ArticleThe Biochemical journal1988
Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E.
Article in The Biochemical journal, 1988. 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 60 citations in OpenAlex.
- Intraductal papillary-mucinous tumours represent a distinct group of pancreatic neoplasms: an investigation of tumour cell differentiation and K-ras, p53 and c-erbB-2 abnormalities in 26 patients.Virchows Archiv : an international journal of pathology · 1994Trial
- Selective detection of Cathepsin E proteolytic activity.Biochimica et biophysica acta · 2010Article
- Analysis of binding interactions of pepsin inhibitor-3 to mammalian and malarial aspartic proteases.Biochemistry · 2007Article
- Immunohistochemically demonstrated variation in expression of cathepsin E between uracil-induced papillomatosis and N-butyl-N-(4-hydroxybutyl)nitrosamine-induced preneoplastic and neoplastic changes in rat urinary bladder.Virchows Archiv : an international journal of pathology · 1996Article
- Specific immunocytochemical localization of cathepsin E at the ruffled border membrane of active osteoclasts.Cell and tissue research · 1995Article
- Isolation and properties of a T-kininogenase from bovine erythrocyte membranes.Journal of protein chemistry · 1994Article
- Kinetic parameters for the generation of endothelins-1,-2 and -3 by human cathepsin E.The Biochemical journal · 1992Article
- Article
- The selectivity of statine-based inhibitors against various human aspartic proteinases.The Biochemical journal · 1990Article
- High molecular mass intracellular proteases.The Biochemical journal · 1989Review
- Inhibition of aspartic proteinases by alpha 2-macroglobulin.The Biochemical journal · 1989Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Three aspartic proteinases with similar Mr values (approx. 80,000) but from distinct sources (human gastric mucosa, human erythrocyte membranes and rat spleen) were shown to have immunological cross-reactivity and comparable mobilities when subjected to polyacrylamide-gel electrophoresis under non-denaturing conditions. Kinetic parameters (kcat, Km and Ki) were determined for the interactions of the three enzymes with two synthetic chromogenic substrates and five inhibitors (naturally occurring and synthetic). On this basis it would appear that all of the enzymes should be considered equivalent to cathepsin E. pH-activity measurements indicated that the aspartic proteinase that originated from the erythrocyte membranes retained activity at a higher pH value than either of its readily soluble counterparts.
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.