Proteasome inhibitors: from research tools to drug candidates

被引：983

作者：

Kisselev, AF ^{[1
]}

Goldberg, AL ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

来源：

CHEMISTRY & BIOLOGY | 2001年 / 8卷 / 08期

关键词：

proteasome inhibitor; ubiquitin-proteasome pathway; drug candidate;

D O I：

10.1016/S1074-5521(01)00056-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The 26S proteasome is a 2.4 MDa multifunctional ATP-dependent proteolytic complex, which degrades the majority of cellular polypeptides by an unusual enzyme mechanism. Several groups of proteasome inhibitors have been developed and are now widely used as research tools to study the role of the ubiquitin-proteasome pathway in various cellular processes, and two inhibitors are now in clinical trials for treatment of multiple cancers and stroke. (C) 2001 Elsevier Science Ltd. All rights reserved.

引用

页码：739 / 758

页数：20

共 152 条

[1]

Adams J, 1999, CANCER RES, V59, P2615

[2] New agents in cancer clinical trials [J].

Adams, J ;

Elliott, PJ .

ONCOGENE, 2000, 19 (56) :6687-6692

[3] Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids [J].

Adams, J ;

Behnke, M ;

Chen, SW ;

Cruickshank, AA ;

Dick, LR ;

Grenier, L ;

Klunder, JM ;

Ma, YT ;

Plamondon, L ;

Stein, RL .

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 1998, 8 (04) :333-338

[4] Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum [J].

Akopian, TN ;

Kisselev, AF ;

Goldberg, AL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (03) :1791-1798

[5] Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts [J].

An, B ;

Goldfarb, RH ;

Siman, R ;

Dou, QP .

CELL DEATH AND DIFFERENTIATION, 1998, 5 (12) :1062-1075

[6] Protease inhibitor-induced apoptosis:: accumulation of wt p53, p21WAF1/CIP1 and induction of apoptosis are independent markers of proteasome inhibition [J].

An, WG ;

Hwang, SG ;

Trepel, JB ;

Blagosklonny, MV .

LEUKEMIA, 2000, 14 (07) :1276-1283

[7] Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation [J].

Arendt, CS ;

Hochstrasser, M .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (14) :7156-7161

[8] The proteasome:: Paradigm of a self-compartmentalizing protease [J].

Baumeister, W ;

Walz, J ;

Zühl, F ;

Seemuller, E .

CELL, 1998, 92 (03) :367-380

[9] PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone [J].

Benaroudj, N ;

Goldberg, AL .

NATURE CELL BIOLOGY, 2000, 2 (11) :833-839

[10] Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors [J].

Bogyo, M ;

McMaster, JS ;

Gaczynska, M ;

Tortorella, D ;

Goldberg, AL ;

Ploegh, H .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (13) :6629-6634

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