Evidence map›Paper›PMID 22701568›Full record

ArticlePloS one2012

A highly scalable peptide-based assay system for proteomics.

Igor A Kozlov, Elliot R Thomsen, Sarah E Munchel, Patricia Villegas, Petr Capek, Austin J Gower, Stephanie J K Pond, Eugene Chudin, Mark S Chee

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Igor A KozlovPrognosys Biosciences Inc., La Jolla, California, United States of America. ikozlov@prognosysbio.com
Elliot R Thomsen
Sarah E Munchel
Patricia Villegas
Petr Capek
Austin J Gower
Stephanie J K Pond
Eugene Chudin
Mark S Chee
Prognosys Biosciences (United States) · US

Funding

High-Throughput System for Protease Activity ProfilingR44GM085884 · NIGMS · PROGNOSYS BIOSCIENCES, INC. · PI KOZLOV, IGOR A. · 2011 to 2012
$2.1M
New Technology for Functional Studies of the KinomeR44GM090392 · NIGMS · PROGNOSYS BIOSCIENCES, INC. · PI CHEE, MARK S. · 2012 to 2013
$1.6M
Microarray Technology for Genomic AssaysR44HG004284 · NHGRI · PROGNOSYS BIOSCIENCES, INC. · PI CHEE, MARK S. · 2008 to 2009
$1.4M
New Technology for Functional Studies of the KinomeR43GM090392 · NIGMS · PROGNOSYS BIOSCIENCES, INC. · PI KOZLOV, IGOR A. · 2010 to 2011
$515k
High-Throughput System for Protease Activity ProfilingR43GM085884 · NIGMS · PROGNOSYS BIOSCIENCES, INC. · PI KOZLOV, IGOR A. · 2009 to 2010
$423k
Microarray Technology for Genomic AssaysR43HG004284 · NHGRI · PROGNOSYS BIOSCIENCES, INC. · PI CHEE, MARK S. · 2007 to 2007
$195k
NHGRI NIH HHS HG004284NHGRI NIH HHS R43 HG004284NHGRI NIH HHS R44 HG004284NIGMS NIH HHS R43 GM085884NIGMS NIH HHS R43GM085884NIGMS NIH HHS R43 GM090392NIGMS NIH HHS R43GM090392NIGMS NIH HHS R44 GM085884NIGMS NIH HHS R44 GM090392
6 · The paper itself

Abstract

We report a scalable and cost-effective technology for generating and screening high-complexity customizable peptide sets. The peptides are made as peptide-cDNA fusions by in vitro transcription/translation from pools of DNA templates generated by microarray-based synthesis. This approach enables large custom sets of peptides to be designed in silico, manufactured cost-effectively in parallel, and assayed efficiently in a multiplexed fashion. The utility of our peptide-cDNA fusion pools was demonstrated in two activity-based assays designed to discover protease and kinase substrates. In the protease assay, cleaved peptide substrates were separated from uncleaved and identified by digital sequencing of their cognate cDNAs. We screened the 3,011 amino acid HCV proteome for susceptibility to cleavage by the HCV NS3/4A protease and identified all 3 known trans cleavage sites with high specificity. In the kinase assay, peptide substrates phosphorylated by tyrosine kinases were captured and identified by sequencing of their cDNAs. We screened a pool of 3,243 peptides against Abl kinase and showed that phosphorylation events detected were specific and consistent with the known substrate preferences of Abl kinase. Our approach is scalable and adaptable to other protein-based assays.

Indexed as

DEAD-box RNA HelicasesDNA, ComplementaryHepacivirusMicroarray AnalysisNucleoside-TriphosphatasePeptide HydrolasesPeptidesPhosphorylationPhosphotransferasesProteomicsSerine EndopeptidasesSubstrate SpecificityViral Nonstructural ProteinsViral ProteasesDEAD-box RNA HelicasesDNA, ComplementaryNS3 protein, hepatitis C virusNucleoside-TriphosphatasePeptide HydrolasesPeptidesPhosphotransferasesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID22701568
PMCPMC3373263
OpenAlexW2008809353

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.