anti-F-Box Protein 2 (FBXO2) Antibodies

Human F-Box Protein 2 (FBXO2) interaction partners

1. Fbs1 GYR variant may be employed for substantially unbiased enrichment of N-linked glycopeptides from human serum

2. These results suggest that the FBXO2 variant rs9614 C allele may decrease the Parkinson Disease risk in mainland Han Chinese and may be a biomarker for PD.

3. summary, our findings suggest that FBXO2-regulated EMT led to carcinogenicity in gastric cancer and may be a novel target in the diagnosis and treatment of gastric cancer.

4. Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase has been presented.

5. This study provides new knowledge of the CFTR biosynthetic pathway. It suggests that SYVN1 and FBXO2 represent two distinct multiprotein complexes that may degrade DeltaF508-CFTR in airway epithelia and identifies a new role for NEDD8 in regulating DeltaF508-CFTR ubiquitination.

6. Although the overall structure of FBG3 is similar to that of Fbs1, the residues that form the Fbs1 carbohydrate-binding pocket failed to be superposed with the corresponding residues of FBG3.

7. FBG1 degrades A1AT-Z through a Beclin1-dependent arm of autophagy.

8. FBG1 is unique among known F-box proteins in that it contains a non-canonical D-Box within F-box domain, required for the growth arrest.

9. interaction of the HSV-1 UL9 protein with NFB42 results in its polyubiquitination and subsequent degradation by the 26S proteasome

Mouse (Murine) F-Box Protein 2 (FBXO2) interaction partners

1. F-box only protein 2 (FBXO2), a substrate recognition component of the Skp1-Cul1-F-box protein (SCF) E3 ubiquitin ligase complex, was upregulated in livers of obese mice. Furthermore, using a protein purification approach combined with high-performance liquid chromatography/tandem mass spectrometry, we carried out a system-wide screening of FBXO2 substrates, in which the insulin receptor (IR) was identified as a substrate

2. FBG1 degrades A1AT-Z through a Beclin1-dependent arm of autophagy.

3. The results of this study suggested that Fbxo2 controls the abundance and localization of specific NMDAR subunits in the brain and may influence synapse formation and maintenance.

4. these results suggest that Fbxo2 regulates APP levels and processing in the brain and may play a role in modulating Alzheimer disease pathogenesis.

5. our studies support a non-essential role for FBG1 on the degradation of torsinA and uncover a novel link of FBG1 to the autophagy pathway.

6. When expressed in hippocampal neurons, the Fbx2 dominant-negative mutant augmented NR1 subunit levels and NMDA receptor-mediated currents in an activity-dependent fashion

7. Fbs1 assists clearance of aberrant glycoproteins in neuronal cells by suppressing aggregates formation, independent of ubiquitin ligase activity, and thus functions as a unique chaperone for those proteins.

8. Our findings demonstrate that components of protein quality control are essential for inner ear homeostasis and implicate Fbx2 and Skp1 as potential genetic modifiers in age-related hearing loss.