Evidence map›Paper›PMID 32188158›Full record

ArticleInternational journal of molecular sciences2020

NMR Structure of the FIV gp36 C-Terminal Heptad Repeat and Membrane-Proximal External Region.

Manuela Grimaldi, Michela Buonocore, Mario Scrima, Ilaria Stillitano, Gerardino D'Errico, Angelo Santoro, Giuseppina Amodio, Daniela Eletto, Antonio Gloria, Teresa Russo and 5 more

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

Article in International journal of molecular sciences, 2020. 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 55% 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

15 authors at 4 institutions in 2 countries.

Manuela GrimaldiDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Michela BuonocoreDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Mario ScrimaDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Ilaria StillitanoDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Gerardino D'ErricoDepartment of Chemical Sciences, University of Naples Federico II, Monte S. Angelo, Via Cinthia, 80126 Naples, Italy.
Angelo SantoroDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Giuseppina AmodioDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Via S. Allende, 84081 Baronissi (SA), Italy.
Daniela ElettoDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Antonio GloriaInstitute of Polymers, Composites and Biomaterials, National Research Council of Italy, V.le J.F. Kennedy 54-Pad. 20 Mostra d'Oltremare, 80125 Naples, Italy.
Teresa RussoInstitute of Polymers, Composites and Biomaterials, National Research Council of Italy, V.le J.F. Kennedy 54-Pad. 20 Mostra d'Oltremare, 80125 Naples, Italy.
Ornella MoltedoDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Paolo RemondelliDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Via S. Allende, 84081 Baronissi (SA), Italy.
Alessandra ToscoDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
Hans L J WienkDepartment of Chemistry, NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Uthrecht, The Netherlands.
Anna Maria D'UrsiDepartment of Pharmacy, University of Salerno, Via Giovanni Paolo II, 134, I-84084 Fisciano, Italy.
University of Salerno · ITNational Research Council · ITUniversity of Naples Federico II · ITUtrecht University · NL

Funding

Seventh Framework Programme 261863
6 · The paper itself

Abstract

Feline immunodeficiency virus (FIV), a lentivirus causing an immunodeficiency syndrome in cats, represents a relevant model of pre-screening therapies for human immunodeficiency virus (HIV). The envelope glycoproteins gp36 in FIV and gp41 in HIV mediate the fusion of the virus with the host cell membrane. They have a common structural framework in the C-terminal region that includes a Trp-rich membrane-proximal external region (MPER) and a C-terminal heptad repeat (CHR). MPER is essential for the correct positioning of gp36 on the lipid membrane, whereas CHR is essential for the stabilization of the low-energy six-helical bundle (6HB) that is necessary for the fusion of the virus envelope with the cell membrane. Conformational data for gp36 are missing, and several aspects of the MPER structure of different lentiviruses are still debated. In the present work, we report the structural investigation of a gp36 construct that includes the MPER and part of the CHR domain (

Indexed as

Amino Acid SequenceElectron Spin Resonance SpectroscopyHIV-1Immunodeficiency Virus, FelineMagnetic Resonance ImagingMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularPhosphorylcholineProtein ConformationViral Envelope ProteinsVirus InternalizationdodecylphosphocholinePhosphorylcholineViral Envelope Proteinsenvelope glicoproteinsFIVHIVMPERNMR

Identifiers

PMID32188158
PMCPMC7139756
OpenAlexW3011942751

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.