ReviewBioorganic & medicinal chemistry2009
Using specificity to strategically target proteases.
Review in Bioorganic & medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- PERRC: Protease Engineering with Reactant Residence Time Control.ACS synthetic biology · 2025Article
- Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- HTS by NMR of combinatorial libraries: a fragment-based approach to ligand discovery.Chemistry & biology · 2013Article
- Macromolecular assembly-driven processing of the 2/3 cleavage site in the alphavirus replicase polyprotein.Journal of virology · 2012Article
- Recent development of highly sensitive protease assay methods: Signal amplification through enzyme cascades.Biotechnology and bioprocess engineering : BBE · 2012Review
- Proteolytic Activity Matrix Analysis (PrAMA) for simultaneous determination of multiple protease activities.Integrative biology : quantitative biosciences from nano to macro · 2011Article
- Peptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors.Chemistry & biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Proteases are a family of naturally occurring enzymes in the body whose dysregulation has been implicated in numerous diseases and cancers. Their ability to selectively and catalytically turnover substrate adds both signal amplification and functionality as parameters for the detection of disease. This review will focus on the development of activity-based methodologies to characterize proteases, and in particular, the use of positional scanning, synthetic combinatorial libraries (PS-SCL's), and substrate activity screening (SAS) assays. The use of these approaches to better understand a protease's natural substrate will be discussed as well as the technologies that emerged.
Indexed as
Identifiers
What OpenQuestion holds
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.