Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–11 of 11 results
Advanced filters: Author: Tian-Min Fu Clear advanced filters

  • The Gabija system constitutes one of the most prevalent anti-phage defense systems and is composed of GajA and GajB. Here, using cryo-EM and biochemistry, the authors show that GajA and GajB form a supramolecular complex with a stoichiometry of 4:4 to promote anti-phage defense.

    • Xiao-Yuan Yang
    • Zhangfei Shen
    • Tian-Min Fu
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 1243-1250

  • Using cryo-electron microscopy the authors show that PtuA, an ATPase, and PtuB, a nuclease, assemble into a supramolecular complex with a stoichiometry of 6:2 for anti-phage defense in bacteria. Nucleoside triphosphates inhibit PtuAB activity while phage infection activates PtuAB to cleave phage genome for immune defense.

    • Yuanyuan Li
    • Zhangfei Shen
    • Yamei Yu
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 413-423

  • Cryo-electron microscopy structures and biochemical analyses provide insight into how short prokaryotic Argonaute proteins are assembled and activated, and reveal that oligomerization has a key role in driving catalytic activity.

    • Zhangfei Shen
    • Xiao-Yuan Yang
    • Tian-Min Fu
    Research
    Nature
    Volume: 621, P: 154-161

  • Combining structural, biochemical, and cellular evidence, the authors elucidate the self-recognition mechanism of a neuronal receptor sDSCAM and provide insights into the evolutionary landscape of the cell recognition molecule diversity.

    • Jie Cheng
    • Yamei Yu
    • Qiang Chen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • Craspase is newly identified type III CRISPR–Cas system with two major components: the nuclease Cas7-11, and the protease TPR-CHAT. Craspases perform a delicate balancing act between nuclease and protease activity to achieve immune tolerance and defense in bacteria, and show promise as highly regulatable genome-editing tools.

    • Anthony D. Rish
    • Tian-Min Fu
    News & Views
    Nature Structural & Molecular Biology
    Volume: 30, P: 126-128

  • Pathogen triggered N-terminal degradation of NLRP1 and CARD8 by the proteasome releases their C-terminal UPA-CARD fragments (CT) to form the inflammasome, which in turn activates caspase-1. Here, the authors present the cryo-EM structures of the NLRP1-CT and CARD8-CT helical filaments as well as the ASC−caspase-1 octamer structure, which together with in vitro and cell based assays provide further insights into the architecture and specificity of the active NLRP1 and CARD8 inflammasomes.

    • L. Robert Hollingsworth
    • Liron David
    • Hao Wu
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13