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  1. Article

    Open Access

    Insights into the dual nature of αB-crystallin chaperone activity from the p.P39L mutant at the N-terminal region

    The substitution of leucine to proline at position 39 (p.P39L) in human αB-crystallin (αB-Cry) has been associated with conflicting interpretations of pathogenicity in cataracts and cardiomyopathy. This study ...

    Anis Barati, Leila Rezaei Somee, Mohammad Bagher Shahsavani in Scientific Reports (2024)

  2. No Access

    Article

    Fibril formation from the amyloid-β peptide is governed by a dynamic equilibrium involving association and dissociation of the monomer

    Here I review the molecular mechanisms by which water-soluble monomeric amyloid-β (Aβ) peptides are transformed into well-organized supramolecular complexes called amyloid fibrils. The mechanism of amyloid for...

    Masaru Hoshino in Biophysical Reviews (2017)

  3. Article

    Open Access

    The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates

    Ubiquitin is known to be one of the most soluble and stably folded intracellular proteins, but it is often found in inclusion bodies associated with various diseases including neurodegenerative disorders and c...

    Daichi Morimoto, Erik Walinda, Harumi Fukada, Yu-Shin Sou in Nature Communications (2015)

  4. Article

    Open Access

    Effects of macromolecular crowding on intracellular diffusion from a single particle perspective

    Compared to biochemical reactions taking place in relatively well-defined aqueous solutions in vitro, the corresponding reactions happening in vivo occur in extremely complex environments containing only 60–70...

    Damien Hall, Masaru Hoshino in Biophysical Reviews (2010)

  5. No Access

    Article

    Map** the core of the β2-microglobulin amyloid fibril by H/D exchange

    Despite numerous efforts, the lack of detailed structural information on amyloid fibrils has hindered clarification of the mechanism of their formation. Here, we describe a novel procedure for characterizing t...

    Masaru Hoshino, Hidenori Katou, Yoshihisa Hagihara in Nature Structural Biology (2002)

  6. No Access

    Article

    Structural and kinetic characterization of early folding events in β-lactoglobulin

    We have defined the structural and dynamic properties of an early folding intermediate of β-lactoglobulin known to contain non-native α-helical structure. The folding of β-lactoglobulin was monitored over the ...

    Kazuo Kuwata, Ramachandra Shastry, Hong Cheng, Masaru Hoshino in Nature Structural Biology (2001)

  7. No Access

    Chapter

    Wireless Image Transmit Unit and High Speed Inspection System for Inner Side of Container

    The Wireless Image Transmit (WIT) unit is the device to transmit plural video image data through closed pairs of special loop antennas shielded against electromagnetic wave.

    Masaru Hoshino in Developments in Food Engineering (1994)