ArticleBioorganic & medicinal chemistry letters2008
Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype.
Article in Bioorganic & medicinal chemistry letters, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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.
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.
Who cites it
9 citing papers in PubMed.
- COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks.International journal of biological macromolecules · 2021Review
- SARS-CoV-2 Entry Inhibitors: Small Molecules and Peptides Targeting Virus or Host Cells.International journal of molecular sciences · 2020Review
- A Review of Small Molecule Inhibitors and Functional Probes of Human Cathepsin L.Molecules (Basel, Switzerland) · 2020Review
- Insights into the Interactions of Fasciola hepatica Cathepsin L3 with a Substrate and Potential Novel Inhibitors through In Silico Approaches.PLoS neglected tropical diseases · 2015Article
- Cell entry of enveloped viruses.Advances in genetics · 2011Review
- A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and ebola pseudotype virus infection into human embryonic kidney 293T cells.Molecular pharmacology · 2010Article
- Design, synthesis and biological evaluation of a library of thiocarbazates and their activity as cysteine protease inhibitors.Combinatorial chemistry & high throughput screening · 2010Article
- Design, synthesis, and biological evaluation of potent thiosemicarbazone based cathepsin L inhibitors.Bioorganic & medicinal chemistry letters · 2010Article
- The identification, characterization and optimization of small molecule probes of cysteine proteases: experiences of the Penn Center for Molecular Discovery with cathepsin B and cathepsin L.Current topics in medicinal chemistry · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Recently, we identified a thiocarbazate that exhibits potent inhibitory activity against human cathepsin L. Since this structure represents a novel chemotype with potential for activity against the entire cysteine protease family, we designed, synthesized, and assayed a series of analogs to probe the mechanism of action, as well as the structural requirements for cathepsin L activity. Molecular docking studies using coordinates of a papain-inhibitor complex as a model for cathepsin L provided useful insights.
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Registered trials
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.