T. Mimoto

发表

Structure-activity relationship of small-sized HIV protease inhibitors containing allophenylnorstatine.

R. Kato, Y. Kiso, M. Shintani, 1999, Journal of medicinal chemistry.

Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.

H Enomoto, Y. Kiso, Y Kiso, 1992, Chemical & pharmaceutical bulletin.

Rational design and synthesis of a novel class of active site-targeted HIV protease inhibitors containing a hydroxymethylcarbonyl isostere. Use of phenylnorstatine or allophenylnorstatine as a transition-state mimic.

O. Takahashi, Y. Kiso, M. Shintani, 1991, Chemical & pharmaceutical bulletin.

In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine

S. Gulnik, J. Erickson, M. Nomizu, 1993, Antimicrobial Agents and Chemotherapy.

JE-2147: a dipeptide protease inhibitor (PI) that potently inhibits multi-PI-resistant HIV-1.

J. Falloon, H. Masur, H. Mitsuya, 1999, Proceedings of the National Academy of Sciences of the United States of America.

DNA sequence of the beta-isopropylmalate dehydrogenase gene and phylogenetic analysis of the yeast Saccharomyces exiguus Yp74L-3.

K. Horio, T. Hisatomi, M. Tsuboi, 1999, Journal of bioscience and bioengineering.

A practical use of ligand efficiency indices out of the fragment-based approach: ligand efficiency-guided lead identification of soluble epoxide hydrolase inhibitors.

Yusuke Tsuda, Yukio Tominaga, N. Kusunose, 2011, Journal of medicinal chemistry.

A new class of amino protecting group removable by reductive acidolysis: the 4-methylsulphinylbenzyloxycarbonyl (Msz) group

Y. Kiso, Makoto Yoshida, Tooru Kimura, 1989 .

Structure-activity relationship of orally potent tripeptide-based HIV protease inhibitors containing hydroxymethylcarbonyl isostere.

R. Kato, Y. Kiso, M. Shintani, 2000, Chemical & pharmaceutical bulletin.

Structure-activity relationships of novel HIV-1 protease inhibitors containing the 3-amino-2-chlorobenzoyl-allophenylnorstatine structure.

M. Shintani, S. Nojima, K. Terashima, 2008, Bioorganic & medicinal chemistry.

Structure-activity and structure-metabolism relationships of HIV protease inhibitors containing the 3-hydroxy-2-methylbenzoyl-allophenylnorstatine structure.

M. Shintani, S. Nojima, T. Yamaoka, 2004, Bioorganic & medicinal chemistry.

KNI‐577, a Potent Small‐Sized HIV Protease Inhibitor Based on the Dipeptide Containing the Hydroxymethylcarbonyl Isostere as an Ideal Transition‐State Mimic

R. Kato, Y. Kiso, H. Matsumoto, 1998, Archiv der Pharmazie.

KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic.

Y. Kiso, K. Akaji, J. Imai, 1991, Chemical & pharmaceutical bulletin.

Potent dipeptide HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimetic

R. Kato, Y. Kiso, H. Matsumoto, 2002 .

Allophenylnorstatine containing HIV-1 protease inhibitors: design, synthesis and structure-activity relationships for selected P2 ligands

Y. Kiso, H. Matsumoto, Tooru Kimura, 2005 .