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Nozomu Koizumi

Researcher at Osaka Prefecture University

Publications -  107
Citations -  5585

Nozomu Koizumi is an academic researcher from Osaka Prefecture University. The author has contributed to research in topics: Unfolded protein response & Endoplasmic reticulum. The author has an hindex of 40, co-authored 103 publications receiving 5073 citations. Previous affiliations of Nozomu Koizumi include National Archives and Records Administration & Kyoto University.

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Periodic DNA Methylation in Maize Nucleosomes and Demethylation by Environmental Stress

TL;DR: When maize seedlings were exposed to cold stress, a genome-wide demethylation occurred in root tissues, and one particular fragment, designated ZmMI1, contained part of the coding region of a putative protein and part of a retrotransposon-like sequence.
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An Arabidopsis transcription factor, AtbZIP60, regulates the endoplasmic reticulum stress response in a manner unique to plants.

TL;DR: Analysis of transcripts of 75 genes encoding putative basic leucine zipper ( bZIP) transcription factors in the Arabidopsis genome identified AtbZIP60, which was induced by tunicamycin, suggesting a signal transduction pathway of the ER stress response unique to plants.
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Arabidopsis IRE1 catalyses unconventional splicing of bZIP60 mRNA to produce the active transcription factor

TL;DR: It is demonstrated that bZip60 mRNA is spliced by ER stress, removing 23 ribonucleotides and therefore causing a frameshift that replaces the C-terminal region of bZIP60 including the transmembrane domain (TMD) with a shorter region without a TMD.
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Arabidopsis bZIP60 Is a Proteolysis-Activated Transcription Factor Involved in the Endoplasmic Reticulum Stress Response

TL;DR: It is reported here that bZIP60, an Arabidopsis thaliana basic leucine zipper (bZIP) transcription factor with a transmembrane domain, is involved in the ER stress response.
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Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum-located transmembrane protein kinases.

TL;DR: Functional complementation of the sensor domains of the two proteins in yeast and show that the Ire1-2 protein is capable of autotransphosphorylation are demonstrated in relation to the involvement of these genes in unfolded protein response signaling in plants.