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Hiroshi Mizuno

Researcher at National Institute of Advanced Industrial Science and Technology

Publications -  36
Citations -  851

Hiroshi Mizuno is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: HutP & Binding protein. The author has an hindex of 16, co-authored 36 publications receiving 812 citations. Previous affiliations of Hiroshi Mizuno include Meiji Pharmaceutical University & NEC Soft.

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Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers.

TL;DR: The overall structure reveals that the molecule is a novel cyclic tetramer made up of four alphabeta-heterodimers related by a crystallographic 4-fold symmetry, which could be explained by a cooperative-binding action through the multiple binding sites of the tetramer.
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Coagulation factor x-binding protein from deinagkistrodon acutus venom is a gla domain-binding protein

TL;DR: Results indicated that X-bp isolated from D. acutus venom was a GD-binding protein, and the C-terminal region of GD peptide was critical for folding of the peptide.
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Monitoring influenza hemagglutinin and glycan interactions using surface plasmon resonance.

TL;DR: The results showed that glycan-HA binding analyses can be performed reliably and efficiently on Biacore-chips in the SPR system, using chemically synthesized biotinylated multivalent-glycans, and suggested that this SPR-based method is suitable for influenza surveillance to define the pandemic scenario as well as to screen of synthetic glycans and other compounds that may interfere with glyCAN-HA interactions.
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Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain

TL;DR: The crystal structures of PsTx, Pdc and Zn2+-bound Pdc revealed that most of the amino-acid-residue differences between PsTx and Pdc are located around the concave surface formed between the PR-1 domain and the CRD, suggesting that the Concave surface is functionally important for CNG-channel binding and inhibition.
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Two forms of secreted and thermostable luciferases from the marine copepod crustacean, Metridia pacifica.

TL;DR: Continuous monitoring of secreted MpLuc1 driven by the c-fos promoter demonstrated the potential usefulness of Mp Luc1 in nondisruptive reporter assays.