K. Murakami

发表

Synthetic biology based construction of biological activity-related library of fungal decalin-containing diterpenoid pyrones

S. Dan, H. Miyoshi, E. Kodama, 2020, Nature Communications.

Formation and stabilization model of the 42-mer Abeta radical: implications for the long-lasting oxidative stress in Alzheimer's disease.

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2005, Journal of the American Chemical Society.

The toxic conformation of the 42-residue amyloid beta peptide and its relevance to oxidative stress in Alzheimer's disease.

M. Nagao, T. Shirasawa, H. Ohigashi, 2007, Mini reviews in medicinal chemistry.

Identification and Biological Activities of Bryostatins from Japanese Bryozoan

A. Murakami, H. Tokuda, T. Fujiwara, 2012, Bioscience, biotechnology, and biochemistry.

Synthesis and physicochemical properties of 20-mer peptide nucleic acid conjugates with testosterone 17β-carboxylic acid

K. Irie, K. Murakami, Ryotaro Yagita, 2020 .

Detection of Amyloid β Oligomers with RNA Aptamers in AppNL-G-F/NL-G-F Mice: A Model of Arctic Alzheimer’s Disease

Takahiko Shimizu, K. Irie, Yayoi Obata, 2020, ACS omega.

The Taurine Transporter Eaat2 Functions in Ensheathing Glia to Modulate Sleep and Metabolic Rate

A. Keene, K. Murakami, B. A. Stahl, 2018, Current Biology.

Potential Role of Vitamin C in the Prevention of Alzheimer’s Disease

Takahiko Shimizu, K. Irie, K. Murakami, 2015 .

Skin atrophy in cytoplasmic SOD-deficient mice and its complete recovery using a vitamin C derivative.

Y. Ikeda, T. Shirasawa, Takahiko Shimizu, 2009, Biochemical and biophysical research communications.

Interactions of amyloid coaggregates with biomolecules and its relevance to neurodegeneration

K. Ono, K. Murakami, 2022, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Toxicity in rat primary neurons through the cellular oxidative stress induced by the turn formation at positions 22 and 23 of Aβ42.

A. Akaike, K. Irie, K. Murakami, 2012, ACS chemical neuroscience.

Cytoplasmic superoxide radical

Takahiko Shimizu, K. Murakami, 2012, Communicative & integrative biology.

Inhibitory Activities of Antioxidant Flavonoids from Tamarix gallica on Amyloid Aggregation Related to Alzheimer's and Type 2 Diabetes Diseases.

H. Isoda, K. Irie, K. Murakami, 2017, Biological & pharmaceutical bulletin.

Synthetic and biophysical studies on the toxic conformer in amyloid β with the E22Δ mutation in Alzheimer pathology.

K. Irie, H. Hara, K. Murakami, 2020, ACS chemical neuroscience.

An RNA aptamer with potent affinity for a toxic dimer of amyloid β42 has potential utility for histochemical studies of Alzheimer's disease

Takahiko Shimizu, K. Takabe, T. Awano, 2020, The Journal of Biological Chemistry.

Role of the carboxy groups of triterpenoids in their inhibition of the nucleation of amyloid β42 required for forming toxic oligomers.

K. Irie, K. Murakami, K. Hirose, 2018, Chemical communications.

Mechanistic analyses of the suppression of amyloid β42 aggregation by apomorphine.

K. Irie, K. Murakami, Sumie Katayama, 2018, Bioorganic & medicinal chemistry.

Lack of the Consensus Sequence Necessary for Tryptophan Prenylation in the ComX Pheromone Precursor

S. Kitamura, Y. Sakagami, K. Irie, 2012, Bioscience, biotechnology, and biochemistry.

Synthesized Aβ42 Caused Intracellular Oxidative Damage, Leading to Cell Death, via Lysosome Rupture.

J. Hoseki, Y. Sakai, K. Irie, 2017, Cell structure and function.

Insulin deficiency promotes formation of toxic amyloid-β42 conformer co-aggregating with hyper-phosphorylated tau oligomer in an Alzheimer's disease model

J. Kira, M. Maeda, K. Irie, 2020, Neurobiology of Disease.

Synthesis and characterization of the amyloid β40 dimer model with a linker at position 30 adjacent to the intermolecular β-sheet region.

