Evidence map›Paper›PMID 26709853›Full record

ArticleThe journal of physical chemistry. B2016

Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies.

Rupal Gupta, Manman Lu, Guangjin Hou, Marc A Caporini, Melanie Rosay, Werner Maas, Jochem Struppe, Christopher Suiter, Jinwoo Ahn, In-Ja L Byeon and 8 more

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Characterization of dielectric properties and their impact on MAS-DNP NMR applications.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells.Journal of the American Chemical Society · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. High-sensitivity protein solid-state NMR spectroscopy.Current opinion in structural biology · 2019
    Review
  18. Article
  19. Article
  20. Journal of the American Chemical Society · 2019
    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

18 authors at 7 institutions in 3 countries.

Rupal GuptaDepartment of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
Manman LuDepartment of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
Guangjin HouDepartment of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
Marc A CaporiniBruker Biospin Corporation , 15 Fortune Drive, Billerica, Massachusetts United States.
Melanie RosayBruker Biospin Corporation , 15 Fortune Drive, Billerica, Massachusetts United States.
Werner MaasBruker Biospin Corporation , 15 Fortune Drive, Billerica, Massachusetts United States.
Jochem StruppeBruker Biospin Corporation , 15 Fortune Drive, Billerica, Massachusetts United States.
Christopher SuiterDepartment of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
Jinwoo Ahn
In-Ja L Byeon
W Trent FranksLeibniz-Institut für Molekulare Pharmakologie , Robert-Roessle-Straße 10, 13125 Berlin, Germany.
Marcella Orwick-RydmarkLeibniz-Institut für Molekulare Pharmakologie , Robert-Roessle-Straße 10, 13125 Berlin, Germany.
Andrea BertarelloCentre de RMN à Très Hauts Champs, Institut des Sciences Analytiques, UMR 5280 CNRS/Ecole Normale Supérieure de Lyon , 5 rue de la Doua, 69100 Villeurbanne (Lyon), France.
Hartmut OschkinatLeibniz-Institut für Molekulare Pharmakologie , Robert-Roessle-Straße 10, 13125 Berlin, Germany.
Anne LesageCentre de RMN à Très Hauts Champs, Institut des Sciences Analytiques, UMR 5280 CNRS/Ecole Normale Supérieure de Lyon , 5 rue de la Doua, 69100 Villeurbanne (Lyon), France.
Guido PintacudaCentre de RMN à Très Hauts Champs, Institut des Sciences Analytiques, UMR 5280 CNRS/Ecole Normale Supérieure de Lyon , 5 rue de la Doua, 69100 Villeurbanne (Lyon), France.
Angela M Gronenborn
Tatyana PolenovaDepartment of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
University of Pittsburgh · USBruker (United States) · USLeibniz-Forschungsinstitut für Molekulare Pharmakologie · DEUniversity of Delaware · USCentre National de la Recherche Scientifique · FRÉcole Normale Supérieure de Lyon · FRInstitut des Sciences Analytiques · FR

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI PATEL, SANDEEP · 2014 to 2018
$5.8M
NIGMS NIH HHS P30 GM110758NIGMS NIH HHS P50 GM082251NIGMS NIH HHS P50GM082251
6 · The paper itself

Abstract

Mature infectious HIV-1 virions contain conical capsids composed of CA protein, generated by the proteolytic cleavage cascade of the Gag polyprotein, termed maturation. The mechanism of capsid core formation through the maturation process remains poorly understood. We present DNP-enhanced MAS NMR studies of tubular assemblies of CA and Gag CA-SP1 maturation intermediate and report 20-64-fold sensitivity enhancements due to DNP at 14.1 T. These sensitivity enhancements enabled direct observation of spacer peptide 1 (SP1) resonances in CA-SP1 by dipolar-based correlation experiments, unequivocally indicating that the SP1 peptide is unstructured in assembled CA-SP1 at cryogenic temperatures, corroborating our earlier results. Furthermore, the dependence of DNP enhancements and spectral resolution on magnetic field strength (9.4-18.8 T) and temperature (109-180 K) was investigated. Our results suggest that DNP-based measurements could potentially provide residue-specific dynamics information by allowing for the extraction of the temperature dependence of the anisotropic tensorial or relaxation parameters. With DNP, we were able to detect multiple well-resolved isoleucine side-chain conformers; unique intermolecular correlations across two CA molecules; and functionally relevant conformationally disordered states such as the 14-residue SP1 peptide, none of which are visible at ambient temperatures. The detection of isolated conformers and intermolecular correlations can provide crucial constraints for structure determination of these assemblies. Overall, our results establish DNP-based MAS NMR spectroscopy as an excellent tool for the characterization of HIV-1 assemblies.

Indexed as

CapsidHIV-1Magnetic Resonance SpectroscopyProtein ConformationViral ProteinsViral Proteins

Identifiers

PMID26709853
PMCPMC4890707
OpenAlexW2339923719

What OpenQuestion holds

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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.