7 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

6 authors at 2 institutions in 2 countries.

Azzurra CarlonMagnetic Resonance Center, University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine, Sesto Fiorentino, Florence, Italy; Department of Chemistry "Ugo Schiff," University of Florence, Sesto Fiorentino, Florence, Italy.
Lucia GigliMagnetic Resonance Center, University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine, Sesto Fiorentino, Florence, Italy; Department of Chemistry "Ugo Schiff," University of Florence, Sesto Fiorentino, Florence, Italy.
Enrico RaveraMagnetic Resonance Center, University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine, Sesto Fiorentino, Florence, Italy; Department of Chemistry "Ugo Schiff," University of Florence, Sesto Fiorentino, Florence, Italy.
Giacomo ParigiMagnetic Resonance Center, University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine, Sesto Fiorentino, Florence, Italy; Department of Chemistry "Ugo Schiff," University of Florence, Sesto Fiorentino, Florence, Italy.
Angela M GronenbornDepartment of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania. Electronic address: amg100@pitt.edu.
Claudio LuchinatMagnetic Resonance Center, University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine, Sesto Fiorentino, Florence, Italy; Department of Chemistry "Ugo Schiff," University of Florence, Sesto Fiorentino, Florence, Italy. Electronic address: luchinat@cerm.unifi.it.
Interuniversity Consortium for Magnetic Resonance · ITUniversity of Pittsburgh · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2019 to 2021
$14.1M
NIAID NIH HHS P50 AI150481NIGMS NIH HHS P50 GM082251
6 · The paper itself

Abstract

Biomacromolecules, such as proteins, often exhibit significant motions intimately associated with their function. Intrinsically disordered proteins and proteins with intrinsically disordered regions, although extremely important for a plethora of cellular functions, are difficult to structurally characterize at the atomic level because the experimental parameters report on ensemble and time averages. Here, we demonstrate for the C-terminal domain of the human immunodeficiency virus type 1 capsid protein that NMR and, in particular, residual dipolar couplings (RDCs) measured for the folded portion of the protein can inform on the structural preferences of the unstructured portion using RDC-prediction tools and the maximum occurrence approach.

Indexed as

Nuclear Magnetic Resonance, BiomolecularIntrinsically Disordered ProteinsModels, MolecularProtein DomainsIntrinsically Disordered Proteins

Identifiers

PMID31676138
PMCPMC7018990
OpenAlexW2981175139

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.