K. Irie, K. Murakami, K. Akagi, 2015, Biochemical and biophysical research communications.

Protective effects of caffeoylquinic acids on the aggregation and neurotoxicity of the 42-residue amyloid β-protein.

H. Isoda, K. Irie, Junkyu Han, 2012, Bioorganic & Medicinal Chemistry.

Synthetic Models of Quasi-Stable Amyloid β40 Oligomers with Significant Neurotoxicity.

K. Irie, K. Murakami, T. Takai, 2017, ACS chemical neuroscience.

Evaluation of Toxic Amyloid β42 Oligomers in Rat Primary Cerebral Cortex Cells and Human iPS-derived Neurons Treated with 10-Me-Aplog-1, a New PKC Activator

H. Inoue, T. Kondo, K. Irie, 2020, International journal of molecular sciences.

Structure of β-amyloid fibrils and its relevance to their neurotoxicity: Implications for the pathogenesis of Alzheimer’s disease

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2005 .

Inhibition of Amyloid β Aggregation by Acteoside, a Phenylethanoid Glycoside

H. Isoda, K. Irie, Junkyu Han, 2013, Bioscience, biotechnology, and biochemistry.

Inhibitory Activity of Hispidin Derivatives Isolated from Inonotus obliquus on Amyloid β Aggregation

K. Irie, K. Murakami, H. Shigemori, 2017 .

Aptamers targeting amyloidogenic proteins and their emerging role in neurodegenerative diseases

G. Bitan, K. Murakami, Naotaka Izuo, 2021, The Journal of biological chemistry.

Modeling Alzheimer's disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness.

Katsuhiro Yoshikawa, Takashi Asada, Takashi Aoi, 2013, Cell stem cell.

Three Structural Features of Functional Food Components and Herbal Medicine with Amyloid β42 Anti-Aggregation Properties

K. Irie, K. Murakami, 2019, Molecules.

A Toxic Conformer of Aβ42 with a Turn at 22–23 is a Novel Therapeutic Target for Alzheimer’s Disease

M. Maeda, Takahiko Shimizu, K. Yokote, 2017, Scientific Reports.

A screen for sleep and starvation resistance identifies a wake-promoting role for the auxiliary channel unc79

A. Keene, Bethany A. Stanhope, K. Murakami, 2021, bioRxiv.

Amyloid β toxic conformer has dynamic localization in the human inferior parietal cortex in absence of amyloid plaques

S. Resnick, Y. An, J. Troncoso, 2018, Scientific Reports.

Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease.

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2003, The Journal of biological chemistry.

Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR.

T. Shirasawa, Takahiko Shimizu, H. Ohigashi, 2005, Bioorganic & medicinal chemistry.

translin Is Required for Metabolic Regulation of Sleep

Pavel Masek, A. Keene, Young-Joon Kim, 2016, Current Biology.

Synthetic biology based construction of biological activity-related library of fungal decalin-containing diterpenoid pyrones

S. Dan, H. Miyoshi, E. Kodama, 2020, Nature Communications.

Development: Better Sleep On It, Children

A. Keene, K. Murakami, 2014, Current Biology.

Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer's-like phenotypes in mice.

T. Shirasawa, Takahiko Shimizu, K. Irie, 2011, Biochemical and biophysical research communications.

Searching for Natural Products That Delay Nucleation Phase and Promote Elongation Phase of Amyloid β42 toward Alzheimer's Disease Therapeutics.

K. Irie, K. Murakami, Mizuho Hanaki, 2021, ACS chemical neuroscience.

Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease

Takahiko Shimizu, K. Irie, K. Murakami, 2011, Journal of amino acids.

Amyloids and Protein Aggregation-Analytical Methods

G. Bitan, F. Rahimi, P. Maiti, 2009 .

Silymarin Attenuated the Amyloid β Plaque Burden and Improved Behavioral Abnormalities in an Alzheimer’s Disease Mouse Model

T. Shirasawa, Takahiko Shimizu, K. Irie, 2010, Bioscience, biotechnology, and biochemistry.

Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23.

T. Shirasawa, Takahiko Shimizu, S. Murayama, 2010, ACS chemical neuroscience.

Intracellular accumulation of toxic turn amyloid-β is associated with endoplasmic reticulum stress in Alzheimer's disease.

