Characterization of CAA0225, a Novel Inhibitor Specific for Cathepsin L, as a Probe for Autophagic Proteolysis-Reference-Cited by-同舟云学术

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Characterization of CAA0225, a Novel Inhibitor Specific for Cathepsin L, as a Probe for Autophagic Proteolysis

Published:2009 Issue:3 Volume:32 Page:475-479
ISSN:0918-6158
Container-title:Biological and Pharmaceutical Bulletin
language:en
Short-container-title:Biol. Pharm. Bull.

Author:

Takahashi Katsuyuki¹²,Ueno Takashi²,Tanida Isei³,Minematsu-Ikeguchi Naoko²,Murata Mitsuo⁴,Kominami Eiki²

Affiliation:

1. Clinical Laboratory Department, Nihon University School of Medicine

2. Department of Biochemistry, Juntendo University School of Medicine

3. Department of Biochemistry and Cell Biology, National Institute of Infectious Disease

4. Research Center, Taisho Pharmaceutical Company

Publisher

Pharmaceutical Society of Japan

Subject

Pharmaceutical Science,Pharmacology,General Medicine

Link

http://www.jstage.jst.go.jp/article/bpb/32/3/32_3_475/_pdf

Reference35 articles.

1. Cathepsin L deficiency as molecular defect offurless:hyperproliferation of keratinocytes and pertubation of hair follicle cycling

2. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation

3. Novel epoxysuccinyl peptides Selective inhibitors of cathepsin B, in vitro

4. Novel epoxysuccinyl peptides A selective inhibitor of cathepsin B, in vivo

5. The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins

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