Zhikun Liu

ORCID: 0009-0006-2037-2516
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About
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Research Areas
  • CRISPR and Genetic Engineering
  • Advanced biosensing and bioanalysis techniques
  • Genetics, Aging, and Longevity in Model Organisms
  • Trace Elements in Health
  • Ocular and Laser Science Research
  • Biochemical and Molecular Research
  • Plant Virus Research Studies
  • Advanced machining processes and optimization
  • Laser Material Processing Techniques
  • Viral Infections and Immunology Research
  • Amino Acid Enzymes and Metabolism
  • Radiopharmaceutical Chemistry and Applications
  • Laser-induced spectroscopy and plasma
  • Metal Alloys Wear and Properties
  • Advanced Surface Polishing Techniques
  • Innovation and Socioeconomic Development
  • Cytomegalovirus and herpesvirus research
  • Bacteriophages and microbial interactions
  • RNA and protein synthesis mechanisms

Tianjin Medical University
2024-2025

Hangzhou Medical College
2024

Zhejiang Provincial People's Hospital
2024

Shandong University
2002

University of Minho
2000

10.1016/j.bbrc.2025.151315 article EN Biochemical and Biophysical Research Communications 2025-01-09

10.1016/s0924-0136(02)00605-2 article EN Journal of Materials Processing Technology 2002-10-01

Cas9d, the smallest known member of Cas9 family, employs a compact domain architecture for effective target cleavage. However, underlying mechanism remains unclear. Here, we present cryo-EM structures Cas9d–sgRNA complex in both target-free and target-bound states. Biochemical assays elucidated PAM recognition DNA cleavage mechanisms Cas9d. Structural comparisons revealed that at least 17 base pairs guide–target heteroduplex is required nuclease activity. Beyond its typical role as an...

10.1038/s41467-025-57455-9 article EN cc-by-nc-nd Nature Communications 2025-03-12

Abstract Recently, a novel two-gene bacterial defense system against phages, encoding SIR2 NADase and HerA ATPase/helicase, has been identified. However, the molecular mechanism of SIR2–HerA immune remains unclear. Here, we determine cryo-EM structures SIR2, their complex from Paenibacillus sp. 453MF in different functional states. The proteins oligomerize into dodecameric ring-shaped structure consisting two layers interlocked hexamers, which each subunit exhibits an auto-inhibited...

10.1093/nar/gkae750 article EN cc-by-nc Nucleic Acids Research 2024-09-01

Abstract The Cas3 nuclease is utilized by canonical type I CRISPR-Cas systems for processive target DNA degradation, while a newly identified I-F CRISPR variant employs an HNH domain from the natural fusion Cas8-HNH protein precise cleavage both in vitro and human cells. Here, we report multiple cryo-electron microscopy structures of system at different functional states. Cascade complex adopts overall G-shaped architecture, with occupying C-terminal helical bundle (HB) Cas8 systems. Linker...

10.1038/s44318-024-00229-8 article EN cc-by The EMBO Journal 2024-09-09
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