T. Tabira, T. Iwaki, J. Kira, 2013, Current Alzheimer research.

An App knock-in mouse inducing the formation of a toxic conformer of Aβ as a model for evaluating only oligomer-induced cognitive decline in Alzheimer's disease.

M. Maeda, Takahiko Shimizu, T. Saido, 2019, Biochemical and biophysical research communications.

Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer’s disease diagnosis

T. Tokuda, M. Maeda, Takahiko Shimizu, 2016, Scientific Reports.

Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease

K. Murakami, 2014, Bioscience, biotechnology, and biochemistry.

Non-toxic conformer of amyloid β may suppress amyloid β-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy for Alzheimer's disease.

Takahiko Shimizu, A. Akaike, K. Irie, 2013, Biochemical and biophysical research communications.

Site-specific Inhibitory Mechanism for Amyloid β42 Aggregation by Catechol-type Flavonoids Targeting the Lys Residues*

K. Irie, Y. Masuda, K. Takegoshi, 2013, Journal of Biological Chemistry.

The turn formation at positions 22 and 23 in the 42‐mer amyloid β peptide: The emerging role in the pathogenesis of Alzheimer's disease

T. Shirasawa, Takahiko Shimizu, K. Irie, 2010, Geriatrics & gerontology international.

Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23.

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2002, Biochemical and biophysical research communications.

Structure-activity studies on the side chain of a simplified analog of aplysiatoxin (aplog-1) with anti-proliferative activity.

A. Murakami, H. Tokuda, K. Irie, 2013, Bioorganic & medicinal chemistry.

Vitamin C restores behavioral deficits and amyloid-β oligomerization without affecting plaque formation in a mouse model of Alzheimer's disease.

T. Shirasawa, Takahiko Shimizu, K. Irie, 2011, Journal of Alzheimer's disease : JAD.

Geranyl modification on the tryptophan residue of ComXRO‐E‐2 pheromone by a cell‐free system

S. Kitamura, Y. Sakagami, K. Irie, 2012, FEBS letters.

Structural insights into mechanisms for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids.

Ken-ichi Akagi, K. Irie, Kazuhiro Irie, 2016, Bioorganic & medicinal chemistry.

Altered regulation of sleep and feeding contributes to starvation resistance in Drosophila melanogaster

Pavel Masek, A. Keene, A. Gibbs, 2014, Journal of Experimental Biology.

Synthetic Biology-Based Discovery of Diterpenoid Pyrones from the Genome of Eupenicillium shearii.

K. Irie, Kento Tsukada, K. Murakami, 2022, Journal of natural products.

E22Δ Mutation in Amyloid β-Protein Promotes β-Sheet Transformation, Radical Production, and Synaptotoxicity, But Not Neurotoxicity

A. Akaike, T. Nagata, T. Nishizaki, 2010, International journal of Alzheimer's disease.

SOD1 (Copper/Zinc Superoxide Dismutase) Deficiency Drives Amyloid β Protein Oligomerization and Memory Loss in Mouse Model of Alzheimer Disease*

Takao Kaneko, Shigeo Murayama, Noriaki Kinoshita, 2011, The Journal of Biological Chemistry.

Preparation of stable amyloid β-protein oligomers of defined assembly order.

G. Bitan, D. Teplow, K. Ono, 2012, Methods in molecular biology.

Semisynthesis and Structure-Activity Studies of Uncarinic Acid C Isolated from Uncaria rhynchophylla as a Specific Inhibitor of the Nucleation Phase in Amyloid β42 Aggregation.

K. Irie, Kyohei Ido, K. Murakami, 2016, Journal of natural products.

Synthetic and biochemical studies on the effect of persulfidation on disulfide dimer models of amyloid β42 at position 35 in Alzheimer's etiology

K. Irie, K. Murakami, K. Hirose, 2020, RSC advances.

Stimulation of the Amyloidogenic Pathway by Cytoplasmic Superoxide Radicals in an Alzheimer's Disease Mouse Model

T. Shirasawa, Takahiko Shimizu, K. Irie, 2012, Bioscience, biotechnology, and biochemistry.

Isomerization and/or racemization at Asp23 of Abeta42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro.

