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anti-Human NEDD4 Anticorps:
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Human Polyclonal NEDD4 Primary Antibody pour IHC (p), WB - ABIN4338483
Zhang, Li, Rezaeian, Xu, Chou, Jin, Han, Pan, Wang, Long, Zhang, Huang, Tsai, Tsai, Logothetis, Lin: H3 ubiquitination by NEDD4 regulates H3 acetylation and tumorigenesis. dans Nature communications 2017
Low HER3 expression is suggested to be a valuable prognostic biomarker to predict recurrence in HER2-amplified breast cancer.
Authors conclude that recruitment of alpha arrestins to membrane receptors and aggregation of unstable proteins after heat shock may be physiologically relevant mechanisms for triggering ubiquitination by Nedd4 family HECT domain-containing E3 ligases.
NEDD4 mediates the EGFR lung cancer cell migration signaling through promoting lysosomal secretion of cathepsin B.
Data indicate the mechanism for epigenetic regulation in cancer by inducing E3 ubiquitin ligase NEDD4-dependent histone H3 ubiquitination.
We further investigated whether curcumin exerts its antitumor activities via suppressing NEDD4 expression. We found that curcumin reduced the expression of NEDD4 and Notch1 and pAKT, leading to glioma cell growth inhibition, apoptosis, and suppression of migration and invasion. Moreover, deletion of NEDD4 expression enhanced the sensitivity of glioma cells to curcumin treatment
an oncogenic E3 ubiquitin ligase promotes loss of gap junctions and Cx43 degradation in human carcinoma cells.
NEDD4 exerts its oncogenic function partly due to regulation of PTEN and Notch-1 in bladder cancer cells.
In the present study, we identified that the adaptor protein Numb, which is demonstrated to be a novel binding partner of NEDD4-1, plays important roles in controlling PTEN ubiquitination through regulating NEDD4-1 activity and the association between PTEN and NEDD4-1.
NEDD4 is an autophagic E3 ubiquitin ligase that ubiquitylates SQSTM1, facilitating SQSTM1-mediated inclusion body autophagy.
NEDD4 is largely involved in epithelial-mesenchymal transition features and chemoresistance of nasopharyngeal carcinoma cancer cells.
NEDD4 ligase regulates RTP801 and is sensitive to Parkinson disease-associated oxidative stress
Two additional regulators of BST2 constitutive ubiquitylation and sorting to the lysosomes: the E3 ubiquitin ligases NEDD4 and MARCH8, are reported.
SQSTM1 is ubiquitinated by NEDD4 while LC3 functions as an activator of NEDD4 ligase activity.
Our results reveal a novel mechanism of upregulation of NEDD4 expression in pancreatic adenocarcinoma
Describe an autoinhibitory mechanism for NEDD4-1 ubiquitin ligase involving a linker-HECT domain interaction. This intramolecular interaction traps the HECT enzyme in its inactive state and can be relieved by linker phosphorylation.
Insights into links between autophagy and the ubiquitin system showed that LC3B-binding can steer intrinsic NEDD4 E3 ligase activity.
NEDD4-1 recognizes SERTA domain containing proline rich region of p34SEI-1. Residues of NEDD4-1 responsible for direct interaction with p34SEI-1 are identified by NMR titration experiments.
Our results demonstrate that NEDD4 may promote the acquired resistance of non-small-cell lung cancer cells to erlotinib by decreasing phosphatase and tensin homolog deleted on chromosome 10 protein expression. Targeted decrease in NEDD4 expression may be a potential therapeutic strategy for tyrosine kinase inhibitor-resistant non-small-cell lung cancer.
this is the first demonstration that Nedd4-1 regulates hOAT1 ubiquitination, expression, and transport activity through its WW2 and WW3 domains
both Nedd4-1 and Nedd4-2 are important regulators for hOAT1 ubiquitination, expression, and function
NEDD4 targets an RNA-binding protein, NANOS2, in spermatogonia to destabilize it, leading to cell differentiation. A NEDD4-mediated mechanism regulates mRNP dynamics, and facilitates spermatogonial progenitor cell homeostasis and viability under normal and stress conditions.
these findings support NEDD4 as a novel regulator of adipogenesis by modulating the stability of PPARgamma.
expression or dysfunction of Nedd4 E3 ligase could be involved in vascular calcification of VSMCs by activating bone-forming signals during atherosclerosis progression
Our data suggest that the behavioral sensitivity to stress is dramatically reduced in FXS, opening new views on the impact of gene-environment interactions in this pathology.
