Evidence map›Paper›PMID 23859204›Full record

ArticleFuture medicinal chemistry2013

Understanding HIV-1 protease autoprocessing for novel therapeutic development.

Liangqun Huang, Chaoping Chen

Open access · greenAbstract read
In one paragraph

Article in Future medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Aptamers for Anti-Viral Therapeutics and Diagnostics.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
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  18. 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

2 authors at 1 institution in 1 country.

Liangqun HuangDepartment of Biochemistry & Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
Chaoping Chen
Colorado State University · US

Funding

Isolation and Characterization of Aptamers Targeted to Inhibit HIV Protease MaturR21AI080351 · NIAID · COLORADO STATE UNIVERSITY · PI CHEN, CHAOPING · 2009 to 2010
$400k
NIAID NIH HHS R21 AI080351PHS HHS R21 A1080351
6 · The paper itself

Abstract

In the infected cell, HIV-1 protease (PR) is initially synthesized as part of the GagPol polyprotein. PR autoprocessing is a virus-specific process by which the PR domain embedded in the precursor catalyzes proteolytic reactions responsible for liberation of free mature PRs, which then recognize and cleave at least ten different peptide sequences in the Gag and GagPol polyproteins. Despite extensive structure and function studies of the mature PRs as well as the successful development of ten US FDA-approved catalytic-site inhibitors, the precursor autoprocessing mechanism remains an intriguing yet-to-be-solved puzzle. This article discusses current understanding of the autoprocessing mechanism, in an effort to prompt the development of novel anti-HIV drugs that selectively target precursor autoprocessing.

Indexed as

Amino Acid SequenceCatalytic DomainHIV-1HIV InfectionsHIV ProteaseHIV Protease InhibitorsHumansProtein PrecursorsProtein Processing, Post-TranslationalHIV ProteaseHIV Protease InhibitorsProtein Precursors

Identifiers

PMID23859204
PMCPMC3826259
OpenAlexW2073005383

What OpenQuestion holds

Textmetadata
LicenceTDM
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.