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Nardilysin in human brain diseases: both friend and foe
Bernstein HG, Stricker R, Dobrowolny H, Steiner J, Bogerts B, Trübner K, Reiser G.. Amino acids, 2013-04-19
Topic: Brain proteins, microglia and lab models
Nardilysin is a metalloprotease that cleaves peptides, such as dynorphin-A, α-neoendorphin, and glucagon, at the N-terminus of arginine and lysine residues in dibasic moieties. It has various functionally important molecular interaction partners (heparin-binding epidermal growth factor-like growth factor, tumour necrosis factor-α-converting enzyme, neuregulin 1, beta-secretase 1, malate dehydrogenase, P42(IP4)/centaurin-α1, the histone H3 dimethyl Lys4, and others) and is involved in a plethora of normal brain functions. Less is known about possible implications of nardilysin for brain diseases. This review, which includes some of our own recent findings, attempts to summarize the current knowledge on possible roles of nardilysin in Alzheimer disease, Down syndrome, schizophrenia, mood disorders, alcohol abuse, heroin addiction, and cancer. We herein show that nardilysin is a Janus-faced enzyme with regard to brain pathology, being probably neuropathogenic in some diseases, but neuroprotective in others.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Bernstein, H. G., Stricker, R., Dobrowolny, H., Steiner, J., Bogerts, B., Trübner, K., et al. (2013). Nardilysin in human brain diseases: both friend and foe. Amino acids. https://doi.org/10.1007/s00726-013-1499-8
Vancouver
Bernstein HG, Stricker R, Dobrowolny H, Steiner J, Bogerts B, Trübner K, et al. Nardilysin in human brain diseases: both friend and foe. Amino acids. 2013. doi:10.1007/s00726-013-1499-8. PMID: 23604405.
BibTeX
@article{bernstein2013-23604405,
author = {Bernstein, H. G. and Stricker, R. and Dobrowolny, H. and Steiner, J. and Bogerts, B. and Trübner, K. and Reiser, G.},
title = {{Nardilysin in human brain diseases: both friend and foe}},
journal = {Amino acids},
year = {2013},
doi = {10.1007/s00726-013-1499-8},
pmid = {23604405},
url = {https://doi.org/10.1007/s00726-013-1499-8}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record names 7 authors; APA and Vancouver show the first six, BibTeX and the downloads carry all of them. Check the citation against the original before you use it.
Key findings
- Nardilysin is a metalloprotease that cleaves peptides, such as dynorphin-A, α-neoendorphin, and glucagon, at the N-terminus of arginine and lysine residues in dibasic moieties.
- It has various functionally important molecular interaction partners (heparin-binding epidermal growth factor-like growth factor, tumour necrosis factor-α-converting enzyme, neuregulin 1, beta-secretase 1, malate dehydrogenase, P42(IP4)/centaurin-α1, the histone H3 dimethyl Lys4, and others) and is involved in a plethora of normal brain functions.
- Less is known about possible implications of nardilysin for brain diseases.
- This review, which includes some of our own recent findings, attempts to summarize the current knowledge on possible roles of nardilysin in Alzheimer disease, Down syndrome, schizophrenia, mood disorders, alcohol abuse, heroin addiction, and cancer.
- We herein show that nardilysin is a Janus-faced enzyme with regard to brain pathology, being probably neuropathogenic in some diseases, but neuroprotective in others.
Why it matters
This review summarizes current knowledge on possible roles of nardilysin in brain diseases including Alzheimer disease and Down syndrome, describing it as possibly neuropathogenic in some diseases and neuroprotective in others. It is a review and does not present a treatment or cure.
Study details
- Evidence strengthLow
How this study scored 32/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Amino acids) |
| Journal's citation record | 2 / 4 | Amino Acids: journal h-index 166 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2013 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 3 / 7 | Cited 19 times (OpenAlex, 2026-10-10) |
| Citations per year | 1 / 5 | 1.3 citations a year over 15 year(s) since 2013 |
| Impact for its field and year | 1 / 6 | Cited 0.8× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 0 / 6 | No other study in this library cites it |
| Still being cited | 0 / 4 | Cited 2 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Georg Reiser: h-index 56 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | University of Duisburg-Essen: institution h-index 679 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 23604405) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 32 / 100 | — |
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