ArticlePloS one2012
Active site mutations change the cleavage specificity of neprilysin.
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 6 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
6 citing papers in PubMed, 19 citations in OpenAlex.
- Serum proenkephalin-A as a potential biomarker for assessing renal impairment severity in diabetic kidney disease.Irish journal of medical science · 2026Article
- Breaking barriers: Neprilysin inhibition in chronic cardiorenal syndrome.World journal of cardiology · 2025Review
- Effect of Mutation Type on Ectopic Ossification Among Adult Patients With X-Linked Hypophosphatemia.Journal of the Endocrine Society · 2024Article
- Proenkephalin: A New Biomarker for Glomerular Filtration Rate and Acute Kidney Injury.Nephron · 2020Review
- Membrane metallo-endopeptidase (Neprilysin) regulates inflammatory response and insulin signaling in white preadipocytes.Molecular metabolism · 2019Article
- Engineering neprilysin activity and specificity to create a novel therapeutic for Alzheimer's disease.PloS one · 2014Article
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
Neprilysin (NEP), a member of the M13 subgroup of the zinc-dependent endopeptidase family is a membrane bound peptidase capable of cleaving a variety of physiological peptides. We have generated a series of neprilysin variants containing mutations at either one of two active site residues, Phe(563) and Ser(546). Among the mutants studied in detail we observed changes in their activity towards leucine(5)-enkephalin, insulin B chain, and amyloid β(1-40). For example, NEP(F563I) displayed an increase in preference towards cleaving leucine(5)-enkephalin relative to insulin B chain, while mutant NEP(S546E) was less discriminating than neprilysin. Mutants NEP(F563L) and NEP(S546E) exhibit different cleavage site preferences than neprilysin with insulin B chain and amyloid ß(1-40) as substrates. These data indicate that it is possible to alter the cleavage site specificity of neprilysin opening the way for the development of substrate specific or substrate exclusive forms of the enzyme with enhanced therapeutic potential.
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Registered trials
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