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Hiroshi Morioka

Researcher at Kumamoto University

Publications -  102
Citations -  3079

Hiroshi Morioka is an academic researcher from Kumamoto University. The author has contributed to research in topics: Ribonuclease T1 & Binding site. The author has an hindex of 25, co-authored 99 publications receiving 2860 citations. Previous affiliations of Hiroshi Morioka include National Institute of Advanced Industrial Science and Technology & Hokkaido University.

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Immunodominant SARS Coronavirus Epitopes in Humans Elicited both Enhancing and Neutralizing Effects on Infection in Non-human Primates

TL;DR: Peptide-based vaccines against SARS-CoV could be engineered to avoid ADE via elimination of the S597–603 epitope, an alternative strategy to prepare a safe and effective vaccine for ADE of viral infection by identifying and eliminating epitope sequence-dependent enhancement of viral infections.
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Structural basis for recruitment of human flap endonuclease 1 to PCNA.

TL;DR: The structure involving the full‐length enzyme has revealed additional interfaces that are involved in the core domain that maintain the enzyme in an inactive 'locked‐down' orientation and might be utilized in rapid DNA‐tracking by preserving the central hole of PCNA for sliding along the DNA.
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DDB Accumulates at DNA Damage Sites Immediately after UV Irradiation and Directly Stimulates Nucleotide Excision Repair

TL;DR: It is shown that with a highly defined system of purified repair factors, DDB can greatly stimulate the excision reaction reconstituted with XPA, RPA, XPC·HR23B, TFIIH, XPF·ERCC1 and XPG, up to 17-fold for CPDs and ∼2- fold for ( 6-4) photoproducts (6-4PPs), indicating that no additional factor is required for the stimulation by D
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Tryptophan H33 plays an important role in pyrimidine (6–4) pyrimidone photoproduct binding by a high-affinity antibody

TL;DR: In this article, the importance of Trp H33 in antibody recognition of DNA containing a central pyrimidine (6-4) pyrimidone photoproduct was investigated.
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Structure-Function Relationship of the Eukaryotic DNA Replication Factor, Proliferating Cell Nuclear Antigen

TL;DR: The functional domains of human PCNA required for stimulation of replication factor C (RF-C) ATPase and DNA synthesis by pol δ are studied, suggesting that short deletions from either the N or C termini caused drastic changes in extraction and chromatographic behaviors.