Evidence map›Paper›PMID 19619643›Full record

ReviewBiochimica et biophysica acta2010

Mitochondrial trafficking of APP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases.

Latha Devi, Hindupur K Anandatheerthavarada

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

72 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Multi-Target-Directed Cinnamic Acid Hybrids Targeting Alzheimer's Disease.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Revisiting Alpha-Synuclein Pathways to Inflammation.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Clusterin: a multifaceted protein in the brain.Neural regeneration research · 2021
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Latha DeviDepartment of Animal Biology, School of Veterinary Medicine, 3800 Spruce Street, University of Pennsylvania, Philadelphia, PA 19104, USA.
Hindupur K Anandatheerthavarada
University of Pennsylvania · US

Funding

APP Mediated Mitochondrial Injury in Aging NeuronsR01AG021920 · NIA · UNIVERSITY OF PENNSYLVANIA · PI HINDUPUR, ANAND · 2004 to 2007
$1.2M
NIA NIH HHS R01 AG 021920NIA NIH HHS R01 AG021920
6 · The paper itself

Abstract

Mitochondrial dysfunction is an important intracellular lesion associated with a wide variety of diseases including neurodegenerative disorders. In addition to aging, oxidative stress and mitochondrial DNA mutations, recent studies have implicated a role for the mitochondrial accumulation of proteins such as plasma membrane associated amyloid precursor protein (APP) and cytosolic alpha synuclein in the pathogenesis of mitochondrial dysfunction in Alzheimer's disease (AD) and Parkinson's disease (PD), respectively. Both of these proteins contain cryptic mitochondrial targeting signals, which drive their transport across mitochondria. In general, mitochondrial entry of nuclear coded proteins is assisted by import receptors situated in both outer and inner mitochondrial membranes. A growing number of evidence suggests that APP and alpha synclein interact with import receptors to gain entry into mitochondrial compartment. Additionally, carboxy terminal cleaved product of APP, approximately 4 kDa Abeta, is also transported into mitochondria with the help of mitochondrial outer membrane import receptors. This review focuses on the mitochondrial targeting and accumulation of these two structurally different proteins and the mode of mechanism by which they affect the physiological functions of mitochondria.

Indexed as

alpha-SynucleinAlzheimer DiseaseAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsHumansMiceMitochondriaMitochondrial MembranesModels, BiologicalMolecular Sequence DataParkinson DiseaseProtein Transportalpha-SynucleinAmyloid beta-Protein Precursor

Identifiers

PMID19619643
PMCPMC2790550
OpenAlexW2119059352

What OpenQuestion holds

Textmetadata
LicenceTDM
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.