Evidence map›Paper›PMID 30093409›Full record

ArticleThe Journal of biological chemistry2018

Bacterially expressed HIV-1 gp120 outer-domain fragment immunogens with improved stability and affinity for CD4-binding site neutralizing antibodies.

Ujjwal Rathore, Mansi Purwar, Venkada Subramanian Vignesh, Raksha Das, Aditya Arun Kumar, Sanchari Bhattacharyya, Heather Arendt, Joanne DeStefano, Aaron Wilson, Christopher Parks and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. A facile method of mapping HIV-1 neutralizing epitopes using chemically masked cysteines and deep sequencing.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. 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

13 authors at 4 institutions in 2 countries.

Ujjwal RathoreFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012.
Mansi PurwarFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012.
Venkada Subramanian VigneshFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012.
Raksha DasFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012.
Aditya Arun KumarFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012.
Sanchari BhattacharyyaFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012.
Heather Arendtthe International AIDS Vaccine Initiative, Brooklyn, New York 11226, and.
Joanne DeStefanothe International AIDS Vaccine Initiative, Brooklyn, New York 11226, and.
Aaron Wilsonthe International AIDS Vaccine Initiative, Brooklyn, New York 11226, and.
Christopher Parksthe International AIDS Vaccine Initiative, Brooklyn, New York 11226, and.
Celia C La Branchethe Department of Surgery, Duke University Medical Center, Durham, North Carolina 27707.
David C Montefiorithe Department of Surgery, Duke University Medical Center, Durham, North Carolina 27707.
Raghavan VaradarajanFrom the Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012, varadar@mbu.iisc.ernet.in.
Indian Institute of Science Bangalore · INInternational AIDS Vaccine Initiative · USDuke Medical Center · USDuke University Hospital · US

Funding

HIV-1 envelope structure, stability and dynamics probed by saturation mutagenesisR01AI118366 · NIAID · INDIAN INSTITUTE OF SCIENCE · PI VARADARAJAN, RAGHAVAN · 2015 to 2019
$607k
NIAID NIH HHS R01 AI118366NIDA NIH HHS HHSN271201100016C
6 · The paper itself

Abstract

Protein minimization is an attractive approach for designing vaccines against rapidly evolving pathogens such as human immunodeficiency virus, type 1 (HIV-1), because it can help in focusing the immune response toward conserved conformational epitopes present on complex targets. The outer domain (OD) of HIV-1 gp120 contains epitopes for a large number of neutralizing antibodies and therefore is a primary target for structure-based vaccine design. We have previously designed a bacterially expressed outer-domain immunogen (OD

Indexed as

AIDS VaccinesAnimalsAntibodies, MonoclonalAntibodies, NeutralizingBinding SitesBroadly Neutralizing AntibodiesCD4 AntigensCrystallography, X-RayEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHumansLigandsProtein BindingAIDS VaccinesAntibodies, MonoclonalAntibodies, NeutralizingBroadly Neutralizing AntibodiesCD4 AntigensEpitopesgp120 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120LigandsVRC01 monoclonal antibodyglycosylationhydrogen–deuterium exchangemutagenesisprotein designprotein refoldingvaccine developmentyeast surface display

Identifiers

PMID30093409
PMCPMC6166733
OpenAlexW2887174992

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.