ArticleThe Biochemical journal1989
The inhibition of proinsulin-processing endopeptidase activities by active-site-directed peptides.
Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 33 citations in OpenAlex.
- Regulation of neuropeptide processing enzymes by catecholamines in endocrine cells.Molecular pharmacology · 2011Article
- Kinetics of an autocatalytic zymogen reaction in the presence of an inhibitor coupled to a monitoring reaction.Bulletin of mathematical biology · 1996Article
- Differences between the catalytic properties of recombinant human PC2 and endogenous rat PC2.The Biochemical journal · 1995Article
- Insulin secretory granule biogenesis and the proinsulin-processing endopeptidases.Diabetologia · 1994Review
- Review
- Sorting and processing of secretory proteins.The Biochemical journal · 1994Review
- The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast.The Biochemical journal · 1993Article
- The kinetics of enzyme systems involving activation of zymogens.Bulletin of mathematical biology · 1993Article
- Processing of proopiomelanocortin by insulin secretory granule proinsulin processing endopeptidases.The Journal of biological chemistry · 1993Article
- Kinetic analysis of the type-1 proinsulin endopeptidase by a monoclonal antibody-based immunoadsorbent assay.The Biochemical journal · 1992Article
- The enzymology of proinsulin conversion.Cell biophysicsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Inhibitor studies were performed on the two endopeptidase activities involved in proinsulin conversion in isolated insulin secretory granules [Davidson, Rhodes & Hutton (1988) Nature (London) 333, 93-96]. The active-site-directed peptides L-alanyl-L-arginyl-L-arginylmethyldimethylsulphonium and L-alanyl-L-lysyl-L-arginylmethyldimethylsulphonium inhibited these activities in accordance with the observed cleavage pattern, suggesting that the primary amino acid sequence of the dibasic site was an important determinant of the endopeptidase substrate specificities.
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.