Koichi Matsuo
Synchrotron Radiation Center
207 Papers
1.2K Citations
Koichi Matsuo is an academic researcher from Synchrotron Radiation Center. The author has contributed to research in topics: Circular dichroism & Chemistry. The author has an hindex of 43, co-authored 190 publications. Previous affiliations of Koichi Matsuo include University of Zurich & Research Institute of Molecular Pathology.
Chat about Author
Papers
A sensitive method based on fluorescence-detected circular dichroism for protein local structure analysis
TL;DR: An improved fluorescence-detected circular dichroism (FDCD)-based analytical method that is useful for probing protein three-dimensional structures and may provide a useful means for "pinpoint analysis" of protein structures.
11
Allele-specific activation of the c-myc gene in an atypical Burkitt's lymphoma carrying the t(2;8) chromosomal translocation 250 kb downstream from c-myc
Kouichi Tachibana,Nobuyuki Takayama,Koichi Matsuo,Shingo Kato,Kotaro Yamamoto,Kyoji Ohyama,Akihiro Umezawa,Toshiya Takano +7 more
TL;DR: Together activation by the long-distance immunoglobulin kappa enhancer, and the alleviation of negative regulation by the mutations, seemed to cause the allele-specific activation of c-myc.
11
Dissection of the Auditory Bulla in Postnatal Mice: Isolation of the Middle Ear Bones and Histological Analysis
TL;DR: How to dissect the auditory bulla and capsule of postnatal mice and then isolate individual ossicles by removing part of the bulla is described and anatomical differences between mouse and human auditory ossicle are enumerated.
Isotope effect on the circular dichroism spectrum of methyl α-D-glucopyranoside in aqueous solution.
TL;DR: It was demonstrated that the isotope effect provides insights not only into the isotopic difference of the intramolecular interactions of thesolutes, but also into that of the solute–solvent intermolecular interaction.
Structural analysis of lysine‐4 methylated histone H3 proteins using synchrotron radiation circular dichroism spectroscopy
TL;DR: The structural differences among K4-unmethylated/methylated H3 may allow epigenetic enzymes to discriminate the substrates both chemically and sterically.
10