YCU PR Office

2020-01-29

Compound lights up brain receptors in PET scans

A radiotracer specifically binds to a major class of brain receptors when injected into living rats and humans, lighting them up in PET scans. The compound, called [11C]K-2, was designed and tested by a large team of scientists in Japan, led by Professor Takuya Takahashi of the department of physiology at Yokohama City University Graduate School of Medicine. It shows promise for diagnosing and treating epilepsy and for improving understanding of psychiatric diseases. Details of the team’s findings were published in the journal Nature Medicine.
2020-01-10

WiDS Tokyo@YCU 2019

The Women in Data Science (WiDS) initiative aims to inspire and educate data scientists worldwide, regardless of gender, and to support women in the field. WiDS is administered by the Institute for Computational & Mathematical Engineering, Stanford University, USA. The WiDS conference, associated events, and data challenges are all aimed at nurturing human resources in the field of data science.
2020-01-10

Women in Data Science (WiDS) Tokyo @ Yokohama City University

The Women in Data Science (WiDS) initiative aims to inspire and educate data scientists worldwide, regardless of gender, and to support women in the field. WiDS is administered by the Institute for Computational & Mathematical Engineering, Stanford University, USA. The WiDS conference, associated events, and data challenges are all aimed at nurturing human resources in the field of data science.
2019-12-03

A GM1b/asialo‐GM1 oligosaccharide‐binding R‐type lectin from purplish bifurcate mussels Mytilisepta virgata and its effect on MAP kinases

A 15‐kDa lectin, termed SeviL, was isolated from Mytilisepta virgata (purplish bifurcate mussel). SeviL forms a noncovalent dimer that binds strongly to ganglio‐series GM1b oligosaccharide (Neu5Acɑ2‐3Galβ1‐3GalNAcβ1‐4Galβ1‐4Glc) and its precursor, asialo‐GM1 (Galβ1‐3GalNAcβ1‐4Galβ1‐4Glc). SeviL also interacts weakly with the glycan moiety of SSEA‐4 hexaose (Neu5Acα2‐3Galβ1‐3GalNAcβ1‐3Galα1‐4Galβ1‐4Glc). A partial protein sequence of the lectin was determined by mass spectrometry, and the complete sequence was identified from transcriptomic analysis.