Cang Wu

ORCID: 0000-0002-6218-8569
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Growth Hormone and Insulin-like Growth Factors
  • RNA and protein synthesis mechanisms
  • Drug Transport and Resistance Mechanisms
  • Signaling Pathways in Disease
  • RNA Research and Splicing
  • Cancer, Hypoxia, and Metabolism
  • Photosynthetic Processes and Mechanisms
  • CRISPR and Genetic Engineering
  • Electron and X-Ray Spectroscopy Techniques
  • Trace Elements in Health
  • Cellular transport and secretion
  • RNA Interference and Gene Delivery
  • RNA regulation and disease
  • Connective tissue disorders research
  • Cell Adhesion Molecules Research
  • Advanced Electron Microscopy Techniques and Applications
  • Cellular Mechanics and Interactions
  • Ion channel regulation and function
  • Thyroid Disorders and Treatments
  • Monoclonal and Polyclonal Antibodies Research
  • Enzyme Structure and Function
  • Cardiac electrophysiology and arrhythmias
  • RNA modifications and cancer
  • Metabolism, Diabetes, and Cancer

Southern University of Science and Technology
2022-2025

Shenzhen Second People's Hospital
2022

Abstract Cryo-electron microscopy (cryo-EM) visualizes the atomic structure of macromolecules that are embedded in vitrified thin ice at their close-to-native state. However, homogeneity thickness, a key factor to ensure high image quality, is poorly controlled during specimen preparation and has become one main challenges for high-resolution cryo-EM. Here we found uniformity relies on surface flatness supporting film, developed method use ultraflat graphene (UFG) as support cryo-EM achieve...

10.1038/s41592-022-01693-y article EN cc-by Nature Methods 2022-12-15

Abstract Alpha-fetoprotein (AFP), a serum glycoprotein, is expressed during embryonic development and the pathogenesis of liver cancer. It serves as clinical tumor marker, function carcinogen, immune suppressor, transport vehicle; but detailed AFP structural information has not yet been reported. In this study, we used single-particle cryo-electron microscopy(cryo-EM) to analyze structure recombinant obtained 3.31 Å cryo-EM built an atomic model AFP. We observed identified certain features...

10.1038/s42003-024-06219-0 article EN cc-by Communications Biology 2024-04-27

Adenosine deaminase acting on RNA (ADAR) proteins, which mediate adenosine-to-inosine editing of double-stranded ribonucleic acid (dsRNA) substrates, play essential roles in balancing innate immunity. Using cryogenic electron microscopy, we solved the structure Caenorhabditis elegans ADR-2-ADBP-1 complex (stoichiometric ratio, 2:2), is an asymmetric ADR-2 dimer with one site blocked by other ADR-2. Unexpectedly, dsRNA recruitment triggered dissociation dimer, exposing more competent sites....

10.1093/nar/gkaf148 article EN cc-by-nc Nucleic Acids Research 2025-02-27

Abstract Secretory-pathway Ca 2+ -ATPases (SPCAs) play critical roles in maintaining homeostasis, but the exact mechanism of SPCAs-mediated transport remains unclear. Here, we determined six cryo-electron microscopy (cryo-EM) structures human SPCA1 (hSPCA1) a series intermediate states, revealing near-complete conformational cycle. With aid molecular dynamics simulations, these offer clear structural basis for entry and release hSPCA1. We found that hSPCA1 undergoes unique changes during ATP...

10.1038/s41422-023-00827-x article EN cc-by Cell Research 2023-05-31

Abstract Human multidrug resistance protein 5 (hMRP5) effluxes anticancer and antivirus drugs, driving resistance. To uncover the mechanism of hMRP5, we determine six distinct cryo-EM structures, revealing an autoinhibitory N-terminal peptide that must dissociate to permit subsequent substrate recruitment. Guided by these molecular insights, design inhibitory could block entry into transport pathway. We also identify a regulatory motif, comprising positively charged cluster hydrophobic...

10.1038/s41467-024-49204-1 article EN cc-by Nature Communications 2024-06-06

Calcium/calmodulin‐dependent serine protein kinase (CASK) interaction 1/2 (Caskin1/2) is essential neuronal synaptic scaffold in nervous system development. Knockouts of Caskin1/2 display severe deficits novelty recognition and spatial memory. The tandem sterile alpha motif (SAM) domains Caskin1/2, also conserved their Drosophila homolog Ckn, are known to form homopolymers, yet dynamic regulation mechanism remains unclear. In this study, SAM SH3 domain‐containing 1 (SASH1) was first...

10.1111/febs.17354 article EN FEBS Journal 2024-12-17

10.1016/j.bbrc.2022.05.063 article EN Biochemical and Biophysical Research Communications 2022-05-20
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