Nedd4-1 is required for efficient internalization of major growth factor receptors involved in liver regeneration and their downstream mitogenic signaling.
NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade.
these results suggest that Nedd4 suppresses colonic WNT signaling and tumor growth, at least in part, by suppressing the transcription factors LEF1 and YY1.
Findings indicate that reducing Nedd4 protein by 50% significantly impairs long-term potentiation and long-term memory thereby demonstrating an important role for Nedd4 in these processes.
Upregulation of long non-coding RNA PAPAS in response to hypoosmotic stress does not increase H4K20me3 because of Nedd4-dependent ubiquitinylation and proteasomal degradation of Suv4-20h2.
we propose that Nedd4 functions as a novel Pax7 regulator, which activity is temporally and spatially controlled to modulate the Pax7 protein levels and therefore satellite cell fate.
PDLIM7 is a bona fide skeletal muscle substrate of Nedd4-1.
show that absence of Nedd4 in pre-osteoblasts results in decreased cell proliferation and altered osteogenic differentiation
Nedd4 overexpression accelerates zebrafish embryonic growth through IRS-2 in vivo.
Nedd4 co-injection was found to have no affect on Gag- or Env-specific IFNgamma but had a trend of increased Gag-specific IL-6, IL-17A and TNFalpha that was not seen following Env stimulation.
NEDD4 is a previously unknown component of the CD40 signalling complex necessary for AKT activation.
Brucella infection inhibits macrophages apoptosis via Nedd4-dependent degradation of calpain2.
Data show that NEDD4-1 E3 ligase as a novel component of the tumor suppressor protein p53/proto-oncogene proteins c-mdm2 regulatory feedback loop that controls p53 activity during stress responses.
PTEN limits Nedd4-1 protein levels by modulating the activity of mTORC1, a protein complex that controls protein synthesis and cell growth.
Rsp5 and its mammalian homologue Nedd4 are important E3 ligases responsible for the increased ubiquitylation induced by heat stress.
This study is the first to show that a 50% reduction in Nedd4 levels is sufficient to produce significant gait defects in 6 month old mice
miR-1-mediated regulation of Nedd4/Nedd4L expression may serve to broadly modulate the trafficking or degradation of Nedd4/Nedd4L substrates in the heart
Nedd4Lo destabilizes Amph in muscles, leading to impaired T-tubule formation and muscle function.
NEDD4 controls the Hippo pathway leading to coordinated cell proliferation and apoptosis
data in two evolutionarily distant model organisms strongly suggest that Nedd4 is a modifier of alpha-synuclein pathobiology and thus a potential target for neuroprotective therapies
Nedd4, another E3 ubiquitin ligase that may have a role in PD, is functionally related to Sep4 and could be involved in regulating Sep4 subcellular localization/trafficking.
splice isoforms of the same dNedd4 gene can lead to opposite effects on neuromuscular synaptogenesis
Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation.
These studies provide insights into the specific regulation of dNedd4-mediated ubiquitination of Comm and subsequent internalization of Comm or the Comm/Roundabout complex, critical for CNS and muscle development.
dNedd4 and ubiquitination are required for Commissureless endocytosis and proper neuromuscular synaptogenesis.
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Involved in ubiquitination of ERBB4 intracellular domain E4ICD1 (PubMed:19193720). Predominantly involved in ubiquitination of membrane bound forms of ERBB4 rather than processed precursors and intermediate membrane-anchored 80 kDa fragments (m80HER4), with a lesser role in ubiquitination of ERBB4 intracellular domain E4ICD1 (PubMed:19047365). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (By similarity).
E3 ubiquitin-protein ligase NEDD4
, cell proliferation-inducing gene 53 protein
, neural precursor cell expressed developmentally down-regulated protein 4
, receptor-potentiating factor 1
, neural precursor cell expressed, developmentally down-regulated gene 4
, neural precursor cell expressed, developmentally down-regulated gene 4a
, neural precursor cell expressed, developmentally down-regulted gene 4
, neural precursor cell expressed, developmentally down-regulated 4
, ubiquitin-protein ligase Nedd4
, E3 ubiquitin-protein ligase NEDD4-like
, e3 ubiquitin-protein ligase NEDD4-like
, neural precursor cell expressed, developmentally down-regulated gene 4A