Kazuma Murakami, Ph.D.

Food Science and Biotechnology  Kyoto University, Kyōto-shi, Kyōto-fu, Japan 
Alzheimer's disease
"Kazuma Murakami"
Mean distance: 15638.9 (cluster 32)
Cross-listing: Alzheimer's Tree


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Gal Bitan post-doc 2007-2008 UCLA
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Murakami K, Tokuda M, Suzuki T, et al. (2016) Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer's disease diagnosis. Scientific Reports. 6: 29038
Murakami K, Suzuki T, Hanaki M, et al. (2015) Synthesis and characterization of the amyloid β40 dimer model with a linker at position 30 adjacent to the intermolecular β-sheet region. Biochemical and Biophysical Research Communications. 466: 463-7
Habukawa C, Murakami K, Endoh M, et al. (2015) Evaluation of airflow limitation using a new modality of lung sound analysis in asthmatic children. Allergology International : Official Journal of the Japanese Society of Allergology. 64: 84-9
Murakami K. (2014) Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer's disease. Bioscience, Biotechnology, and Biochemistry. 78: 1293-305
Murakami K, Irie K, Shimizu T. (2014) Potential Role of Vitamin C in the Prevention of Alzheimer's Disease Diet and Nutrition in Dementia and Cognitive Decline. 663-668
Sato M, Murakami K, Uno M, et al. (2013) Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues. The Journal of Biological Chemistry. 288: 23212-24
Kurisu M, Miyamae Y, Murakami K, et al. (2013) Inhibition of amyloid β aggregation by acteoside, a phenylethanoid glycoside. Bioscience, Biotechnology, and Biochemistry. 77: 1329-32
Izuo N, Murakami K, Sato M, et al. (2013) 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. Biochemical and Biophysical Research Communications. 438: 1-5
Sato M, Murakami K, Uno M, et al. (2013) Structure-activity relationship for (+)-taxifolin isolated from silymarin as an inhibitor of amyloid β aggregation. Bioscience, Biotechnology, and Biochemistry. 77: 1100-3
Kamachi H, Tanaka K, Yanagita RC, et al. (2013) Structure-activity studies on the side chain of a simplified analog of aplysiatoxin (aplog-1) with anti-proliferative activity. Bioorganic & Medicinal Chemistry. 21: 2695-702
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