Chaperonin-mediated folding of actin and tubulin.
作者信息
Lewis S A, Tian G, Vainberg I E, Cowan N J
机构信息
Department of Biochemistry, New York University Medical Center, New York 10016, USA.
出版信息
J Cell Biol. 1996 Jan;132(1-2):1-4. doi: 10.1083/jcb.132.1.1.
Abstract
摘要
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本文引用的文献
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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.从无折叠状态重构活性二聚体核酮糖二磷酸羧化酶依赖于两种伴侣蛋白和Mg-ATP。
Nature. 1989;342(6252):884-9. doi: 10.1038/342884a0.
2
The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.t-复合体多肽1复合体在体内是微管蛋白和肌动蛋白的伴侣蛋白。
Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9422-6. doi: 10.1073/pnas.90.20.9422.
3
Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.细菌胞质蛋白在体内的折叠：GroEL的作用
Cell. 1993 Sep 10;74(5):909-17. doi: 10.1016/0092-8674(93)90470-b.
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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.大肠杆菌GroEL对腺苷5'-三磷酸的水解作用：GroES和钾离子的影响
Biochemistry. 1993 Aug 24;32(33):8560-7. doi: 10.1021/bi00084a024.
5
To fold or not to fold...折还是不折...
Science. 1993 Jun 25;260(5116):1903-4. doi: 10.1126/science.8100365.
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Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin.α-微管蛋白和β-微管蛋白的折叠需要两种辅因子和细胞质伴侣蛋白。
Mol Cell Biol. 1993 Apr;13(4):2478-85. doi: 10.1128/mcb.13.4.2478-2485.1993.
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Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.鉴定六个与Tcp-1相关的基因，这些基因编码含Tcp-1伴侣蛋白的不同亚基。
Curr Biol. 1994 Feb 1;4(2):89-99. doi: 10.1016/s0960-9822(94)00024-2.
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Residues in chaperonin GroEL required for polypeptide binding and release.伴侣蛋白GroEL中多肽结合与释放所需的残基。
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The crystal structure of the bacterial chaperonin GroEL at 2.8 A.细菌伴侣蛋白GroEL在2.8埃时的晶体结构。
Nature. 1994 Oct 13;371(6498):578-86. doi: 10.1038/371578a0.
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A yeast TCP-1-like protein is required for actin function in vivo.一种酵母类TCP-1蛋白在体内对肌动蛋白功能是必需的。
Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):9116-20. doi: 10.1073/pnas.91.19.9116.
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