Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

Kazuma Murakami

Showing results (41-50 of 83) with videos related to

Pageof 9
Sort By:
Biochemical and Biophysical Research Communications|June 11, 2002
Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23Kazuma Murakami, Kazuhiro Irie, Akira Morimoto, et al.
Scientific Reports|September 20, 2017
A Toxic Conformer of Aβ42 with a Turn at 22-23 is a Novel Therapeutic Target for Alzheimer's DiseaseNaotaka Izuo, Chihiro Kasahara, Kazuma Murakami, et al.
Biochemical and Biophysical Research Communications|August 2, 2002
Aggregation and neurotoxicity of mutant amyloid beta (A beta) peptides with proline replacement: importance of turn formation at positions 22 and 23Akira Morimoto, Kazuhiro Irie, Kazuma Murakami, et al.
Bioorganic & Medicinal Chemistry|September 27, 2005
Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMRYuichi Masuda, Kazuhiro Irie, Kazuma Murakami, et al.
Bioscience, Biotechnology, and Biochemistry|June 29, 2012
Identification and biological activities of bryostatins from Japanese bryozoanSayo Ueno, Ryo C Yanagita, Kazuma Murakami, et al.
RSC Advances|May 6, 2022
Synthetic and biochemical studies on the effect of persulfidation on disulfide dimer models of amyloid β42 at position 35 in Alzheimer's etiologyKazuma Murakami, Haruka Kato, Mizuho Hanaki, et al.
Biochemical and Biophysical Research Communications|June 6, 2019
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 diseaseNaotaka Izuo, Kazuma Murakami, Yoshitaka Fujihara, et al.
Bioscience, Biotechnology, and Biochemistry|May 8, 2013
Structure-activity relationship for (+)-taxifolin isolated from silymarin as an inhibitor of amyloid β aggregationMizuho Sato, Kazuma Murakami, Mayumi Uno, et al.
RSC Chemical Biology|December 22, 2022
Lysine-targeting inhibition of amyloid β oligomerization by a green perilla-derived metastable chalcone <i>in vitro</i> and <i>in vivo</i>Kazuma Murakami, Yoshiki Sakaguchi, Kota Taniwa, et al.
Journal of Agricultural and Food Chemistry|September 13, 2023
Detection of Dietary Chalcone and Flavonoid Metabolites in Mice Using UPLC-MS/MS and Their Modulatory Effects on Amyloid β AggregationKota Taniwa, Kazuma Murakami, Yoshiki Sakaguchi, et al.
Pageof 9

Showing results (41-50 of 83) with videos related to

Sort By:
Pageof 9
Biochemical and Biophysical Research Communications|June 11, 2002
Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23Kazuma Murakami, Kazuhiro Irie, Akira Morimoto, et al.
Scientific Reports|September 20, 2017
A Toxic Conformer of Aβ42 with a Turn at 22-23 is a Novel Therapeutic Target for Alzheimer's DiseaseNaotaka Izuo, Chihiro Kasahara, Kazuma Murakami, et al.
Biochemical and Biophysical Research Communications|August 2, 2002
Aggregation and neurotoxicity of mutant amyloid beta (A beta) peptides with proline replacement: importance of turn formation at positions 22 and 23Akira Morimoto, Kazuhiro Irie, Kazuma Murakami, et al.
Bioorganic & Medicinal Chemistry|September 27, 2005
Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMRYuichi Masuda, Kazuhiro Irie, Kazuma Murakami, et al.
Bioscience, Biotechnology, and Biochemistry|June 29, 2012
Identification and biological activities of bryostatins from Japanese bryozoanSayo Ueno, Ryo C Yanagita, Kazuma Murakami, et al.
RSC Advances|May 6, 2022
Synthetic and biochemical studies on the effect of persulfidation on disulfide dimer models of amyloid β42 at position 35 in Alzheimer's etiologyKazuma Murakami, Haruka Kato, Mizuho Hanaki, et al.
Biochemical and Biophysical Research Communications|June 6, 2019
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 diseaseNaotaka Izuo, Kazuma Murakami, Yoshitaka Fujihara, et al.
Bioscience, Biotechnology, and Biochemistry|May 8, 2013
Structure-activity relationship for (+)-taxifolin isolated from silymarin as an inhibitor of amyloid β aggregationMizuho Sato, Kazuma Murakami, Mayumi Uno, et al.
RSC Chemical Biology|December 22, 2022
Lysine-targeting inhibition of amyloid β oligomerization by a green perilla-derived metastable chalcone <i>in vitro</i> and <i>in vivo</i>Kazuma Murakami, Yoshiki Sakaguchi, Kota Taniwa, et al.
Journal of Agricultural and Food Chemistry|September 13, 2023
Detection of Dietary Chalcone and Flavonoid Metabolites in Mice Using UPLC-MS/MS and Their Modulatory Effects on Amyloid β AggregationKota Taniwa, Kazuma Murakami, Yoshiki Sakaguchi, et al.
Pageof 9