Evidence map›Paper›PMID 41068187›Full record

ArticleScientific reports2025

High-throughput screening and characterization of novel inhibitors targeting HIV-1 protease precursor autoprocessing.

Ryan H Jeep, Liangqun Huang, Tram A Ngo, Fu-Yue Zeng, James Boehlke, Luke Bennett, Stanton Ashman, Ian Pass, Thomas D Y Chung, Chaoping Chen

Abstract read
In one paragraph

Article in Scientific reports, 2025. 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

10 authors.

Ryan H JeepDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, USA.
Liangqun HuangDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, USA.
Tram A NgoSanford Burnham Prebys Medical Discovery Institute, Lo Jolla, CA, 92037, USA.
Fu-Yue ZengSanford Burnham Prebys Medical Discovery Institute, Lo Jolla, CA, 92037, USA.
James BoehlkeDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, USA.
Luke BennettDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, USA.
Stanton AshmanDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, USA.
Ian PassSanford Burnham Prebys Medical Discovery Institute, Lo Jolla, CA, 92037, USA.
Thomas D Y ChungSanford Burnham Prebys Medical Discovery Institute, Lo Jolla, CA, 92037, USA.
Chaoping ChenDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, USA. chaoping@colostate.edu.

Funding

HTS Targeting HIV-1 Protease Autoprocessing for First in Class Drug DiscoveryR01AI150223 · NIAID · COLORADO STATE UNIVERSITY · PI CHEN, CHAOPING, CHUNG, THOMAS D Y · 2020 to 2023
$2.6M
Assay Development for Identification of HIV-1 Protease Autoprocessing Specific InhibitorsR01AI120365 · NIAID · COLORADO STATE UNIVERSITY · PI CHEN, CHAOPING, LABARBERA, DANIEL V. · 2016 to 2018
$1.1M
Assay Development and Validation for Precision Antiretroviral Therapy to Combat Drug ResistanceR56AI179558 · NIAID · COLORADO STATE UNIVERSITY · PI CHEN, CHAOPING · 2023 to 2023
$340k
National Institute of Allergy and Infectious Diseases R01AI150223National Institute of Allergy and Infectious Diseases R56AI179558NIAID NIH HHS R01 AI120365NIAID NIH HHS R01 AI150223NIAID NIH HHS R56 AI179558
6 · The paper itself

Abstract

HIV-1 protease (PR) is initially synthesized as part of the Gag-Pol polyprotein precursor, which undergoes temporospatially regulated autoprocessing to liberate mature PR. The free mature enzyme is the target of currently available protease inhibitors (PIs). To explore alternative therapeutic strategies, we developed a cell-based high-throughput screening (HTS) platform targeting precursor autoprocessing, screened approximately 320,000 small molecules, and identified 27 compounds that partially suppress precursor autoprocessing. A highly sensitive infectivity assay confirmed that several compounds inhibited viral infectivity in a dose-dependent manner, with EC

Indexed as

High-Throughput Screening AssaysHIV-1HIV ProteaseHIV Protease InhibitorsDrug DiscoveryDrug Resistance, ViralHEK293 CellsHumansStructure-Activity RelationshipHIV ProteaseHIV Protease Inhibitorsp16 protease, Human immunodeficiency virus 1

Identifiers

PMID41068187
PMCPMC12511561

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.