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Cow (Bovine) Monoclonal ARF1 Primary Antibody for ICC, FACS - ABIN152664
Lu, Horstmann, Ng, Hong: Regulation of Golgi structure and function by ARF-like protein 1 (Arl1). in Journal of cell science 2002
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Arabidopsis thaliana Polyclonal ARF1 Primary Antibody for IF, WB - ABIN2688655
Pimpl, Movafeghi, Coughlan, Denecke, Hillmer, Robinson: In situ localization and in vitro induction of plant COPI-coated vesicles. in The Plant cell 2001
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Dog (Canine) Polyclonal ARF1 Primary Antibody for ELISA, WB - ABIN547815
Dubois, Paléotti, Mironov, Fraisier, Stradal, De Matteis, Franco, Chavrier: Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. in Nature cell biology 2005
ARF1 activation status is altered at cold temperatures. Activated ARF1 can prevent cold-induced dispersal of golgin-160.
Coincident with the loss of PICK1 by GBF1-activated ARF1, CDC42 recruitment leads to the activation of IRSp53 and the ARP2/3 complex, resulting in a burst of F-actin polymerisation potentially powering scission.
This study suggests that simultaneous blockade of Arf1 and Ras activation in prostate cancer cells is a potential targeted therapeutic strategy for preventing prostate cancer development.
Silencing of ARF1 impaired RAC1 recruitment to leading edge in neutrophil chemotaxis.
Data show that only ADP-ribosylation factor 1 (ARF1) promoter hypermethylation was significantly associated with epidermal growth factor receptor gene (EGFR) gene amplification in glioblastoma.
The zebrafish-metastasis model confirms that the ARF1 gene depletion suppresses breast cancer cells to metastatic disseminate throughout fish body.
ARF1 is a critical regulator in prostate cancer progression
our findings demonstrate that ARF1 is a molecular switch for cancer progression and thus suggest that limiting the expression/activation of this GTPase could help improve outcome for breast cancer patients.
changes in distinct lipid ratios may converge on ARF1 to increase SBP-1/SREBP-1 activity.
Experiments using a mutant form of ARF1 affecting GTP hydrolysis suggest that ARF1[GTP] is functionally required for the tubules to form.
ARNO-ARF1 regulates formation of podosomes by inhibition of RhoA/myosin-II and promotion of actin core assembly.
Activation of ARF1 dissociates ADRP from lipid droplets. A constitute active form of ARF1 (ARF1Q71I) promotes HCV assembly. ADRP played a positive role in Hepatitis C virus replication and negative role in Hepatitis C virus assembly.
ARF1 may reverse CAM-DR by regulating phosphorylation of p27 at T157 in MM. our data shed new light on the molecular mechanism of CAM-DR in MM, and targeting ARF1 may be a novel therapeutic approach for improving the effectiveness of chemotherapy in MM.
We report here that 2-methylcoprophilinamide (M-COPA), a compound that induces disassembly of the Golgi apparatus by inactivating ADP-ribosylation factor 1 (Arf1), suppresses Stx-induced apoptosis. M-COPA inhibited transport of Stx from the plasma membrane to the Golgi apparatus and suppressed degradation of anti-apoptotic proteins and the activation of caspases
observations indicate that Arf1 and Arf3 as well as Arf6 play important roles in cytokinesis.
ARF1 activates the MAPK pathway likely using the Golgi as a main platform, which in turn activates the cytoplasmic RSK1, leading to cell proliferation.
Data indicate that ADP-ribosylation factor 1 (Arf1) colocalizes with chromogranin A and regulates secretion of insulin like growth factor 1 (IGF-1) and is required for anchorage dependent growth.
this study reports the cryo-electron microscopy structures of the Nef- and Arf1-bound AP-1 trimer in the active and inactive states.
Suggest a model in which Arf1/COPI machinery acts to control endoplasmic reticulum-lipid droplet connections for localization of key enzymes of triglyceride storage and catabolism.
ARF1 regulates cellularmigration of highly invasive triple-negative breast cancer cells, through the regulation of the focal adhesions complex.
results suggest that the peptide derived from ARF1 could be developed into a novel anti-allergic agent for therapeutic intervention in allergy and mast cell-related pathologies.
The authors found that Arf1 occupies contrasting molecular environments within the Coat Protein Complex I, leading them to hypothesize that some Arf1 molecules may regulate vesicle assembly while others regulate coat disassembly.
ARF1 may be a plausible inter-player that mediates the transition to osteoclast fusion at multiple steps during osteoclast differentiation.
Increased gene dosage of Ink4a, Arf1 and p53 delays age-associated central nervous system functional decline.
ARF1/TBCE-mediated cross-talk that coordinates COPI formation and tubulin polymerization at the Golgi.
These data establish for the first time that the Arf1 gene is indispensable for mouse embryonic development after implantation.
Arf modulates LRP6 phosphorylation for the transduction of Wnt/beta-catenin signaling.
Down-regulation of ADP-ribosylation factor results in corneal neovascularization regression.
ARF1-dependent trafficking of procathepsin B and the maturation of autophagosomes results in cathepsin B-mediated trypsinogen activation induced by caerulein.
Egr1 mediates p53-independent c-Myc-induced apoptosis via a noncanonical ARF-dependent transcriptional mechanism
A senescence rescue screen identifies BCL6 as an inhibitor of anti-proliferative p19(ARF)-p53 signaling
termination of Arf1 signals mediated through GGA require that Arf1.GTP dissociates from GGA prior to interaction with GAP and consequent hydrolysis of GTP
GDP-bound ARF1 induces dissociation of ADRP from the Lipid droplet surface.
The recruitment of certain adhesion components such as paxillin requires dynamic GTP/GDP turnover of Arf1 GTPase.
The crystal structure of the activated GTP-bound form of ARF1 in a complex with the Arf-binding domain (ArfBD) of ARHGAP21 at 2.1 A resolution, is presented.
ARF1 plays an essential role in regulating asymmetric cell division in female meiosis.
findings reveal a novel signalling pathway involved in development of the semicircular canal system, and suggest a previously unrecognized role for NCS-1 in mitochondrial function via its association with several mitochondrial proteins.
Vascular endothelial growth factor receptor-2 activates ADP-ribosylation factor 1 to promote endothelial nitric-oxide synthase activation and nitric oxide release from endothelial cells
Data show that AP-1 recruitment to the cell membrane was found to be dependent on myristoylated ADP-ribosylation factor (ARF1), GTP or nonhydrolyzable GTP-analogs, tyrosine signals, and small amounts of phosphoinositides.
NCS-1-ARF1 interaction provides evidence for functional cross-talk between Ca(2+)-dependent and ARF-dependent pathways in TGN to plasma membrane traffic
The ARF1 machinery also might produce movement- and fission-promoting forces through actin polymerization.
Binding of cargo signal peptides to AP-1 induces a conformational change in its core domain that greatly enhances its interaction with Arf-1-GTP.
Study shows that ARF DNA-binding domains ahomodimerize to generate cooperative DNA binding, which is critical for in vivo ARF5/MP function. Strikingly, DNA-contacting residues are conserved between ARFs, and found that monomers have the same intrinsic specificity; ARF1 and ARF5 homodimers, however, differ in spacing tolerated between binding sites.
Data indicate that ArfGAP domain8 (AGD8) and ARF-GAP domain 9 (AGD9), are involved in the recruitment of Arf1-GDP to the Golgi apparatus .
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2 and ARF3), class II (ARF4 and ARF5) and class III (ARF6), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.
ADP-ribosylation factor 1
, adp-ribosylation factor 1