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Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
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scientific journal article
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rdf:type
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description
artículu científicu espublizáu en 2000
(ast)
vědecký článek publikovaný v roce 2000
(cs)
wüsseschaftlicher Artikel, wo im März 2000 veröffentlicht worden isch
(gsw)
im März 2000 veröffentlichter wissenschaftlicher Artikel
(de)
2000 թվականի մարտին հրատարակված գիտական հոդված
(hy)
наукова стаття, опублікована в березні 2000
(uk)
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
(hyw)
wetenschappelijk artikel (gepubliceerd op 2000/03/16)
(nl)
vedecký článok (publikovaný 2000/03/16)
(sk)
مقالة علمية (نشرت في 16-3-2000)
(ar)
article publié dans la revue scientifique Nature
(fr)
scientific journal article
(en)
publication date
wds:Q28576517-A51C7390-BB9D-4E68-A8DB-BC9C4680A845
publication date
2000-03-16 00:00:00Z
(
xsd:dateTime
)
language of work or name
wds:Q28576517-DBC1D9D6-8DC4-4A5E-A2AA-888AED783CD8
language of work or name
English
cites work
wds:Q28576517-0A40D528-E105-49E0-A6ED-59B1D05D5882
wds:Q28576517-0F2B7B1C-2869-4B43-9247-C062538C8EF4
wds:Q28576517-209061CF-3F63-4C46-9D78-C28CA5DFC871
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wds:Q28576517-35B586F2-900B-4A1A-A364-B91C8468F089
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wds:Q28576517-529B3B83-D35F-46B1-BAE4-3E461743AC21
wds:Q28576517-5AA193F3-6E29-473F-A538-AE2BDD32F43A
wds:Q28576517-668B3A2E-872F-4960-8F36-9015DA6B6072
wds:Q28576517-66E21BF6-C1BE-453D-A4AE-1822A6DE2F6A
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wds:Q28576517-F5A1F356-8732-40EC-A1FE-34C802AC0566
cites work
Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting
Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
Polarized signaling: basolateral receptor localization in epithelial cells by PDZ-containing proteins
PDZ proteins organize synaptic signaling pathways
Cell signalling: MAGUK magic
The T protein encoded by Brachyury is a tissue-specific transcription factor
The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules
A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
Signal transduction through beta-catenin and specification of cell fate during embryogenesis
Beta-catenin as oncogene: the smoking gun.
Tissue-specific in vitro transcription from the mouse albumin promoter
The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts.
T-brain-1: a homolog of Brachyury whose expression defines molecularly distinct domains within the cerebral cortex
Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4.
Identification of ion channel-associated proteins using the yeast two-hybrid system
Sorting out genes that regulate epithelial and neuronal polarity.
author name string
wds:Q28576517-068372EC-0BCB-409C-B3C0-BAE3FDB4490A
wds:Q28576517-173EDF2F-34A7-475C-82F3-C5373DB7E6ED
wds:Q28576517-6F73D844-1ADD-4268-80DA-2FFB953C6E11
wds:Q28576517-E0837372-CE95-4208-8B71-17FC80B706C8
OpenCitations bibliographic resource ID
wds:Q28576517-4B6BF7D7-3692-4106-8D2B-35B4E5EB64EF
OpenCitations bibliographic resource ID
https://w3id.org/oc/corpus/br/4974508
author name string
F. C. Yang
M. Sheng
T. F. Wang
Y. P. Hsueh
OpenCitations bibliographic resource ID
4974508
rdfs:label
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(en)
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(nl)
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(ast)
skos:prefLabel
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(en)
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(nl)
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(ast)
name
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(en)
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(nl)
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(ast)
title
wds:Q28576517-90D1F3C0-96A2-4507-BF0A-07D662EA0E14
title
Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
(en)
page(s)
wds:Q28576517-9537562E-1578-4B5C-B7E8-69EBF6BFA256
page(s)
298–302
instance of
wds:Q28576517-65933EA0-2188-4B59-A26C-AD489D34D095
instance of
scholarly article
PubMed ID
wds:Q28576517-A00061A6-6839-41EC-87F2-15523D4CB31C
PubMed ID
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10749215
PubMed ID
10749215
published in
wds:Q28576517-C0ABF4B5-A979-4EA6-B13B-3E481ECE6D0E
published in
Nature
issue
wds:Q28576517-939C8711-FBEB-4D31-8150-3BD015156F3A
volume
wds:Q28576517-4260667C-A4EB-4482-82E8-40CB9EC0EE98
issue
6775
volume
404
DOI
wds:Q28576517-14E1C124-2B08-4457-9221-874CDD206914
DOI
http://dx.doi.org/10.1038/35005118
DOI
10.1038/35005118
Springer Nature article ID
wds:Q28576517-E87F0C41-D29C-4815-B5FD-EE8B57DBAFFB
Dimensions Publication ID
wds:Q28576517-7313478D-14CE-4AA6-B979-C7BF010F0A54
Springer Nature article ID
10.1038/35005118
Dimensions Publication ID
1003313867
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about
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https://www.wikidata.org/wiki/Special:EntityData/Q28576517
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cites work
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Molecular mechanisms of glioma cell migration and invasion
Glutamate receptor ion channels: structure, regulation, and function
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