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Koichi Ishiguro

Koichi Ishiguro

D-Index & Metrics

Biology and Biochemistry

D-Index
64
Citations
13211
World Ranking
9777
National Ranking
656

Overview

Koichi Ishiguro is affiliated with Juntendo University in Japan with a research focus primarily in medicine. Their work spans various subfields including physiology, cellular and molecular neuroscience, pharmacology, psychiatry and mental health, and neurology.

Their research largely concentrates on Alzheimer's disease and related neurodegenerative disorders, covering topics such as Alzheimer's disease research and treatments, cholinesterase and neurodegenerative diseases, dementia and cognitive impairment research, neuroscience and neuropharmacology research, drug transport and resistance mechanisms, autophagy in disease and therapy, and Parkinson's disease mechanisms and treatments.

Selected recent papers authored by Ishiguro include:

  • High-fat diet-induced activation of SGK1 promotes Alzheimer's disease-associated tau pathology, 2021, Human Molecular Genetics
  • Asparagine residue 368 is involved in Alzheimer's disease tau strain-specific aggregation, 2020, Journal of Biological Chemistry
  • Strain-specific clearance of seed-dependent tau aggregation by lithium-induced autophagy, 2021, Biochemical and Biophysical Research Communications
  • Learning Deficits Accompanied by Microglial Proliferation After the Long-Term Post-Injection of Alzheimer's Disease Brain Extract in Mouse Brains, 2021, Journal of Alzheimer s Disease
  • High-fat diet-induced activation of SGK1 promotes Alzheimer's disease-associated tau pathology, 2020, bioRxiv (Cold Spring Harbor Laboratory)

Frequent co-authors in Ishiguro's research include:

  • Montasir Elahi
  • Yumiko Motoi
  • Shotaro Shimonaka
  • Nobutaka Hattori
  • Masashi Takanashi

Ishiguro has published repeatedly in venues such as Alzheimer s & Dementia, Human Molecular Genetics, Journal of Biological Chemistry, Biochemical and Biophysical Research Communications, and Journal of Alzheimer s Disease.

Best Publications

  • Measurement of phosphorylated tau epitopes in the differential diagnosis of Alzheimer disease: a comparative cerebrospinal fluid study.

    Harald Hampel;Katharina Buerger;Raymond Zinkowski;Stefan J. Teipel

  • Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments

    Koichi Ishiguro;Akiko Shiratsuchi;Showbu Sato;Akira Omori

  • Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25.

    Gen-ichi Kusakawa;Gen-ichi Kusakawa;Taro Saito;Reiko Onuki;Reiko Onuki;Koichi Ishiguro

  • Activation of tau protein kinase I/glycogen synthase kinase-3β by amyloid β peptide (25–35) enhances phosphorylation of tau in hippocampal neurons

    Akihiko Takashima;Toshiyuki Honda;Kaori Yasutake;Gilles Michel

  • Regulation of mitochondrial pyruvate dehydrogenase activity by tau protein kinase I/glycogen synthase kinase 3beta in brain

    Minako Hoshi;Akihiko Takashima;Kaori Noguchi;Miyuki Murayama

  • Exposure of rat hippocampal neurons to amyloid β peptide (25–35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β

    Akihiko Takashima;Kaori Noguchi;Gilles Michel;Marc Mercken

  • Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments.

    K Ishiguro;M Takamatsu;K Tomizawa;A Omori

  • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II

    Haruyasu Yamaguchi;Koichi Ishiguro;Tsuneko Uchida;Akihiko Takashima

  • Tau filament formation and associative memory deficit in aged mice expressing mutant (R406W) human tau

    Yoshitaka Tatebayashi;Tomohiro Miyasaka;De-Hua Chui;Takumi Akagi

  • Alterations in Glucose Metabolism Induce Hypothermia Leading to Tau Hyperphosphorylation through Differential Inhibition of Kinase and Phosphatase Activities: Implications for Alzheimer's Disease

    Emmanuel Planel;Tomohiro Miyasaka;Thomas Launey;De Hua Chui

  • Site-specific Phosphorylation of Synapsin I by Mitogen-activated Protein Kinase and Cdk5 and Its Effects on Physiological Functions

    Mamoru Matsubara;Masashi Kusubata;Koichi Ishiguro;Tsuneko Uchida

  • A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubule

    Shunsuke Kobayashi;Koichi Ishiguro;Akira Omori;Masako Takamatsu

  • Large-scale, multicenter study of cerebrospinal fluid tau protein phosphorylated at serine 199 for the antemortem diagnosis of Alzheimer's disease

    Nobuo Itoh;Hiroyuki Arai;Katsuya Urakami;Koichi Ishiguro

  • Inhibition of Protein Phosphatase 2A Overrides Tau Protein Kinase I/Glycogen Synthase Kinase 3β and Cyclin-dependent Kinase 5 Inhibition and Results in Tau Hyperphosphorylation in the Hippocampus of Starved Mouse

    Emmanuel Planel;Kaori Yasutake;Shinobu C. Fujita;Koichi Ishiguro

  • Physiological and pathological phosphorylation of tau by Cdk5

    Taeko Kimura;Koichi Ishiguro;Shin-ichi Hisanaga

  • Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3beta.

    Fumiko Mukai;Koichi Ishiguro;Yumiko Sano;Shinobu C. Fujita

  • Phosphorylated tau in human cerebrospinal fluid is a diagnostic marker for Alzheimer's disease.

    Koichi Ishiguro;Hideto Ohno;Hiroyuki Arai;Haruyasu Yamaguchi

  • Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments.

    Koichi Ishiguro;Akira Omori;Masako Takamatsu;Kazuki Sato

  • Identification of amino‐terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration

    Tetsuaki Arai;Kenji Ikeda;Haruhiko Akiyama;Takashi Nonaka

  • Nontoxic amyloid beta peptide 1-42 suppresses acetylcholine synthesis. Possible role in cholinergic dysfunction in Alzheimer's disease.

    Minako Hoshi;Akihiko Takashima;Miyuki Murayama;Kaori Yasutake

Frequent Co-Authors

Shin-ichi Hisanaga
Shin-ichi Hisanaga Tokyo Metropolitan University
Nobutaka Hattori
Nobutaka Hattori Juntendo University
Masato Hasegawa
Masato Hasegawa Tokyo Metropolitan Institute of Medical Science
Kazuki Sato
Kazuki Sato Fukuoka Women's University
Akihiko Takashima
Akihiko Takashima Gakushuin University
Mikio Shoji
Mikio Shoji Hirosaki University
Hiroyuki Arai
Hiroyuki Arai University of Tokyo
Takeo Kishimoto
Takeo Kishimoto Tokyo Institute of Technology
Katharina Buerger
Katharina Buerger Ludwig-Maximilians-Universität München
Masatoshi Takeda
Masatoshi Takeda Izumi University

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