Evidence map›Paper›PMID 32633155›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2020

Design, synthesis, and

Thomas S Corrigan, Leilani M Lotti Diaz, Sarah E Border, Steven C Ratigan, Kayla Q Kasper, Daniel Sojka, Pavla Fajtova, Conor R Caffrey, Guy S Salvesen, Craig A McElroy and 2 more

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Synthesis, structures and Hirshfeld surface analyses of 2-hy-droxy-Acta crystallographica. Section E, Crystallographic communications · 2024
    Article
  3. 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

12 authors at 6 institutions in 2 countries.

Thomas S CorriganDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Leilani M Lotti DiazDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Sarah E BorderDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Steven C RatiganDivision of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, The Ohio State University, Columbus, OH, USA.
Kayla Q KasperDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Daniel SojkaInstitute of Parasitology, Biology Centre of the Czech Academy of Sciences, Ceske Budejovice, Czech Republic.
Pavla FajtovaCenter for Discovery and Innovation in Parasitic Diseases, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.
Conor R CaffreyCenter for Discovery and Innovation in Parasitic Diseases, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.
Guy S SalvesenSanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Craig A McElroyDivision of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, The Ohio State University, Columbus, OH, USA.
Christopher M HadadDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Özlem Doğan EkiciDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
The Ohio State University · USCenter for Discovery · USInstitute of Parasitology · CZSanford Burnham Prebys Medical Discovery Institute · USThe Ohio State University Newark · USUniversity of California, San Diego · US

Funding

Survival Mechanisms for Apoptotic CaspaseR01GM099040 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI SALVESEN, GUY S. · 2012 to 2020
$3.8M
Defining the death transcriptome of Schistosoma mansoni to construct a molecular drug screenR21AI126296 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CAFFREY, CONOR · 2017 to 2018
$415k
NIAID NIH HHS R21 AI126296NIGMS NIH HHS R01 GM099040
6 · The paper itself

Abstract

Aza-peptide aldehydes and ketones are a new class of reversible protease inhibitors that are specific for the proteasome and clan CD cysteine proteases. We designed and synthesised aza-Leu derivatives that were specific for the chymotrypsin-like active site of the proteasome, aza-Asp derivatives that were effective inhibitors of caspases-3 and -6, and aza-Asn derivatives that inhibited

Indexed as

Drug DesignAldehydesAnimalsAza CompoundsCattleCrystallography, X-RayCysteine EndopeptidasesDose-Response Relationship, DrugHumansKetonesModels, MolecularMolecular StructurePeptidesProtease InhibitorsProteasome Endopeptidase ComplexStructure-Activity RelationshipAldehydesAza CompoundsCysteine EndopeptidasesKetonesPeptidesProtease InhibitorsProteasome Endopeptidase Complexanticancerantiparasiticaza-peptide carbonylscaspase and legumain inhibitorsProteasome inhibitor

Identifiers

PMID32633155
PMCPMC7470110
OpenAlexW3041428447

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.