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S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, Marsh L, Dawson VL, Dawson TM.. Science (New York, N.Y.), 2004-04-22
Topic: Brain proteins, microglia and lab models
Plain-language summary
Parkin is an E3 ubiquitin ligase involved in the ubiquitination of proteins that are important in the survival of dopamine neurons in Parkinson's disease (PD). We show that parkin is S-nitrosylated in vitro, as well as in vivo in a mouse model of PD and in brains of patients with PD and diffuse Lewy body disease. Moreover, S-nitrosylation inhibits parkin's ubiquitin E3 ligase activity and its protective function. The inhibition of parkin's ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in these disorders by impairing the ubiquitination of parkin substrates.
What this study adds
Evidence grade: Low
Parkin was found to be S-nitrosylated in vitro, in a mouse model of Parkinson's disease, and in brains of patients with Parkinson's disease and diffuse Lewy body disease. S-nitrosylation inhibited parkin's ubiquitin E3 ligase activity and its protective function, which the authors suggest could contribute to degeneration by impairing ubiquitination of parkin substrates.
Taken from this record’s own fields, not from reading the paper. The grade is assigned from the abstract’s wording; what that means.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Chung, K. K., Thomas, B., Li, X., Pletnikova, O., Troncoso, J. C., Marsh, L., et al. (2004). S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science (New York, N.Y.). https://doi.org/10.1126/science.1093891
Vancouver
Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, Marsh L, et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science (New York, N.Y.). 2004. doi:10.1126/science.1093891. PMID: 15105460.
BibTeX
@article{chung2004-15105460,
author = {Chung, K. K. and Thomas, B. and Li, X. and Pletnikova, O. and Troncoso, J. C. and Marsh, L. and Dawson, V. L. and Dawson, T. M.},
title = {{S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function}},
journal = {Science (New York, N.Y.)},
year = {2004},
doi = {10.1126/science.1093891},
pmid = {15105460},
url = {https://doi.org/10.1126/science.1093891}
}
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 8 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
- Parkin is an E3 ubiquitin ligase involved in the ubiquitination of proteins that are important in the survival of dopamine neurons in Parkinson's disease (PD).
- We show that parkin is S-nitrosylated in vitro, as well as in vivo in a mouse model of PD and in brains of patients with PD and diffuse Lewy body disease.
- Moreover, S-nitrosylation inhibits parkin's ubiquitin E3 ligase activity and its protective function.
- The inhibition of parkin's ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in these disorders by impairing the ubiquitination of parkin substrates.
Why it matters
Parkin was found to be S-nitrosylated in vitro, in a mouse model of Parkinson's disease, and in brains of patients with Parkinson's disease and diffuse Lewy body disease. S-nitrosylation inhibited parkin's ubiquitin E3 ligase activity and its protective function, which the authors suggest could contribute to degeneration by impairing ubiquitination of parkin substrates.
Study details
- Evidence strengthLow
How this study scored 55/100
Published in a top-tier journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 10 / 10 | Tier 1 — top-tier general journal (Science (New York, N.Y.)) |
| Journal's citation record | 4 / 4 | Science: journal h-index 1,754 (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 | 2004 — older than 20 years, still counted |
| 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) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 6 / 7 | Cited 769 times (OpenAlex, 2026-10-10) |
| Citations per year | 4 / 5 | 32.0 citations a year over 24 year(s) since 2004 |
| Impact for its field and year | 5 / 6 | Cited 35.2× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 5 other studies in this library |
| Still being cited | 3 / 4 | Cited 54 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Ted M. Dawson: h-index 160 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | Johns Hopkins University: institution h-index 2,306 (OpenAlex) |
| Multicenter collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 15105460) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 55 / 100 | — |
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