INVOLVEMENT OF PROTEASOMES (MULTICATALYTIC PROTEINASE) IN ATP-DEPENDENT PROTEOLYSIS IN RAT RETICULOCYTE EXTRACTS

被引：67

作者：

TANAKA, K ^{[1
]}

ICHIHARA, A ^{[1
]}

机构：

[1] UNIV TOKUSHIMA, INST ENZYME RES, TOKUSHIMA 770, JAPAN

来源：

FEBS LETTERS | 1988年 / 236卷 / 01期

关键词：

D O I：

10.1016/0014-5793(88)80306-5

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：

引用

页码：159 / 162

页数：4

共 21 条

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[2] PURIFICATION AND CHARACTERIZATION OF A MULTICATALYTIC HIGH-MOLECULAR-MASS PROTEINASE FROM RAT SKELETAL-MUSCLE
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[J]. BIOCHEMICAL JOURNAL, 1985, 228 (01) : 161 - 170
[3] SOLUBLE ATP-DEPENDENT PROTEOLYTIC SYSTEM RESPONSIBLE FOR DEGRADATION OF ABNORMAL PROTEINS IN RETICULOCYTES
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[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1977, 74 (01) : 54 - 58
[4] INTRACELLULAR PROTEIN DEGRADATION IN MAMMALIAN AND BACTERIAL-CELLS .2.
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STJOHN, AC
[J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1976, 45 : 747 - 803
[5] ATP-DEPENDENT DEGRADATION OF UBIQUITIN-PROTEIN CONJUGATES
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HELLER, H
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (06): : 1619 - 1623
[6] MECHANISMS OF INTRACELLULAR PROTEIN BREAKDOWN
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[J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1982, 51 : 335 - 364
[7] HOUGH R, 1987, J BIOL CHEM, V262, P8303
[8] EFFECTS OF TEMPERATURE ON THE DEGRADATION OF PROTEINS IN RABBIT RETICULOCYTE LYSATES AND AFTER INJECTION INTO HELA-CELLS
HOUGH, R
RECHSTEINER, M
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (01): : 90 - 94
[9] ATP-STIMULATED PROTEOLYSIS IN SOLUBLE EXTRACTS OF BHK 21/C13 CELLS - EVIDENCE FOR MULTIPLE PATHWAYS AND A ROLE FOR AN ENZYME RELATED TO THE HIGH-MOLECULAR-WEIGHT PROTEASE, MACROPAIN
MCGUIRE, MJ
CROALL, DE
DEMARTINO, GN
[J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1988, 262 (01) : 273 - 285
[10] PURIFICATION AND CHARACTERIZATION OF A HIGH-MOLECULAR-WEIGHT PROTEINASE (MACROPAIN) FROM HUMAN-ERYTHROCYTES
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DEMARTINO, GN
[J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 873 (02) : 279 - 289

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