Evidence map›Paper›PMID 25573596›Full record

ReviewExperimental cell research2015

Amyloid-β precursor protein: Multiple fragments, numerous transport routes and mechanisms.

Virgil Muresan, Zoia Ladescu Muresan

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Experimental cell research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

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  17. Review
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  19. Neural Stem Cell Death Mechanisms Induced by Amyloid Beta.Dementia and neurocognitive disorders · 2017
    Article
  20. Filling the void: a role for exercise-induced BDNF and brain amyloid precursor protein processing.American journal of physiology. Regulatory, integrative and comparative physiology · 2017
    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

2 authors.

Virgil MuresanDepartment of Pharmacology and Physiology, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07101-1709, USA. Electronic address: muresavi@njms.rutgers.edu.
Zoia Ladescu MuresanDepartment of Pharmacology and Physiology, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07101-1709, USA. Electronic address: muresazo@njms.rutgers.edu.

Funding

Reporter Mice For APP Processing And TransportR21AG039668 · NIA · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI MURESAN, ZOIA · 2011 to 2012
$352k
NIA NIH HHS AG039668NIA NIH HHS R21 AG039668
6 · The paper itself

Abstract

This review provides insight into the intraneuronal transport of the Amyloid-β Precursor Protein (APP), the prototype of an extensively posttranslationally modified and proteolytically cleaved transmembrane protein. Uncovering the intricacies of APP transport proves to be a challenging endeavor of cell biology research, deserving increased priority, since APP is at the core of the pathogenic process in Alzheimer's disease. After being synthesized in the endoplasmic reticulum in the neuronal soma, APP enters the intracellular transport along the secretory, endocytic, and recycling routes. Along these routes, APP undergoes cleavage into defined sets of fragments, which themselves are transported - mostly independently - to distinct sites in neurons, where they exert their functions. We review the currently known routes and mechanisms of transport of full-length APP, and of APP fragments, commenting largely on the experimental challenges posed by studying transport of extensively cleaved proteins. The review emphasizes the interrelationships between the proteolytic and posttranslational modifications, the intracellular transport, and the functions of the APP species. A goal remaining to be addressed in the future is the incorporation of the various views on APP transport into a coherent picture. In this review, the disease context is only marginally addressed; the focus is on the basic biology of APP transport under normal conditions. As shown, the studies of APP transport uncovered numerous mechanisms of transport, some of them conventional, and others, novel, awaiting exploration.

Indexed as

Amyloid beta-Protein PrecursorAnimalsBiological TransportHumansPeptide FragmentsAmyloid beta-Protein PrecursorPeptide FragmentsAmyloid-β Precursor ProteinIntracellular transportKinesin-1Microtubule motorsPhosphorylationSecretase cleavage

Identifiers

PMID25573596
PMCPMC4433838

What OpenQuestion holds

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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.