ArticleInflammation research : official journal of the European Histamine Research Society ... [et al.]1996
Substrate specificity and inhibitor profile of human recombinant p56lck from a baculovirus expression vector.
Article in Inflammation research : official journal of the European Histamine Research Society ... [et al.], 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed, 4 citations in OpenAlex.
- Peptide reporters of kinase activity in whole cell lysates.Biopolymers · 2010Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p56lck, a member of the src family of non-receptor protein receptor kinases, is required for normal signal transduction through the T cell receptor. Inappropriate T cell activation and proliferation has been identified as an early event in auto-immune disease-agents which control T cell activation through modulation of p56lck kinase activity could therefore be potential therapeutic agents for a range of pathological conditions. To identify p56lck inhibitors, we have established an assay system suitable for the high throughput screening of compound libraries. The assay uses enzyme purified from baculovirus infected SF9 cells, and a novel peptidic substrate identified by L. Cantley from a degenerate combinatorial peptide library. We have used this assay system to screen a number of different compounds as potential inhibitors of p56lck. In addition, peptides based on the substrate sequence were also tested to identify a sequence that could be used in the rational design of peptide inhibitors of p56lck.
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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.