Evidence map›Paper›PMID 32158194›Full record

ArticleDrug design, development and therapy2020

Metalloprotoporphyrin Inhibition of HCV NS3-4A Protease: Structure-Activity Relationships.

Katherine Hu, Zhaowen Zhu, Meleah M Mathahs, Huy Tran, Jerry Bommer, Charles A Testa, Warren N Schmidt

Open access · goldAbstract read
In one paragraph

Article in Drug design, development and therapy, 2020. 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
0.4field-weighted citation impact, top 41% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

7 authors at 3 institutions in 1 country.

Katherine HuDepartment of Internal Medicine and Research Service, Veterans Affairs Medical Center, Iowa City, IA 52246, USA.ORCID 0000-0003-0724-5433
Zhaowen ZhuDepartment of Internal Medicine and Research Service, Veterans Affairs Medical Center, Iowa City, IA 52246, USA.
Meleah M MathahsDepartment of Internal Medicine and Research Service, Veterans Affairs Medical Center, Iowa City, IA 52246, USA.
Huy TranDepartment of Internal Medicine and Research Service, Veterans Affairs Medical Center, Iowa City, IA 52246, USA.ORCID 0000-0001-5383-3143
Jerry BommerFrontier Scientific, Logan, UT 84321, USA.
Charles A TestaCurza, Provo, UT and Cambridge, MA, USA.
Warren N SchmidtDepartment of Internal Medicine and Research Service, Veterans Affairs Medical Center, Iowa City, IA 52246, USA.
University of Iowa · USFrontier Scientific (United States) · USProvo College · US

Funding

Neoplastic interactions of hepatitis C virus with telomerase.I01BX000159 · VA · IOWA CITY VA MEDICAL CENTER · PI SCHMIDT, WARREN N · 2009 to 2021
–
BLRD VA I01 BX000159
6 · The paper itself

Abstract

backgroundAntiviral actions of tetrapyrroles have been described in a number of systems. Our goal was to evaluate antagonism of the HCV NS3-4A protease by a variety of common porphyrins and characterize structure-activity relationships that may be useful for future drug design of HCV and related

methodsUsing fluorometric assays, common metalloprotoporphyrins (MPP) all inhibited NS3-4A protease with IC

resultsLineweaver-Burk plots confirmed that MPP: NS3 inhibition was basically competitive. All tested MPPs inhibited HCV genotype 1A, 1B, 2A and 3A recombinant proteases with the same fidelity suggesting wide antagonistic capabilities. However, when the MPPs were tested in cellular incubations with HCV replicons only Zn, Fe and free-base protoporphyrin showed comparable EC

conclusionThese findings document the versatility of MPPs as antiviral agents with an expanded sensitivity for HCV genotypes and resistance to some common viral mutations. The results also suggest that further study of MPP structure and function will be useful for the development of new antiviral agents.

Indexed as

Antiviral AgentsCells, CulturedDose-Response Relationship, DrugHepacivirusHumansMicrobial Sensitivity TestsMolecular StructureProtease InhibitorsSerine ProteasesStructure-Activity RelationshipViral Nonstructural ProteinsVirus ReplicationAntiviral AgentsNS3-4A serine protease, Hepatitis C virusProtease InhibitorsSerine ProteasesViral Nonstructural Proteinsantiviral agentshepatitis C genotypehepatitis C virusporphyrins

Identifiers

PMID32158194
PMCPMC7048954
OpenAlexW3007575355

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.