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Publications by authors named "Mu-Ya Zhang"

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Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.
Li-Qiang Wang Yeyang Ma Mu-Ya Zhang Han-Ye Yuan Xiang-Ning Li

Sci Adv

November 2024

Article Synopsis
  • Over 200 genetic mutations in the SOD1 gene are associated with ALS, with two specific mutations (H46R and G85R) showing reduced metal ion binding.
  • Two cryo-electron microscopy structures of amyloid fibrils formed by these mutants reveal unique structural features, including a serpentine arrangement of β strands and specific interactions that stabilize the fibrils.
  • The mutant fibrils are more toxic and enhance the aggregation of normal SOD1, leading to mitochondrial dysfunction and cell death through ferroptosis, providing new insights into the molecular mechanisms behind ALS.
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Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion.
Li-Qiang Wang Yeyang Ma Han-Ye Yuan Kun Zhao Mu-Ya Zhang Delin Zhang

Nat Commun

June 2022

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease. Misfolded Cu, Zn-superoxide dismutase (SOD1) has been linked to both familial and sporadic ALS. SOD1 fibrils formed in vitro share toxic properties with ALS inclusions.

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Synopsis of recent research by authors named "Mu-Ya Zhang"

  • - Mu-Ya Zhang's research primarily focuses on the structural analysis of amyloid fibrils related to amyotrophic lateral sclerosis (ALS), particularly those formed by mutant variants of superoxide dismutase 1 (SOD1).
  • - Recent studies utilize advanced cryo-electron microscopy (cryo-EM) to elucidate the structures of amyloid fibrils associated with ALS-causing SOD1 mutations H46R and G85R, highlighting their reduced metal ion binding capacity.
  • - Findings indicate that the structural conformations of SOD1 fibrils are critical for understanding the toxic properties of misfolded proteins in ALS, contributing valuable insights into the mechanisms of this neurodegenerative disease.

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