Evidence map›Paper›PMID 21805241›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2011

Inhibitor screening of proprotein convertases using positional scanning libraries.

Iris Lindberg, Jon R Appel

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Iris LindbergSchool of Medicine Anatomy and Neurobiology, University of Maryland-Baltimore, Baltimore, MD 21201, USA. ilind001@umaryland.edu
Jon R Appel

Funding

OPIOID PEPTIDE SYNTHESIZING ENZYMESR01DA005084 · NIDA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 1988 to 2014
$4.4M
Opioid Peptide Synthesizing EnzymesR56DA005084 · NIDA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 2016 to 2016
$174k
NIDA NIH HHS DA05084NIDA NIH HHS R01 DA005084NIDA NIH HHS R56 DA005084
6 · The paper itself

Abstract

Proprotein convertases represent an important class of biosynthetic enzymes that are increasingly viewed as targets for therapeutic approaches to infection, cancer, and potentially endocrine disorders. The identification of potent inhibitors can be accomplished by screening synthetic combinatorial libraries containing thousands of small molecules to millions of peptides. In this chapter, the screening of positional scanning libraries is described for the identification of PC1/3 and PC2 inhibitors.

Indexed as

Amino Acid SequenceCombinatorial Chemistry TechniquesEndocrine System DiseasesHigh-Throughput Screening AssaysHumansInfectionsNeoplasmsPeptide LibraryPeptidesProprotein ConvertasesProtease InhibitorsSmall Molecule LibrariesPeptide LibraryPeptidesProprotein ConvertasesProtease InhibitorsSmall Molecule Libraries

Identifiers

PMID21805241
PMCPMC3845831

What OpenQuestion holds

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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.