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Akademický článek

VPS4B orchestrates response to nuclear envelope stress by regulating ESCRT-III dynamics in glioblastoma

Autor: Zuqian Wu, Issei Omura, Atsushi Saito, Kazunori Imaizumi, Yasunao Kamikawa

Publikováno v: Nucleus, Vol 15, Iss 1 (2024)

The Nuclear envelope (NE) is frequently challenged by mechanical stimuli involving cells passing through a tight space and such stress is known as “NE stress.” Various factors that cooperate to repair the NE have been identified, including endoso

Externí odkaz: https://doaj.org/article/5646e51eb01b4945a82a489ed16c4ce6

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Converting cytochrome c into a DyP-like metalloenzyme

Autor: Koichiro Ishimori, Issei Omura, Takeshi Uchida

Publikováno v: Dalton Transactions. 51:12641-12649

Dye-decolorizing peroxidase (DyP), which can degrade anthraquinone dyes using H2O2, is an attractive prospect for potential biotechnological applications for environmental purification.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a126cd636f070fadfe3c5866a723a872
https://doi.org/10.1039/d2dt02137d

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Radical transfer but not heme distal residues is essential for pH dependence of dye-decolorizing activity of peroxidase from Vibrio cholerae

Autor: Issei Omura, Koichiro Ishimori, Sayaka Umetsu, Takeshi Uchida

Publikováno v: Journal of inorganic biochemistry. 219

Dye-decolorizing peroxidase (DyP) is a heme-containing enzyme that catalyzes the degradation of anthraquinone dyes. A main feature of DyP is the acidic optimal pH for dye-decolorizing activity. In this study, we constructed several mutant DyP enzymes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97d5c2d96bb3725a259e26cdef77585c
https://pubmed.ncbi.nlm.nih.gov/33756393

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