Evidence map›Paper›PMID 17062754›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

A peptide zipcode sufficient for anterograde transport within amyloid precursor protein.

Prasanna Satpute-Krishnan, Joseph A DeGiorgis, Michael P Conley, Marcus Jang, Elaine L Bearer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

52 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
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  6. Review
  7. The Giant Axon of the Squid: A Simple System for Axonal Transport Studies.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Redox signaling and metabolism in Alzheimer's disease.Frontiers in aging neuroscience · 2022
    Review
  9. Article
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  15. Review
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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.

Prasanna Satpute-KrishnanDepartment of Pathology and Laboratory Medicine, Brown University Medical School, 70 Ship Street, Providence, RI 02912, USA.
Joseph A DeGiorgis
Michael P Conley
Marcus Jang
Elaine L Bearer
Brown University · USMarine Biological Laboratory · USNational Institute of Neurological Disorders and Stroke · US

Funding

Molecular mechanisms of anterograde transportR01NS046810 · NINDS · BROWN UNIVERSITY · PI BEARER, ELAINE L · 2004 to 2007
$1.1M
STRUCTURE OF NEURONAL CYTOPLASMZ01NS002551 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI REESE, THOMAS S · 1985 to 2008
$810k
Intramural NIH HHSNIGMS NIH HHS GM 47562NINDS NIH HHS NS 046810NINDS NIH HHS R01 NS046810
6 · The paper itself

Abstract

Fast anterograde transport of membrane-bound organelles delivers molecules synthesized in the neuronal cell body outward to distant synapses. Identification of the molecular "zipcodes" on organelles that mediate attachment and activation of microtubule-based motors for this directed transport is a major area of inquiry. Here we identify a short peptide sequence (15 aa) from the cytoplasmic C terminus of amyloid precursor protein (APP-C) sufficient to mediate the anterograde transport of peptide-conjugated beads in the squid giant axon. APP-C beads travel at fast axonal transport rates (0.53 mum/s average velocity, 0.9 mum/s maximal velocity) whereas beads coupled to other peptides coinjected into the same axon remain stationary at the injection site. This transport appears physiologic, because it mimics behavior of endogenous squid organelles and of beads conjugated to C99, a polypeptide containing the full-length cytoplasmic domain of amyloid precursor protein (APP). Beads conjugated to APP lacking the APP-C domain are not transported. Coinjection of APP-C peptide reduces C99 bead motility by 75% and abolishes APP-C bead motility, suggesting that the soluble peptide competes with protein-conjugated beads for axoplasmic motor(s). The APP-C domain is conserved (13/15 aa) from squid to human, and peptides from either squid or human APP behave similarly. Thus, we have identified a conserved peptide zipcode sufficient to direct anterograde transport of exogenous cargo and suggest that one of APP's roles may be to recruit and activate axonal machinery for endogenous cargo transport.

Indexed as

Axonal TransportAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsAxonsConserved SequenceCytoplasmDecapodiformesHumansMolecular Sequence DataPeptide FragmentsAmyloid beta-Protein PrecursorPeptide Fragments

Identifiers

PMID17062754
PMCPMC1621108
OpenAlexW1989861729

What OpenQuestion holds

Textmetadata
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.