Evidence map›Paper›PMID 8876242›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Phosphorylation of synaptic vesicle proteins: modulation of the alpha SNAP interaction with the core complex.

H Hirling, R H Scheller

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

59 citing papers in PubMed, 185 citations in OpenAlex.

  1. Syntaxin 3B: A SNARE Protein Required for Vision.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Age-Related Cognitive Impairment: Role of Reduced Synaptobrevin-2 Levels in Deficits of Memory and Synaptic Plasticity.The journals of gerontology. Series A, Biological sciences and medical sciences · 2020
    Article
  7. Article
  8. Article
  9. Diverse exocytic pathways for mast cell mediators.Biochemical Society transactions · 2018
    Review
  10. Review
  11. Review
  12. Article
  13. Millisecond CaProceedings of the Japan Academy. Series B, Physical and biological sciences · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

H HirlingHoward Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center 94305-5428, USA.
R H Scheller
University of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We analyzed whether synaptic membrane trafficking proteins are substrates for casein kinase II, calcium/calmodulin-dependent protein kinase II, and cAMP-dependent protein kinase (PKA), three kinases implicated in the modulation of synaptic transmission. Each kinase phosphorylates a specific set of the vesicle proteins syntaxin 1A, N-ethylmaleimide-sensitive factor (NSF), vesicle-associated membrane protein (VAMP), synaptosome-associated 25-kDa protein (SNAP-25), n-sec1, alpha soluble NSF attachment protein (alpha SNAP), and synaptotagmin. VAMP is phosphorylated by calcium/calmodulin-dependent protein kinase II on serine 61. alpha SNAP is phosphorylated by PKA; however, the beta SNAP isoform is phosphorylated only 20% as efficiently. alpha SNAP phosphorylated by PKA binds to the core docking and fusion complex 10 times weaker than the dephosphorylated form. These studies provide a first glimpse at regulatory events that may be important in modulating neurotransmitter release during learning and memory.

Indexed as

Vesicular Transport ProteinsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Carrier ProteinsCasein Kinase IICyclic AMP-Dependent Protein KinasesLearningMembrane FusionMembrane ProteinsMemoryMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphorylationPhosphoserineProtein Serine-Threonine KinasesCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Carrier ProteinsCasein Kinase IICyclic AMP-Dependent Protein KinasesMembrane ProteinsNerve Tissue ProteinsPhosphoserineProtein Serine-Threonine KinasesRecombinant Fusion ProteinsR-SNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsSynaptosomal-Associated Protein 25Vesicular Transport Proteins

Identifiers

PMID8876242
PMCPMC38163
OpenAlexW1972977742

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.