The spectrin skeleton: from red cells to brain.
作者信息
Bennett V, Lambert S
机构信息
Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710.
出版信息
J Clin Invest. 1991 May;87(5):1483-9. doi: 10.1172/JCI115157.
Abstract
摘要
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本文引用的文献
1
Properties and structural role of the subunits of human spectrin.人血影蛋白亚基的特性及结构作用
Eur J Biochem. 1980 Jun;107(2):355-61. doi: 10.1111/j.1432-1033.1980.tb06036.x.
2
Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin.脑血影蛋白，一种在结构和功能上与红细胞血影蛋白相关的膜相关蛋白。
Nature. 1982 Sep 9;299(5879):126-31. doi: 10.1038/299126a0.
3
Switching of subunit composition of muscle spectrin during myogenesis in vitro.体外成肌过程中肌动蛋白亚基组成的转换
Nature. 1983;304(5924):364-8. doi: 10.1038/304364a0.
4
The spectrin-related molecule, TW-260/240, cross-links the actin bundles of the microvillus rootlets in the brush borders of intestinal epithelial cells.血影蛋白相关分子TW-260/240可交联肠上皮细胞刷状缘微绒毛小根中的肌动蛋白束。
J Cell Biol. 1983 May;96(5):1491-6. doi: 10.1083/jcb.96.5.1491.
5
Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations.在突触后致密物制剂中鉴定血影蛋白为一种主要的钙调蛋白结合蛋白。
J Cell Biol. 1983 Feb;96(2):443-8. doi: 10.1083/jcb.96.2.443.
6
Widespread occurrence of avian spectrin in nonerythroid cells.鸟类血影蛋白在非红细胞中的广泛存在。
Cell. 1982 Jul;29(3):821-33. doi: 10.1016/0092-8674(82)90444-5.
7
Erythrocyte membrane tropomyosin. Purification and properties.红细胞膜原肌球蛋白。纯化及特性
J Biol Chem. 1984 May 10;259(9):5978-89.
8
Erythrocyte spectrin is comprised of many homologous triple helical segments.红细胞血影蛋白由许多同源的三螺旋片段组成。
Nature. 1984;311(5982):177-80. doi: 10.1038/311177a0.
9
Spectrin immunofluorescence distinguishes a population of naturally capped lymphocytes in situ.血影蛋白免疫荧光可在原位区分出一群天然加帽的淋巴细胞。
J Cell Biol. 1984 Jul;99(1 Pt 1):350-5. doi: 10.1083/jcb.99.1.350.
10
Erythrocyte and brain forms of spectrin in cerebellum: distinct membrane-cytoskeletal domains in neurons.小脑红细胞型和脑型血影蛋白：神经元中不同的膜细胞骨架结构域。
Science. 1983 Jun 17;220(4603):1295-6. doi: 10.1126/science.6190228.
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