Noriko Yasuhara

ORCID: 0000-0003-2093-8840
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About
Contact & Profiles
Research Areas
  • Nuclear Structure and Function
  • RNA Research and Splicing
  • Genomics and Chromatin Dynamics
  • Cell death mechanisms and regulation
  • Pluripotent Stem Cells Research
  • Epigenetics and DNA Methylation
  • RNA Interference and Gene Delivery
  • Animal Genetics and Reproduction
  • RNA modifications and cancer
  • Trace Elements in Health
  • Cell Adhesion Molecules Research
  • Bacteriophages and microbial interactions
  • Diffusion and Search Dynamics
  • Cancer-related Molecular Pathways
  • Insect and Pesticide Research
  • Kruppel-like factors research
  • Nutrition, Genetics, and Disease
  • Cancer-related gene regulation
  • Circadian rhythm and melatonin
  • Wnt/β-catenin signaling in development and cancer
  • Protein Kinase Regulation and GTPase Signaling
  • Sarcoma Diagnosis and Treatment
  • Signaling Pathways in Disease
  • Virus-based gene therapy research
  • Renal and related cancers

Nihon University
2017-2025

Osaka University
2002-2016

National Institute of Biomedical Innovation, Health and Nutrition
2016

Ube Frontier University
2004-2014

Kanazawa University
2000

Significance The emergence of the cell-autonomous circadian oscillator is coupled with cellular differentiation. Cellular differentiation, as well reprogramming, results in global alterations transcriptional program via epigenetic modification such DNA methylation. We here demonstrate that c-Myc constitutive expression and Dnmt1 ablation disrupt differentiation-coupled clock from mouse ES cells (ESCs). Using these model ESCs, 484 genes were identified by gene analysis factors correlated...

10.1073/pnas.1419272111 article EN Proceedings of the National Academy of Sciences 2014-11-11

Background : Apoptosis is defined by chromatin condensation, nuclear fragmentation and the formation of apoptotic bodies. Because signals are transmitted through a common pathway that includes target steps death‐driving ICE‐family proteases anti‐cell death protein Bcl‐2 in cytoplasm, must be transferred from cytoplasm to nucleus, at least induce manifestation nucleus. Small signal molecules might diffuse across pores, but larger transported active mechanisms requiring ATP GTP hydrolysis. It...

10.1046/j.1365-2443.1997.1010302.x article EN Genes to Cells 1997-01-01

Upon activation, cell surface death receptors, Fas/APO-1/CD95 and tumor necrosis factor receptor-1 (TNFR-1), are attached to cytosolic adaptor proteins, which in turn recruit caspase-8 (MACH/FLICE/Mch5) activate the interleukin-1 β-converting enzyme (ICE)/CED-3 family protease (caspase) cascade. However, it remains unknown whether these apoptotic proteases generally involved apoptosis triggered by other stimuli such as Myc p53. In this study, we provide lines of evidence that a cascade...

10.1128/mcb.17.11.6736 article EN Molecular and Cellular Biology 1997-11-01

Snail contributes to the epithelial-mesenchymal transition by suppressing E-cadherin in transcription processes. The C2H2-type zinc-finger (ZF) domain functions both as a nuclear localization signal which binds importin β directly and DNA-binding domain. Here, 2.5 Å resolution structure of four ZF domains Snail1 complexed with is presented. X-ray reveals that ZFs are required for tight binding import Snail1. shape reminiscent round snail, where ZF1 represents head, ZF2-ZF4 shell, showing...

10.1107/s1399004714000972 article EN Acta Crystallographica Section D Biological Crystallography 2014-03-18

Transport of functional molecules across the nuclear membrane a eukaryotic cell is regulated by dedicated set transporter proteins that carry into nucleus or out to cytoplasm for homeostasis cell. One categories cargo these transporters are cycle regulation. Therefore, their role critical in terms cancer development. Any misregulation transport factors would means aberrant abundance regulators and might have consequences progression. While earlier studies focussed on individual related...

10.1016/j.heliyon.2021.e06039 article EN cc-by-nc-nd Heliyon 2021-01-01

Nuclear import of karyophilic proteins is carried out by a variety mechanisms. We previously showed that two basic helix-loop-helix proteins, NeuroD1 and E47, synergistically affect each other's nuclear import. In this study, we dissected the molecular pathways underlying NeuroD1/E47 heterodimer. vitro assays indicated importin α family members are major receptors for E47. However, inhibition resulted in cytoplasmic retention E47 could be rescued its binding partner, NeuroD1, through...

10.1091/mbc.e10-10-0809 article EN cc-by-nc-sa Molecular Biology of the Cell 2011-08-11

The nuclear transport of proteins is important for facilitating appropriate functions. importin α family play key roles in as receptors copious proteins. Additionally, these possess other functions, including chromatin association and gene regulation. However, nontransport functions are not yet fully understood, especially their molecular-level mechanisms consequences functioning with chromatin. Here, we report the novel molecular characteristics binding to diverse DNA sequences We newly...

10.1111/gtc.12896 article EN Genes to Cells 2021-09-14

The Ewing's sarcoma (EWS) oncogene is fused to a variety of cellular transcription factors in various forms human cancers. Although EWS fusion proteins have been extensively studied, the normal function remains poorly characterized. We previously reported that monoclonal antibody, referred as MY95, recognized nucleoporins such p62, Nup98, and CAN/Nup214 an uncharacterized polypeptide with apparent molecular mass 83 kDa. In present study, amino acid sequence analysis this 83-kDa protein...

10.1089/153685902760213831 article EN Hybridoma and Hybridomics 2002-08-01

The importin-α family of proteins plays an important role in the eukaryotic importin/exportin nuclear transport system. These recognize a localization signal (NLS) within cargo and import them into nucleus through pores, process mediated by importin-β. Recent studies have shown that specifically NLS several cellular factors viral proteins, thus regulating their movement. Dysregulation is common hallmark many pathologies including, multiple cancers. In this study, we isolated aptamers 76 72,...

10.1093/jb/mvw032 article EN The Journal of Biochemistry 2016-05-06

Importin α has been described as a nuclear protein transport receptor that enables proteins synthesized in the cytoplasm to translocate into nucleus. Besides its function transport, an increasing number of studies have examined non-nuclear functions. In both and functional domain called IBB (importin β binding domain) plays key role regulating importin behavior, is common interacting for multiple partners. However, it not yet fully understood how interacts with partners, which leads...

10.1111/gtc.12917 article EN Genes to Cells 2021-12-26
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