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Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
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scientific journal article
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description
2010 թվականի հունիսին հրատարակված գիտական հոդված
(hy)
artículu científicu espublizáu en 2010
(ast)
vědecký článek publikovaný v roce 2010
(cs)
наукова стаття, опублікована в червні 2010
(uk)
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
(hyw)
article scientifique publié en 2010
(fr)
im Juni 2010 veröffentlichter wissenschaftlicher Artikel
(de)
wetenschappelijk artikel (gepubliceerd op 2010/06/11)
(nl)
vedecký článok (publikovaný 2010/06/11)
(sk)
مقالة علمية (نشرت في 11-6-2010)
(ar)
scientific journal article
(en)
publication date
wds:Q28510819-352D7DBD-59F8-4A07-897D-65BE15030BD9
publication date
2010-05-27 00:00:00Z
(
xsd:dateTime
)
language of work or name
wds:Q28510819-E9FE0CB7-EE22-48AD-B928-C3384018515E
language of work or name
English
author name string
wds:Q28510819-09B0B747-DEA8-4DAB-99CF-D9C82534CAD2
wds:Q28510819-5964B0D8-58B9-4F24-9DBC-F2E57548F9E7
wds:Q28510819-7C0EA990-33A1-484E-9561-05AC4405CD84
wds:Q28510819-A0C08861-0E23-4F20-BCB7-42A8C206918B
wds:Q28510819-B0CC4BF9-EE70-4211-87A5-CFADCBCC7440
wds:Q28510819-B53B9C42-422A-4E05-8DE3-4BCAD9E70748
wds:Q28510819-F114AA1F-4AC5-4F97-96EB-A41ACBDF590E
OpenCitations bibliographic resource ID
wds:Q28510819-A4829292-94DF-4F57-AC6F-CE70EF7F3748
OpenCitations bibliographic resource ID
https://w3id.org/oc/corpus/br/1263644
author name string
Sung-Jin Lee
Masayoshi Mishina
Misato Yasumura
Moonjin Ra
Takeshi Uemura
Tomoyuki Yoshida
Kenji Sakimura
OpenCitations bibliographic resource ID
1263644
rdfs:label
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(en)
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(nl)
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(ast)
skos:prefLabel
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(en)
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(nl)
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(ast)
name
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(en)
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(nl)
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(ast)
author
wds:Q28510819-08F78E94-26BA-4884-9A17-DB2F4F40EC7D
wds:Q28510819-DEB550F4-CA55-423C-94AD-60B8F40C4BFD
author
Ryo Taguchi
Tomonori Takeuchi
title
wds:Q28510819-A4A746A5-403B-46A7-B9F2-6CEC9FF52BCD
title
Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
(en)
page(s)
wds:Q28510819-079F1141-A828-464C-B0C4-23CDEBD7F8DA
page(s)
1068-1079
instance of
wds:Q28510819-E20F0727-83C7-4121-B3BF-9CDE124F6475
instance of
scholarly article
main subject
wds:Q28510819-021661DB-879E-4578-A956-210B1E704A9C
wds:Q28510819-0FF7C89C-EDF7-4E82-BBE8-C4245F1AFD4D
wds:Q28510819-986A277A-9934-4047-BA91-341A4BB0D1F4
main subject
cerebellum
Glutamate receptor, ionotropic, delta 2
Cerebellin 1 precursor protein
PubMed ID
wds:Q28510819-9946B90A-529A-4928-87B9-02D7E5466DE8
PubMed ID
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20537373
PubMed ID
20537373
published in
wds:Q28510819-06727878-79A6-437F-ACDF-8DEF30068A35
published in
Cell
issue
wds:Q28510819-A5953EC0-215B-4F34-8AE2-E8126B07D53F
volume
wds:Q28510819-1CD2CAAA-5C76-4C78-800F-5D3E95235AA7
issue
6
volume
141
number of pages
wds:Q28510819-3FF461F6-F066-4931-AD72-A9BE3DC1C2EC
number of pages
12
(
xsd:decimal
)
DOI
wds:Q28510819-40C80523-4E03-4A0B-87EE-A26FE6B41CAC
DOI
http://dx.doi.org/10.1016/J.CELL.2010.04.035
DOI
10.1016/J.CELL.2010.04.035
is
about
of
https://www.wikidata.org/wiki/Special:EntityData/Q28510819
is
cites work
of
Glutamate receptor ion channels: structure, regulation, and function
Neuronal Nogo-A negatively regulates dendritic morphology and synaptic transmission in the cerebellum
Cell biology in neuroscience: cellular and molecular mechanisms underlying presynapse formation
Enriched expression of GluD1 in higher brain regions and its involvement in parallel fiber-interneuron synapse formation in the cerebellum.
Are Type 1 metabotropic glutamate receptors a viable therapeutic target for the treatment of cerebellar ataxia?
Structural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis
Dynamic changes in neurexins' alternative splicing: role of Rho-associated protein kinases and relevance to memory formation
High affinity neurexin binding to cell adhesion G-protein-coupled receptor CIRL1/latrophilin-1 produces an intercellular adhesion complex
Membrane-tethered monomeric neurexin LNS-domain triggers synapse formation
Synaptic cell adhesion
Pathogenetic model for Tourette syndrome delineates overlap with related neurodevelopmental disorders including Autism.
SAM68 regulates neuronal activity-dependent alternative splicing of neurexin-1
Neurexin-1α contributes to insulin-containing secretory granule docking
Structural basis for integration of GluD receptors within synaptic organizer complexes
Structure and Assembly Mechanism for Heteromeric Kainate Receptors
Presenilin/γ-secretase regulates neurexin processing at synapses
Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases
A dramatic increase of C1q protein in the CNS during normal aging.
The specific α-neurexin interactor calsyntenin-3 promotes excitatory and inhibitory synapse development
Interleukin-1 receptor accessory protein organizes neuronal synaptogenesis as a cell adhesion molecule
Single-Cell mRNA Profiling Reveals Cell-Type-Specific Expression of Neurexin Isoforms
The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins
Structures of C1q-like proteins reveal unique features among the C1q/TNF superfamily
NAB-1 instructs synapse assembly by linking adhesion molecules and F-actin to active zone proteins
A blueprint for research on Shankopathies: a view from research on autism spectrum disorder
Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor
Type 1 metabotropic glutamate receptors (mGlu1) trigger the gating of GluD2 delta glutamate receptors
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