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Yukio Ishimi

Researcher at Ibaraki University

Publications -  58
Citations -  3320

Yukio Ishimi is an academic researcher from Ibaraki University. The author has contributed to research in topics: DNA replication & Control of chromosome duplication. The author has an hindex of 27, co-authored 58 publications receiving 3201 citations. Previous affiliations of Yukio Ishimi include Mitsubishi & Gyeongsang National University.

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Journal ArticleDOI

A DNA Helicase Activity Is Associated with an MCM4, -6, and -7 Protein Complex *

TL;DR: Results suggest that this helicase may be involved in the initiation of DNA replication as a DNA unwinding enzyme.
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The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome.

TL;DR: The identification of a human multiprotein complex (WINAC) that directly interacts with the vitamin D receptor (VDR) through the Williams syndrome transcription factor (WSTF) suggests that WINAC dysfunction contributes to Williams syndrome, which could therefore be considered, at least in part, a chromatin-remodeling factor disease.
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Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis

TL;DR: The cloning of two human cDNAs encoding TAF-I is described, which revealed that the 39-kDa polypeptide corresponds to the protein encoded by the set gene, which is the part of the putative oncogene associated with acute undifferentiated leukemia when translocated to the can gene.
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Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro.

TL;DR: The amino acid sequence deduced from the gene coding for the yeast NAP-I defines a polypeptide of molecular mass 47,848 Da with three negatively charged regions that is probably involved in the interaction with histones.
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Human Cdc7-related Kinase Complex: IN VITRO PHOSPHORYLATION OF MCM BY CONCERTED ACTIONS OF Cdks AND Cdc7 AND THAT OF A CRITICAL THREONINE RESIDUE OF Cdc7 BY Cdks *

TL;DR: Replacement of Thr-376, corresponding to the activating threonine of Cdk, with alanine (T376A mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue.