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anti-Human AMFR Anticorps:
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Human Polyclonal AMFR Primary Antibody pour Func, IHC - ABIN4280243
Lucarelli, Galleggiante, Rutigliano, Sanguedolce, Cagiano, Bufo, Lastilla, Maiorano, Ribatti, Giglio, Serino, Vavallo, Bettocchi, Selvaggi, Battaglia, Ditonno: Metabolomic profile of glycolysis and the pentose phosphate pathway identifies the central role of glucose-6-phosphate dehydrogenase in clear cell-renal cell carcinoma. dans Oncotarget 2015
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Human Polyclonal AMFR Primary Antibody pour IHC - ABIN965545
Shimizu, Tani, Watanabe, Nagamachi, Niinaka, Shiroishi, Ohwada, Raz, Yokota: The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein. dans FEBS letters 1999
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Human Polyclonal AMFR Primary Antibody pour FACS, IHC (p) - ABIN388938
Huang, Xie, Raz: Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor. dans Biochemical and biophysical research communications 1995
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There was a significant correlation between the 145 locus of the gp89 gene and coronary atherosclerotic heart disease, indexes of blood fat, blood glucose and blood pressure.
This is the first study to show that HSPA1L mediated HIF-1alpha stabilization. In addition, this is the first study to show that GP78 inactivation promotes cancer cell proliferation, migration and eventual tumor growth both in vivo and in vitro by increasing cellular prion protein.
overexpression of gp78 or SVIP suppression may eliminate the toxic gain of function associated with polymerization of ZAAT, thus providing a potential new therapeutic approach to the treatment of alpha-1 antitrypsin deficiency
Despite its interaction with gp78, Lnp does not seem to have a broad function in degradation of misfolded ER proteins.
Further study discovered that the gp78 CUE domain works as a proofreading machine during the growth of K48-linked polyubiquitin chains to ensure the linkage specificity. Together, our studies uncover a novel mechanism underlying the linkage specificity determination of longer polyubiquitin chains.
AMFR expression is significantly reduced in plasma from osteoporosis patients.
Catalytic inactivation of MGRN1 results in elevated levels of GP78 and a consequential increase in the initiation of mitophagy.
Authors conclude that the Hrd1 complex forms an essential retrotranslocation module that is evolutionarily conserved, but the mammalian ERAD system uses additional ubiquitin ligases to assist Hrd1 during retrotranslocation.
Downregulation of AMFR induced cell cycle arrest at the G0/G1 phase, and increased apoptosis of the THP1 cells.
The authors identify USP13 as a gp78-associated deubiquitinase that eliminates ubiquitin conjugates from Ubl4A to maintain the functionality of Bag6.
Data show that autocrine motility factor receptor (AMFR) and NOTCH1 protein are the direct target genes of microRNA miR-139-5p in colorectal cancer (CRC).
gp78 elongates polyubiquitin chains from the distal end through the cooperation of its G2BR and CUE domains.
Our data uncovers a previously unknown functional link between gp78 and TRIM25 and provides mechanistic insight into gp78-mediated protein ubiquitylation.
The ubiquitin ligase gp78, known for its role in protein quality control, is critical for unglycosylated PrP ubiquitylation and degradation.
High AMFR expression is associated with invasion depth and lymph node metastasis in gastric cancer.
DGAT2 is regulated by gp78-associated endoplasmic-reticulum-associated degradation at the post-translational level.
gp78 is expressed specifically in human prostate cancer rather than normal prostate tissues, it could be a putative biomarker for prostate cancer diagnosis.
data thus implicate two parallel pathways by which Gp78 regulates MAVS signaling
gp78 is a ubiquitination machine where multiple E2-binding sites coordinately facilitate processive ubiquitination.
A novel role for the endoplasmic reticulum-associated Gp78 ubiquitin ligase and the Mfn1 mitochondrial fusion factor in mitophagy.
n the absence of both RNF145 and gp78, Hrd1, a third UBE2G2-dependent E3 ligase, partially regulates HMGCR activity. Our findings reveal a critical role for the sterol-responsive RNF145 in HMGCR regulation and elucidate the complexity of sterol-accelerated HMGCR degradation
the role of gp78 and cidec in hepatic steatosis, were investigated.
Gp78, an E3 ubiquitin ligase acts as a gatekeeper suppressing nonalcoholic steatohepatitis (NASH) and liver cancer.
role in innate immunity and STING signaling pathway
we consistently observe involvement of gp78 in Insig-1 degradation, we find no substantive evidence to support roles for either gp78 or TRC8 in the robust sterol-accelerated degradation of HMG-CoA reductase
Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis.
Palmitoylation of RING finger cysteines therefore regulates gp78 distribution to the peripheral ER
AMFR is involved in the process of learning and memory in the central nervous system.
KAI1 has a role in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase
Gp78 promotes SOD1 and ataxin-3 degradation in endoplasmic reticulum.
cytoplasmic protein mouse p97(mp97) participates in the formation of a ternary complex containing mouse autocrine motility factor receptor (mAMFR), mp97, and peptide N-glycanase
the receptor molecule for AMF/NLK/MF in leukemic differentiation is not gp78
Endoplasmic reticulum (ER) stress differentially regulates the stabilities of Endoplasmic reticulum associated degradation (ERAD)E3s and their substrates, which may represent a novel mechanism by which ER stress increases ERAD
gp78 promotes sarcoma metastasis by targeting KAI1 for degradation
revealed by small interfering RNA methods that the ubiquitin ligase RMA1 functioned as an E3 enzyme upstream of gp78
gp78 plays a critical role in protecting against ER stress in liver
This locus encodes a glycosylated transmembrane receptor. Its ligand, autocrine motility factor, is a tumor motility-stimulating protein secreted by tumor cells. The encoded receptor is also a member of the E3 ubiquitin ligase family of proteins. It catalyzes ubiquitination and endoplasmic reticulum-associated degradation of specific proteins.
E3 ubiquitin-protein ligase AMFR
, RING finger protein 45
, AMF receptor
, autocrine motility factor receptor
, autocrine motility factor receptor, amfr
, autocrine motility factor receptor amfr
, autocrine motility factor receptor, isoform 2-like