WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
about
Genetic detection and characterization of Lujo virus, a new hemorrhagic fever-associated arenavirus from southern AfricaNedd4-2 and the regulation of epithelial sodium transportRole of the UPS in Liddle syndromeRING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitinationHuman Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunitsInteraction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel)HECT E3 ubiquitin ligase Nedd4-1 ubiquitinates ACK and regulates epidermal growth factor (EGF)-induced degradation of EGF receptor and ACKRegulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite developmentNedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and functionInteractive cloning with the SH3 domain of N-src identifies a new brain specific ion channel protein, with homology to eag and cyclic nucleotide-gated channelsThe phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor proteinThe HECT ubiquitin ligase AIP4 regulates the cell surface expression of select TRP channelsTransport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitinationThe ubiquitin-protein ligase Nedd4-2 differentially interacts with and regulates members of the Tweety family of chloride ion channelsCD63 interacts with the carboxy terminus of the colonic H+-K+-ATPase to decrease [corrected] plasma membrane localization and 86Rb+ uptakeLatent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinasesWW domains provide a platform for the assembly of multiprotein networksIdentification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligandsRegulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination.A WW domain-containing yes-associated protein (YAP) is a novel transcriptional co-activator.Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expressionA new locus on chromosome 12p13.3 for pseudohypoaldosteronism type II, an autosomal dominant form of hypertensionProteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cellsSCF(β-TRCP)-mediated degradation of NEDD4 inhibits tumorigenesis through modulating the PTEN/Akt signaling pathwayThe ESCRT-associated protein Alix recruits the ubiquitin ligase Nedd4-1 to facilitate HIV-1 release through the LYPXnL L domain motifCalcium activates Nedd4 E3 ubiquitin ligases by releasing the C2 domain-mediated auto-inhibitionRegulation of p53 localization and transcription by the HECT domain E3 ligase WWP1Salt handling and hypertensionNedd4 controls animal growth by regulating IGF-1 signalingIdentification of human gene products containing Pro-Pro-x-Tyr (PY) motifs that enhance glutathione and endocytotic marker uptake in yeastA role for ubiquitin ligase recruitment in retrovirus releaseNedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cellsViral infection and human disease--insights from minimotifsFunctional and biochemical analysis of the C2 domains of synaptotagmin IVNedd4 mediates control of an epithelial Na+ channel in salivary duct cells by cytosolic Na+The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localizationNedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functionsCell surface expression of the epithelial Na channel and a mutant causing Liddle syndrome: a quantitative approachThe basic helix-loop-helix transcription factors dHAND and eHAND exhibit dimerization characteristics that suggest complex regulation of function
P2860
Q21089619-91323E43-D668-45C6-8205-76F76A18524AQ21129256-7DA8D4B3-6706-4D0B-95D2-C9DA8B7AAFC2Q21284380-E9EA2CDC-405C-4BD6-A801-ACD90C9A019DQ22010577-E7574E2A-0487-4394-8CA4-140143030C93Q22011107-EAD2BE35-234E-4783-8C7B-79890C6A4665Q24292192-47BEB837-FCA7-43FE-B074-7FE0FA927C92Q24296458-9F4E6174-0B1C-49D5-9850-7ED6AD3E33E6Q24299364-9405BA14-BD94-4C7E-B9D0-F06999A3CB4EQ24314826-B486EC79-295A-4D4A-84F6-6DD07BA74032Q24315270-323A4AAE-9DAA-4A5C-BDC3-8BA3309B22AEQ24315811-DF5D5394-7BDB-4B82-B9EC-FD7949E1E3EBQ24316916-49D944DA-0676-4220-9116-9A93BA27E4A8Q24318243-7D5DF462-FF89-476E-891B-79BADF1387C8Q24328849-A373EF86-75F1-44D7-B008-8E94CC8D1B64Q24337934-8BFF261F-1E2B-4619-A05E-5C5072876629Q24515076-24C44157-837A-4F4A-B2D5-31A4B8812179Q24529906-256AF2F2-DBB8-4010-8DD1-D5AACCA30484Q24532178-7F5C195E-8173-496E-B25A-75B371F06874Q24532189-54AD1770-A044-47E5-A1D1-DAA2BBBF2E1DQ24532806-A3CE1411-B6CF-42D5-95A0-5AEC094C7BAAQ24534123-A159A532-75E7-40F5-AD1C-13772F4EAF19Q24534668-6317AC2A-D1B9-4A24-BC51-B51C63B7EDA8Q24538746-53ADE7E0-EB43-470A-8CA5-8BD672479CB7Q24555190-56E5536E-C77C-4900-877D-15D8C1F894F3Q24567471-C0454AF5-C780-4045-9803-D56D0B908ED6Q24596374-FB1CA75D-C6DE-4B45-8FAB-C180E74928B8Q24598118-120BCC8C-80B1-4CEE-A231-CA203A44BC1EQ24630964-32CA4258-847C-45FF-B1CD-063E1694F577Q24631439-3954894E-E30B-4DC6-B24E-367685517221Q24632761-7FB29780-5588-4F85-A7B3-CCA12DFB409BQ24632870-B89A801E-55F4-42ED-8623-3005EDDC26FBQ24642874-136032B8-E413-413C-B324-86BA67F34062Q24644225-31FA3FD8-8C21-4C47-8490-29AEDB2C053BQ24647289-199B7AFC-C8E5-496E-977C-B292BD5CD449Q24647716-98739793-71B1-42C5-B76E-8E3DA55AE263Q24647839-5EB3B534-E3D5-4AEB-9FDE-150D2801CC86Q24650856-CB89811C-635F-404F-AC6F-E4019DE93ADEQ24651528-AB4C2360-8742-4F7A-8FC9-2F6D5F077830Q24653749-8DFA127C-6BA1-4EDD-BC9C-07EC13DC48E7Q24657772-9EBDC288-654A-4993-BABD-723EE86A938A
P2860
WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@ast
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@en
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@nl
type
label
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@ast
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@en
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@nl
prefLabel
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@ast
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@en
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@nl
P2093
P2860
P3181
P1433
P1476
WW domains of Nedd4 bind to th ...... l deleted in Liddle's syndrome
@en
P2093
T Ishikawa
P2860
P304
P3181
P356
10.1002/J.1460-2075.1996.TB00593.X
P407
P577
1996-05-01T00:00:00Z