AMFR antibody
- Known as:
- AMFR (anti-)
- Catalog number:
- orb100348
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- AMFR antibody
Related genes to: AMFR antibody
- Gene:
- AMFR NIH gene
- Name:
- autocrine motility factor receptor
- Previous symbol:
- -
- Synonyms:
- RNF45, gp78
- Chromosome:
- 16q13
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-10
- Date modifiied:
- 2017-12-06
Related products to: AMFR antibody
Related articles to: AMFR antibody
- Additive manufacturing by Fused Filament Fabrication (FFF) enables the fabrication of complex polymer components, although limitations in surface quality and dimensional accuracy often require post-processing. Abrasive water jet machining (AWJM) is a non-thermal technique suitable for improving surface integrity in polymers and composites without inducing thermal damage. This study investigates the AWJM performance on FFF-printed polylactic acid (PLA) and carbon-fiber-reinforced PLA (PLA-CF), focusing on the influence of water pressure (WP), traverse feed rate (TFR), and abrasive mass flow rate (AMFR). A full factorial design was implemented, and surface integrity was evaluated through surface roughness (Ra) and kerf taper (T), considering their variation across characteristic cutting regions: initial damage region (IDR), smooth cutting region (SCR), and rough cutting region (RCR). Results show that WP and TFR are the dominant parameters, while AMFR has a limited effect within the studied range. The SCR exhibits the lowest roughness, whereas the RCR shows significant degradation due to energy loss. Both materials present similar behavior, with only minor improvements in PLA-CF. ANOVA confirms that process parameters have a stronger influence than material type, providing useful criteria for AWJM optimization in FFF polymers. - Source: PubMed
Publication date: 2026/05/15
Mayuet Ares Pedro FRodríguez-Parada Lucíade la Rosa SergioBatista Moises - - Source: PubMed
Publication date: 2026/04/15
Feng TianliSu YulingZhou ChunleiZhang XinxinLiu JiabinZhang WenliHe JingHuang Xinjiang - Accurate delineation of crop growth stages under real-world field conditions remains a long-standing challenge in computational phenotyping, particularly for wheat whose developmental phases are characterized by subtle, continuous morphological transitions and environmental noise. In this study, we propose AMFR-Net, an Adaptive Multi-Scale Feature Refinement Network tailored for fine-grained wheat stage identification using ground-level RGB imagery. Unlike conventional architectures that struggle with ambiguous inter-stage boundaries and rigid receptive structures, AMFR-Net leverages a ResNet-101 backbone augmented by a novel Adaptive Multi-Scale Attention Fusion (AMSAF) module-comprising cross-scale interaction blocks and confidence-weighted feature aggregation-to hierarchically recalibrate spatial-semantic representations. This design enables the network to adaptively amplify phenologically salient cues while suppressing irrelevant context, ensuring robust generalization under constrained annotation and deployment conditions. Evaluated on the expert-labeled CGIAR benchmark, AMFR-Net achieves state-of-the-art performance across all major metrics (Top-1 Accuracy: 89.10%; Macro-F1: 89.10%; AUC: 97.88%) and demonstrates superior discriminability in phenologically adjacent stages compared to lightweight and deep CNN baselines. Ablation studies validate the synergistic effect of multi-level attention and scale-aware refinement. The proposed framework offers a scalable, interpretable, and field-deployable solution for phenology monitoring, and sets a foundation for future integration of multimodal sensing, weak supervision, and cross-seasonal adaptation. - Source: PubMed
Publication date: 2026/03/19
Sun HaifangHou LiangGuo XiaoruiWang YananMin JiananZheng XiaoliuTian ZhehaoZhang DonghuiZhang XinshiLiu SenhaoGao YuAn ZhaoliQi HaoLv Liangjie - In PINK1 (PTEN induced kinase 1)/PRKN (Parkin)-mediated mitophagy, the rupture of the outer mitochondrial membrane (OMM) emerges as a crucial event required for efficient mitochondrial clearance. Mechanistically, OMM rupture exposes inner mitochondrial membrane (IMM) mitophagy receptors, facilitating subsequent autophagic removal. Despite the important role of OMM rupture in mitophagy, the underlying mechanism remains elusive and technically difficult to monitor. In a recent study, we developed a novel fluorescent biosensor to directly visualize OMM rupture. This technique enables temporal and spatial characterization of OMM rupture and provides a powerful platform to dissect the underlying mechanism. Using this tool, we revealed that VCP (valosin containing protein) and its recruitment factors are required for OMM rupture, suggesting that VCP-dependent remodeling of the OMM proteome primes the rupture of OMM during mitophagy. : ARIH1, Ariadne RBR E3 ubiquitin protein Ligase 1; AMFR, autocrine motility factor receptor; ANKRD13A, ankyrin repeat domain-containing protein 13 A; FUNDC1, FUN14 domain containing 1; OA, oligomycin and antimycin; CID, chemical-induced dimerization; IMM, nner mitochondrial membrane; LC3, microtubule-associated protein 1 light chain 3; MUL1, mitochondrial E3 ubiquitin protein ligase 1; NIX, BCL2 interacting protein 3 like; OMM, outer mitochondrial membrane; UBXN1, ubiquitin regulatory X domain-containing protein 1; UBXN6, ubiquitin regulatory X domain-containing protein 6; VCP, valosin-containing protein; WIPI2, WD repeat domain phosphoinositide interacting protein 2. - Source: PubMed
Publication date: 2026/02/13
Chu Wei-HuaChiang Wei-Chung - Genetic mutations in retinol dehydrogenase 5 (RDH5) are associated with the inherited autosomal recessive retinal degeneration diseases, especially fundus albipunctatus (FA). Most of RDH5 mutants exhibit downregulation of RDH5 protein expression. However, the regulatory mechanism remains unclear. Here, we studied the metabolism of RDH5/L310delinsEV mutation, an indel mutation closely associated with the inherited FA disease. The half-life of RDH5/L310delinsEV was much less than RDH5/WT. Unlike RDH5/WT, which normally underwent degradation in autophagy-lysosomes, the RDH5/L310delinsEV reduced its location to the endoplasmic reticulum and was easy to be polyubiquitinated and degraded in the ubiquitin-proteasome pathway. Both RDH5/WT and RDH5/L310delinsEV interacted with autocrine motility factor receptor (AMFR), which is an E3 ligase on the endoplasmic reticulum. Overexpression of or knockdown of AMFR by siRNA increased or reduced the degradation of RDH5/L310delinsEV. The lysine 179 and lysine 263 of RDH5/L310delinsEV protein were polyubiquitination sites by AMFR. Mutation of K179R and K263R in RDH5/L310delinsEV protein reduced AMFR-mediated polyubiquitination and degradation. Taken together, these results highlight that RDH5/L310delinsEV mutant in RDH5 causes a rapid degradation in the ubiquitin-proteasome pathway. The fast degradation of RDH5/L310delinsEV may be associated with the FA development. - Source: PubMed
Publication date: 2026/02/10
Dong YichenXue RongZhang YiJia XiaolinJiang MingjunXue MengjiaoPeng XuyanWan GuangmingHu Yanzhong