Evidence map›Paper›PMID 33606110›Full record

ReviewArchives of virology2021

On the irrationality of rational design of an HIV vaccine in light of protein intrinsic disorder.

Vladimir N Uversky

Abstract readReview
In one paragraph

Review in Archives of virology, 2021. 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
–field-weighted citation impact
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.

  1. 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

1 author.

Vladimir N UverskyDepartment of Molecular Medicine, USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA. vuversky@usf.edu.ORCID http://orcid.org/0000-0002-4037-5857

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lack of progress in finding an efficient vaccine for a human immunodeficiency virus (HIV) is daunting. In fact, this search has spanned nearly four decades without much success. There are several objective reasons for such a failure, which include the highly glycosylated nature of HIV-1, the presence of neotopes, and high mutation rates. This article argues that the presence of highly flexible and intrinsically disordered regions in both human anti-HIV-1 antibodies and the major HIV-1immunogen, its surface glycoprotein gp120, represent one of the major causes for the lack of success in utilization of structure-based reverse vaccinology.

Indexed as

AIDS VaccinesAntibodies, NeutralizingAntigen-Antibody ComplexHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHumansImmunoglobulin GIntrinsically Disordered ProteinsAIDS VaccinesAntibodies, NeutralizingAntigen-Antibody ComplexHIV AntibodiesHIV Envelope Protein gp120Immunoglobulin GIntrinsically Disordered Proteins

Identifiers

PMID33606110
PMCPMC7892713

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.