T. Shirasawa, Takahiko Shimizu, K. Irie, 2008, Biochemical and biophysical research communications.

Distance Measurement between Tyr10 and Met35 in Amyloid β by Site‐Directed Spin‐Labeling ESR Spectroscopy: Implications for the Stronger Neurotoxicity of Aβ42 than Aβ40

H. Ohigashi, K. Irie, H. Hara, 2007 .

Structure–Activity Relationship for (+)-Taxifolin Isolated from Silymarin as an Inhibitor of Amyloid β Aggregation

K. Irie, K. Murakami, Y. Nakagawa, 2013, Bioscience, biotechnology, and biochemistry.

Development of a platinum complex as an anti-amyloid agent for the therapy of Alzheimer's disease.

C. Masters, P. Adlard, R. Cappai, 2013, Angewandte Chemie.

Synthesis and biochemical characterization of quasi-stable trimer models of full-length amyloid β40 with a toxic conformation.

T. Kawabata, K. Irie, K. Murakami, 2018, Chemical communications.

RNA Aptamers Generated against Oligomeric Aβ40 Recognize Common Amyloid Aptatopes with Low Specificity but High Sensitivity

G. Bitan, F. Rahimi, Chi‐hong B. Chen, 2009, PloS one.

Neurotoxicity and Physicochemical Properties of Aβ Mutant Peptides from Cerebral Amyloid Angiopathy

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2003, Journal of Biological Chemistry.

Aggregation and neurotoxicity of mutant amyloid β (Aβ) peptides with proline replacement: importance of turn formation at positions 22 and 23

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2002 .

Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease.

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2005, Journal of bioscience and bioengineering.

[Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23].

T. Shirasawa, Takahiko Shimizu, S. Murayama, 2011, Rinsho shinkeigaku = Clinical neurology.

Analysis of the Secondary Structure of β-Amyloid (Aβ42) Fibrils by Systematic Proline Replacement*

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2004, Journal of Biological Chemistry.

Activity-differential search for amyloid-β aggregation inhibitors using LC-MS combined with principal component analysis.

K. Irie, K. Murakami, H. Gunji, 2022, Bioorganic & medicinal chemistry letters.

Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement.

M. Nagao, T. Shirasawa, Takahiko Shimizu, 2004, The Journal of biological chemistry.

Amyloid β toxic conformer has dynamic localization in the human inferior parietal cortex in absence of amyloid plaques

S. Resnick, Y. An, J. Troncoso, 2018, Scientific Reports.

The turn formation at positions 22 and 23 in the 42‐mer amyloid β peptide: The emerging role in the pathogenesis of Alzheimer's disease

T. Shirasawa, Takahiko Shimizu, K. Irie, 2010, Geriatrics & gerontology international.

Site-specific Inhibitory Mechanism for Amyloid β42 Aggregation by Catechol-type Flavonoids Targeting the Lys Residues*

K. Irie, Y. Masuda, K. Takegoshi, 2013, The Journal of Biological Chemistry.

Detection of Dietary Chalcone and Flavonoid Metabolites in Mice Using UPLC-MS/MS and Their Modulatory Effects on Amyloid β Aggregation.

K. Murakami, Naotaka Izuo, Mizuho Hanaki, 2023, Journal of Agricultural and Food Chemistry.

Early accumulation of intracellular fibrillar oligomers and late congophilic amyloid angiopathy in mice expressing the Osaka intra-Aβ APP mutation

R. Nitsch, T. Welt, L. Kulic, 2012, Translational Psychiatry.

Role of the carboxy groups of triterpenoids in their inhibition of the nucleation of amyloid β42 required for forming toxic oligomers.

K. Irie, K. Murakami, K. Hirose, 2018, Chemical communications.

Altered regulation of sleep and feeding contributes to starvation resistance in Drosophila melanogaster

Pavel Masek, A. Keene, A. Gibbs, 2014, Journal of Experimental Biology.

SYNTHESIS AND BIOLOGICAL ACTIVITIES OF THE Aβ40 DIMER WITH TOXIC CONFORMATION

K. Murakami, Toshiaki Kume, Kazuhiro Irie, 2014, Alzheimer's & Dementia.