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Institution

University of Tokyo

EducationTokyo, Japan
About: University of Tokyo is a education organization based out in Tokyo, Japan. It is known for research contribution in the topics: Population & Gene. The organization has 134564 authors who have published 337567 publications receiving 10178620 citations. The organization is also known as: Todai & Universitas Tociensis.


Papers
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Journal ArticleDOI
Marcos Daniel Actis1, G. Agnetta2, Felix Aharonian3, A. G. Akhperjanian  +682 moreInstitutions (109)
TL;DR: The ground-based gamma-ray astronomy has had a major breakthrough with the impressive results obtained using systems of imaging atmospheric Cherenkov telescopes as mentioned in this paper, which is an international initiative to build the next generation instrument, with a factor of 5-10 improvement in sensitivity in the 100 GeV-10 TeV range and the extension to energies well below 100GeV and above 100 TeV.
Abstract: Ground-based gamma-ray astronomy has had a major breakthrough with the impressive results obtained using systems of imaging atmospheric Cherenkov telescopes. Ground-based gamma-ray astronomy has a huge potential in astrophysics, particle physics and cosmology. CTA is an international initiative to build the next generation instrument, with a factor of 5-10 improvement in sensitivity in the 100 GeV-10 TeV range and the extension to energies well below 100 GeV and above 100 TeV. CTA will consist of two arrays (one in the north, one in the south) for full sky coverage and will be operated as open observatory. The design of CTA is based on currently available technology. This document reports on the status and presents the major design concepts of CTA.

1,006 citations

Journal ArticleDOI
TL;DR: In this article, the authors focused on the promising features of block copolymer micelles as drug vehicles mimicking the natural carrier-systems with supramolecular structures (i.e. viruses and lipoproteins).

1,006 citations

Journal ArticleDOI
TL;DR: Results show that the single cysteine residue determines LMB sensitivity and is selectively alkylated by LMB, leading to CRM1 inactivation.
Abstract: The cellular target of leptomycin B (LMB), a nuclear export inhibitor, has been identified as CRM1 (exportin 1), an evolutionarily conserved receptor for the nuclear export signal of proteins. However, the mechanism by which LMB inhibits CRM1 still remains unclear. CRM1 in a Schizosaccharomyces pombe mutant showing extremely high resistance to LMB had a single amino acid replacement at Cys-529 with Ser. The mutant gene, named crm1-K1, conferred LMB resistance on wild-type S. pombe, and Crm1-K1 no longer bound biotinylated LMB. 1H NMR analysis showed that LMB bound N-acetyl-l-cysteine methyl ester through a Michael-type addition, consistent with the idea that LMB binds covalently via its α,β-unsaturated δ-lactone to the sulfhydryl group of Cys-529. When HeLa cells were cultured with biotinylated LMB, the only cellular protein bound covalently was CRM1. Inhibition by N-ethylmaleimide (NEM), an alkylating agent, of CRM1-mediated nuclear export probably was caused by covalent binding of the electrophilic structure in NEM to the sulfhydryl group of Cys-529, because the crm1-K1 mutant showed the normal rate for the export of Rev nuclear export signal-bearing proteins in the presence of not only LMB but also NEM. These results show that the single cysteine residue determines LMB sensitivity and is selectively alkylated by LMB, leading to CRM1 inactivation.

1,002 citations

Journal ArticleDOI
TL;DR: It is demonstrated that simple SDS-PAGE under non-reducing and non-heat-denaturing conditions clearly separates multimer species of adiponectin.

1,001 citations

Journal ArticleDOI
TL;DR: The pattern of inhibition for the phosphatase in myosin B is similar to that of the type-1 enzyme, and the effects of both compounds on various phosphatases are screened.

999 citations


Authors

Showing all 135252 results

NameH-indexPapersCitations
Ronald C. Kessler2741332328983
Donald P. Schneider2421622263641
George M. Whitesides2401739269833
Jing Wang1844046202769
Tadamitsu Kishimoto1811067130860
Yusuke Nakamura1792076160313
Dennis J. Selkoe177607145825
David L. Kaplan1771944146082
D. M. Strom1763167194314
Masayuki Yamamoto1711576123028
Krzysztof Matyjaszewski1691431128585
Yang Yang1642704144071
Qiang Zhang1611137100950
Kenji Kangawa1531117110059
Takashi Taniguchi1522141110658
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20241
2023354
20221,250
202112,942
202013,511
201912,656