Evidence map›Paper›PMID 2182650›Full record

ArticleThe Journal of cell biology1990

P29: a novel tyrosine-phosphorylated membrane protein present in small clear vesicles of neurons and endocrine cells.

M Baumert, K Takei, J Hartinger, P M Burger, G Fischer von Mollard, P R Maycox, P De Camilli, R Jahn

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Genetic Regulation of Immunoglobulin G Glycosylation.Experientia supplementum (2012) · 2021
    Article
  3. Article
  4. Synaptic vesicles studied by dynamic light scattering.The European physical journal. E, Soft matter · 2011
    Article
  5. Article
  6. Article
  7. A conserved mechanism of synaptogyrin localization.Molecular biology of the cell · 2001
    Article
  8. Article
  9. Article
  10. Article
  11. Multiple and diverse forms of regulated exocytosis in wild-type and defective PC12 cells.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  12. SVOP, an evolutionarily conserved synaptic vesicle protein, suggests novel transport functions of synaptic vesicles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. A gamma-aminobutyric acid transporter driven by a proton pump is present in synaptic-like microvesicles of pancreatic beta cells.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
  19. Article
  20. Article
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

8 authors.

M BaumertDepartment of Neurochemistry, Max-Planck-Institute for Psychiatry, Martinsried, Federal Republic of Germany.
K Takei
J Hartinger
P M Burger
G Fischer von Mollard
P R Maycox
P De Camilli
R Jahn

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel membrane protein from rat brain synaptic vesicles with an apparent 29,000 Mr (p29) was characterized. Using monospecific polyclonal antibodies, the distribution of p29 was studied in a variety of tissues by light and electron microscopy and immunoblot analysis. Within the nervous system, p29 was present in virtually all nerve terminals. It was selectively associated with small synaptic vesicles and a perinuclear region corresponding to the area of the Golgi complex. P29 was not detected in any other subcellular organelles including large dense-core vesicles. The distribution of p29 in various subcellular fractions from rat brain was very similar to that of synaptophysin and synaptobrevin. The highest enrichment occurred in purified small synaptic vesicles. Outside the nervous system, p29 was found only in endocrine cell types specialized for peptide hormone secretion. In these cells, p29 had a distribution very similar to that of synaptophysin. It was associated with microvesicles of heterogeneous size and shape that are primarily concentrated in the centrosomal-Golgi complex area. Secretory granules were mostly unlabeled, but their membrane occasionally contained small labeled evaginations. Immunoisolation of subcellular organelles from undifferentiated PC12 cells with antisynaptophysin antibodies led to a concomitant enrichment of p29, synaptobrevin, and synaptophysin, further supporting a colocalization of all three proteins. P29 has an isoelectric point of approximately 5.0 and is not N-glycosylated. It is an integral membrane protein and all antibody binding sites are exposed on the cytoplasmic side of the vesicles. Two monoclonal antibodies raised against p29 cross reacted with synaptophysin, indicating the presence of related epitopes. P29, like synaptophysin, was phosphorylated on tyrosine residues by endogenous tyrosine kinase activity in intact vesicles.

Indexed as

AnimalsAntibodiesAntibodies, MonoclonalBrainBrain ChemistryCattleCell FractionationCerebral CortexElectrophoresis, Polyacrylamide GelEndocrine GlandsFluorescent Antibody TechniqueMembrane ProteinsMicroscopy, ElectronMolecular WeightMotor EndplateNerve Tissue ProteinsAntibodiesAntibodies, MonoclonalMembrane ProteinsNerve Tissue ProteinsPhosphoproteins

Identifiers

PMID2182650
PMCPMC2116065
OpenAlexW2058860860

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.