A5087768419- DNA Repair Mechanisms
- Invertebrate Immune Response Mechanisms
- DNA and Nucleic Acid Chemistry
- Advanced Electron Microscopy Techniques and Applications
- Aquaculture disease management and microbiota
- RNA modifications and cancer
- Insect symbiosis and bacterial influences
- Whipple's Disease and Interleukins
- Cellular transport and secretion
- Neurobiology and Insect Physiology Research
- CRISPR and Genetic Engineering
- Computational Drug Discovery Methods
- Aquaculture Nutrition and Growth
- Biotin and Related Studies
- Vibrio bacteria research studies
- Vector-Borne Animal Diseases
- Protein Kinase Regulation and GTPase Signaling
- Studies on Chitinases and Chitosanases
- PARP inhibition in cancer therapy
- Echinoderm biology and ecology
- Advanced biosensing and bioanalysis techniques
- PI3K/AKT/mTOR signaling in cancer
- Monoclonal and Polyclonal Antibodies Research
- Click Chemistry and Applications
- Photosynthetic Processes and Mechanisms
Sun Yat-sen University
2017-2025
Sun Yat-sen Memorial Hospital
2024-2025
Guangdong Pharmaceutical University
2024
Peking University
2023
Sixth Affiliated Hospital of Sun Yat-sen University
2023
A comprehensive dataset detailing protein interactors for the PARP family has been generated using TurboID proximity labeling under standardized experimental conditions. V5-TurboID fusion constructs enabled identification of 6,314 high-confidence interacting proteins through mass spectrometry, capturing transient interactions undetectable by conventional methods. Parallel GFP-PARP localization experiments validated physiological subcellular distributions. The reveals both shared and unique...
MCM8 and MCM9 form a functional helicase complex (MCM8/9) that plays an essential role in DNA homologous recombination repair for double-strand break. However, the structural characterization of MCM8/9 binding/unwinding remains unclear. Here, we report structures using cryo-electron microscopy single particle analysis. The reveal is arranged into heterohexamer through threefold symmetry axis, creating central channel accommodates DNA. Multiple characteristic hairpins from N-terminal...
MCM8 and MCM9 form a functional helicase complex (MCM8/9) that plays an essential role in DNA homologous recombination repair for double-strand break. However, the structural characterization of MCM8/9 binding/unwinding remains unclear. Here, we report structures using cryo-electron microscopy single particle analysis. The reveal is arranged into heterohexamer through threefold symmetry axis, creating central channel accommodates DNA. Multiple characteristic hairpins from N-terminal...
MCM8 and MCM9 form a functional helicase complex (MCM8/9) that plays an essential role in DNA homologous recombination repair for double-strand break. However, the structural characterization of MCM8/9 binding/unwinding remains unclear. Here, we report structures using cryo-electron microscopy single particle analysis. The reveal is arranged through three-fold symmetry axis to heterohexamer with central channel accommodate DNA. Multiple characteristic hairpins from N-terminal...
<title>Abstract</title> Background The ribosome assembly factors PNO1 and NOB1 play crucial roles in the maturation of 40S ribosomal small subunit. TurboID is an efficient biotin ligase that can biotinylate proteins proximity to target protein widely used study complex biological processes within cells.Here, we utilized this technology investigate interaction network cells. Results Through immunofluorescence experiments, found have different localizations By identifying proximal biotinylated...
MCM8 and MCM9 form a functional helicase complex (MCM8/9) that plays an essential role in DNA homologous recombination repair for double-strand break. However, the structural characterization of MCM8/9 binding/unwinding remains unclear. Here, we report structures using cryo-electron microscopy single particle analysis. The reveal is arranged into heterohexamer through three-fold symmetry axis, creating central channel accommodates DNA. Multiple characteristic hairpins from N-terminal...
Abstract MCM8 and MCM9 form a functional helicase complex (MCM8/9) that plays an essential role in DNA homologous recombination repair for double-strand break. However, the structural characterization of MCM8/9 binding/unwinding remains unclear. Here, we report structures using cryo-electron microscopy single particle analysis. The reveal is arranged into heterohexamer through three-fold symmetry axis, creating central channel accommodates DNA. Multiple characteristic hairpins from...