Evidence map›Paper›PMID 30700558›Full record

ReviewThe Journal of biological chemistry2019

Intrinsically disordered proteins in synaptic vesicle trafficking and release.

David Snead, David Eliezer

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  15. Investigating Complexin-Membrane Interactions Using NMR and Optical Methods.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  16. Review
  17. Mild cognitive impairment in Huntington's disease: challenges and outlooks.Journal of neural transmission (Vienna, Austria : 1996) · 2024
    Review
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  19. Article
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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

2 authors at 1 institution in 1 country.

David SneadFrom the Department of Biochemistry, Weill Cornell Medicine, New York, New York 10021.
David EliezerFrom the Department of Biochemistry, Weill Cornell Medicine, New York, New York 10021 dae2005@med.cornell.edu.ORCID 0000-0002-1311-7537
Cornell University · US

Funding

Structure and Function of Alpha-SynucleinR37AG019391 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2010 to 2019
$3.4M
Structure and Function of Alpha-SynucleinR01AG019391 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2001 to 2009
$2.6M
Structure and Function of ComplexinR01GM117518 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2016 to 2019
$1.3M
Biophysical Characterization of Complexin C-terminal Domain Lipid InteractionsF30MH101982 · NIMH · WEILL MEDICAL COLL OF CORNELL UNIV · PI SNEAD, DAVID M · 2013 to 2016
$190k
NIA NIH HHS R01 AG019391NIA NIH HHS R37 AG019391NIGMS NIH HHS R01 GM117518NIMH NIH HHS F30 MH101982
6 · The paper itself

Abstract

The past few years have resulted in an increased awareness and recognition of the prevalence and roles of intrinsically disordered proteins and protein regions (IDPs and IDRs, respectively) in synaptic vesicle trafficking and exocytosis and in overall synaptic organization. IDPs and IDRs constitute a class of proteins and protein regions that lack stable tertiary structure, but nevertheless retain biological function. Their significance in processes such as cell signaling is now well accepted, but their pervasiveness and importance in other areas of biology are not as widely appreciated. Here, we review the prevalence and functional roles of IDPs and IDRs associated with the release and recycling of synaptic vesicles at nerve terminals, as well as with the architecture of these terminals. We hope to promote awareness, especially among neuroscientists, of the importance of this class of proteins in these critical pathways and structures. The examples discussed illustrate some of the ways in which the structural flexibility conferred by intrinsic protein disorder can be functionally advantageous in the context of cellular trafficking and synaptic function.

Indexed as

AnimalsBiological Transport, ActiveExocytosisHumansIntrinsically Disordered ProteinsSynaptic VesiclesIntrinsically Disordered Proteinscomplexinintrinsically disordered proteinlipid vesiclemembraneless organellesmembrane traffickingneurotransmitter releasephase transitionsprotein foldingsynaptic vesiclesα-synuclein

Identifiers

PMID30700558
PMCPMC6416451
OpenAlexW2912919723

What Socratic 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 Socratic graph.