Evidence map›Paper›PMID 34064208›Full record

ReviewInternational journal of molecular sciences2021

Proteolytic α-Synuclein Cleavage in Health and Disease.

Alexandra Bluhm, Sarah Schrempel, Stephan von Hörsten, Anja Schulze, Steffen Roßner

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Neurobiology of Parkinson's Disease.International journal of molecular sciences · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Alexandra BluhmFlechsig Institute for Brain Research, University of Leipzig, 04103 Leipzig, Germany.
Sarah SchrempelFlechsig Institute for Brain Research, University of Leipzig, 04103 Leipzig, Germany.
Stephan von HörstenDepartment for Experimental Therapy, University Clinics Erlangen and Preclinical Experimental Center, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91054 Erlangen, Germany.ORCID 0000-0001-6409-0664
Anja SchulzeDepartment of Molecular Drug Design and Target Validation, Fraunhofer Institute for Cell Therapy and Immunology, 06120 Halle/Saale, Germany.ORCID 0000-0002-3358-8299
Steffen RoßnerFlechsig Institute for Brain Research, University of Leipzig, 04103 Leipzig, Germany.
Leipzig University · DEFraunhofer Institute for Cell Therapy and Immunology · DEFriedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

Alzheimer Forschung Initiative 16004Deutsche Forschungsgemeinschaft RO 2226/13-1
6 · The paper itself

Abstract

In Parkinson's disease, aggregates of α-synuclein within Lewy bodies and Lewy neurites represent neuropathological hallmarks. However, the cellular and molecular mechanisms triggering oligomeric and fibrillary α-synuclein aggregation are not fully understood. Recent evidence indicates that oxidative stress induced by metal ions and post-translational modifications such as phosphorylation, ubiquitination, nitration, glycation, and SUMOylation affect α-synuclein conformation along with its aggregation propensity and neurotoxic profiles. In addition, proteolytic cleavage of α-synuclein by specific proteases results in the formation of a broad spectrum of fragments with consecutively altered and not fully understood physiological and/or pathological properties. In the present review, we summarize the current knowledge on proteolytical α-synuclein cleavage by neurosin, calpain-1, cathepsin D, and matrix metalloproteinase-3 in health and disease. We also shed light on the contribution of the same enzymes to proteolytical processing of pathogenic proteins in Alzheimer's disease and report potential cross-disease mechanisms of pathogenic protein aggregation.

Indexed as

alpha-SynucleinAlzheimer DiseaseAnimalsHumansParkinson DiseasePeptide HydrolasesProtein AggregatesProteolysisalpha-SynucleinPeptide HydrolasesProtein Aggregatesanimal modelsdementia with Lewy bodiesParkinson’s diseasepost-translational modificationproteolysissubstantia nigraα-synuclein

Identifiers

PMID34064208
PMCPMC8196865
OpenAlexW3165115994

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.