Evidence map›Paper›PMID 3541904›Full record

ArticleThe Biochemical journal1986

A systematic series of synthetic chromophoric substrates for aspartic proteinases.

B M Dunn, M Jimenez, B F Parten, M J Valler, C E Rolph, J Kay

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Ionic derivatives of betulinic acid as novel HIV-1 protease inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2012
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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

6 authors at 2 institutions in 1 country.

B M Dunn
M Jimenez
B F Parten
M J Valler
C E Rolph
J Kay
University of Florida · USFlorida College · US

Funding

MECHANISM OF PEPSIN CATALYSIS AND INHIBITIONR01AM018865 · AM · UNIVERSITY OF FLORIDA · PI DUNN, BEN M. · 1985 to 1985
–
NIADDK NIH HHS AM 18865
6 · The paper itself

Abstract

The hydrolysis of the chromogenic peptide Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu at the Phe-Phe(4-NO2) bond by nine aspartic proteinases of animal origin and seven enzymes from micro-organisms is described [Phe(4-NO2) is p-nitro-L-phenylalanine]. A further series of six peptides was synthesized in which the residue in the P3 position was systematically varied from hydrophobic to hydrophilic. The Phe-Phe(4-NO2) bond was established as the only peptide bond cleaved, and kinetic constants were obtained for the hydrolysis of these peptide substrates by a representative selection of aspartic proteinases of animal and microbial origin. The value of these water-soluble substrates for structure-function investigations is discussed.

Indexed as

AnimalsAspartic Acid EndopeptidasesBinding SitesCattleChickensChromatography, High Pressure LiquidColorimetryEndopeptidasesHumansHydrolysisKineticsMucorPeptide BiosynthesisPeptidesSpecies SpecificitySubstrate SpecificityAspartic Acid EndopeptidasesEndopeptidasesPeptides

Identifiers

PMID3541904
PMCPMC1147073
OpenAlexW1945578658

What OpenQuestion holds

Textmetadata
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.