Evidence map›Paper›PMID 19025416›Full record

ArticleAIDS research and human retroviruses2008

Design and characterization of an HIV-specific ribonuclease zymogen.

Rebecca F Turcotte, Ronald T Raines

Open access · greenAbstract read
In one paragraph

Article in AIDS research and human retroviruses, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Sensitive detection of SARS-CoV-2 main protease 3CLProtein science : a publication of the Protein Society · 2024
    Article
  2. Massively parallel, computationally guided design of a proenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Review
  4. Article
  5. Circular zymogens of human ribonuclease 1.Protein science : a publication of the Protein Society · 2019
    Article
  6. Article
  7. Active Targeting of the Nucleus Using Nonpeptidic Boronate Tags.Journal of the American Chemical Society · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. The N-end rule pathway and regulation by proteolysis.Protein science : a publication of the Protein Society · 2011
    Review
  12. Article
  13. Converting a protein into a switch for biosensing and functional regulation.Protein science : a publication of the Protein Society · 2011
    Review
  14. Engineering an artificial zymogen by alternate frame protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. 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.

Rebecca F TurcotteMedical Scientist Training Program and Biophysics Graduate Program, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Ronald T Raines
University of Wisconsin–Madison · US

Funding

INTEGRATED TRAINING FOR PHYSICIAN-SCIENTISTST32GM008692 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BURKARD, MARK E · 1998 to 2020
$10.3M
RIBONUCLEASES IN CANCER THERAPYR01CA073808 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1997 to 2024
$7.3M
ACQUISITION OF MASS SPECTROMETER FOR CORE FACILITYS10RR013790 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI RAINES, RONALD T · 1999 to 1999
–
NCI NIH HHS CA073808NCI NIH HHS R01 CA073808NCRR NIH HHS RR13790NIGMS NIH HHS T32 GM008692
6 · The paper itself

Abstract

Ribonucleases are evoking medical interest because of their intrinsic cytotoxic activity. Most notably, ranpirnase, which is an amphibian ribonuclease, is in advanced clinical trials as a chemotherapeutic agent for the treatment of cancer. Here, we describe a strategy to create a novel antiviral agent based on bovine pancreatic ribonuclease (RNase A), a mammalian homologue of ranpirnase. Specifically, we have linked the N- and C-termini of RNase A with an amino acid sequence that is recognized and cleaved by human immunodeficiency virus (HIV) protease. This linkage obstructs the active site, forming an HIV-specific RNase A zymogen. Cleavage by HIV-1 protease increases ribonucleolytic activity by 50-fold. By relying on the proper function of HIV-1 protease, rather than its inhibition, our approach will not engender known mechanisms of resistance. Thus, we report an initial step toward a new class of agents for the treatment of HIV/AIDS.

Indexed as

Drug DesignAnimalsAnti-HIV AgentsCattleEnzyme ActivationEnzyme PrecursorsHIV-1HIV InfectionsHumansK562 CellsRibonuclease, PancreaticRibonucleasesSubstrate SpecificityAnti-HIV AgentsEnzyme PrecursorsranpirnaseRibonuclease, PancreaticRibonucleases

Identifiers

PMID19025416
PMCPMC2888699
OpenAlexW2078036275

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.