Evidence map›Paper›PMID 9463376›Full record

ArticleThe EMBO journal1998

Synapsin I is structurally similar to ATP-utilizing enzymes.

L Esser, C R Wang, M Hosaka, C S Smagula, T C Südhof, J Deisenhofer

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
  2. Article
  3. Synapsin Is Required for Dense Core Vesicle Capture and cAMP-Dependent Neuropeptide Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  4. Phase separation at the synapse.Nature neuroscience · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. ATP binding to synaspsin IIa regulates usage and clustering of vesicles in terminals of hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  16. Article
  17. Functional role of ATP binding to synapsin I in synaptic vesicle trafficking and release dynamics.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  18. Review
  19. Article
  20. The ATP-grasp enzymes.Bioorganic chemistry · 2011
    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

6 authors at 1 institution in 1 country.

L EsserHoward Hughes Medical Institute, Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9050, USA.
C R Wang
M Hosaka
C S Smagula
T C Südhof
J Deisenhofer
The University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110-420 of bovine synapsin I; synC coincides with the large middle domain (C-domain), the most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure to a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine:D-alanine ligase. SynC binds ATP in a Ca2+-dependent manner. The crystal structure of synC in complex with ATPgammaS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.

Indexed as

Adenosine TriphosphateAnimalsBinding SitesCalciumCattleCrystallography, X-RayDimerizationGlutathione SynthaseModels, MolecularPeptide SynthasesProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidStructure-Activity RelationshipSynapsinsAdenosine TriphosphateCalciumD-alanylalanine synthetaseGlutathione SynthasePeptide SynthasesSynapsins

Identifiers

PMID9463376
PMCPMC1170447
OpenAlexW1987040923

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.