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1
Cargo-activated ATPase activity of kinesin.驱动蛋白的货物激活ATP酶活性。
Biophys J. 1995 Apr;68(4 Suppl):283S-284S; discussion 285S.
2
Pathway of the microtubule-kinesin ATPase.微管-驱动蛋白ATP酶的途径。
Biophys J. 1995 Apr;68(4 Suppl):173S-176S; discussion 176S-179S.
3
Pathway of processive ATP hydrolysis by kinesin.驱动蛋白进行性ATP水解的途径。
Nature. 1995 Feb 23;373(6516):671-6. doi: 10.1038/373671a0.
4
Implications of diffusion-controlled limit for processivity of dimeric kinesin head domains.扩散控制极限对二聚体驱动蛋白头部结构域持续运动性的影响。
Biophys J. 1995 Apr;68(4 Suppl):267S-269S; discussion 269S-270S.
5
High-resolution tracking of microtubule motility driven by a single kinesin motor.由单个驱动蛋白马达驱动的微管运动的高分辨率追踪
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6
Chemomechanical cycle of kinesin differs from that of myosin.驱动蛋白的化学机械循环与肌球蛋白的不同。
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7
Kinesin hydrolyses one ATP per 8-nm step.驱动蛋白每移动8纳米水解一个ATP。
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8
Bovine brain kinesin is a microtubule-activated ATPase.牛脑驱动蛋白是一种微管激活的ATP酶。
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9
Evidence that the 116 kDa component of kinesin binds and hydrolyzes ATP.驱动蛋白116 kDa组分结合并水解ATP的证据。
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10
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.驱动蛋白每水解一个三磷酸腺苷(ATP)会移动8纳米的距离。
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Synthesis, physicochemical characterisation and biological activity of anandamide/ɛ-polycaprolactone nanoparticles obtained by electrospraying.电喷射法制备大麻素/ɛ-聚己内酯纳米粒及其理化性质和生物活性。
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High-Resolution Imaging of a Single Gliding Protofilament of Tubulins by HS-AFM.高分辨率成像的单个滑行原丝的微管蛋白由 HS-AFM。
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Single molecule FRET observation of kinesin-1's head-tail interaction on microtubule.单分子荧光共振能量转移技术观察驱动蛋白-1在微管上的头尾相互作用
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Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation.动力蛋白结合蛋白作为衔接分子,在物质形成过程中连接驱动蛋白 5 及其货物参与小泡运输。
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Regulation of a heterodimeric kinesin-2 through an unprocessive motor domain that is turned processive by its partner.通过一个非运行的马达结构域来调节异二聚体的动力蛋白-2,该马达结构域在其伴侣的作用下变成运行的。
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A peptide zipcode sufficient for anterograde transport within amyloid precursor protein.一个足以在淀粉样前体蛋白内进行顺行运输的肽邮政编码。
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Single fungal kinesin motor molecules move processively along microtubules.单个真菌驱动蛋白运动分子沿微管持续移动。
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本文引用的文献

1
Direct observation of kinesin stepping by optical trapping interferometry.通过光镊干涉测量法直接观察驱动蛋白的步移。
Nature. 1993 Oct 21;365(6448):721-7. doi: 10.1038/365721a0.
2
Preparation of tubulin from brain.从大脑中制备微管蛋白。
Methods Enzymol. 1982;85 Pt B:376-85. doi: 10.1016/0076-6879(82)85038-6.
3
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility.鉴定一种参与基于微管运动的新型力产生蛋白——驱动蛋白。
Cell. 1985 Aug;42(1):39-50. doi: 10.1016/s0092-8674(85)80099-4.
4
Correlation between the ATPase and microtubule translocating activities of sea urchin egg kinesin.海胆卵驱动蛋白的ATP酶活性与微管转运活性之间的相关性。
Nature. 1987;328(6126):160-3. doi: 10.1038/328160a0.
5
The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate.用改良孔雀绿法测定无机磷酸盐研究肌球蛋白和亚片段-1水解ATP时最初的磷酸盐释放。
J Biochem. 1986 May;99(5):1465-72. doi: 10.1093/oxfordjournals.jbchem.a135616.
6
Kinesin undergoes a 9 S to 6 S conformational transition.驱动蛋白经历从9 S到6 S的构象转变。
J Biol Chem. 1992 Apr 25;267(12):8696-701.
7
Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range.0.1至5纳摩尔范围内无机磷和有机磷的测定。
Anal Biochem. 1975 Feb;63(2):607-13. doi: 10.1016/0003-2697(75)90388-7.
8
An improved assay for nanomole amounts of inorganic phosphate.一种用于检测纳摩尔量无机磷酸盐的改进测定法。
Anal Biochem. 1979 Nov 15;100(1):95-7. doi: 10.1016/0003-2697(79)90115-5.

驱动蛋白的货物激活ATP酶活性。

Cargo-activated ATPase activity of kinesin.

作者信息

Jiang M Y, Sheetz M P

机构信息

Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.

出版信息

Biophys J. 1995 Apr;68(4 Suppl):283S-284S; discussion 285S.

PMID:7787091
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1281948/
Abstract

We have measured the ATPase activity of squid optic lobe kinesin bound to polystyrene beads in the presence of microtubules. We find that there is a substantial increase (> 10-fold) in the microtubule-activated ATPase activity for bead-bound kinesin over free kinesin. We tentatively attribute such cargo-activated ATPase activity to the presence of a self-inhibited form of kinesin in solution, which becomes activated when bound to a bead in the presence of alpha-casein. Further experiments are underway to unravel this phenomenon and, in addition, to associate the traveling distance of beads with the observed ATPase rate to determine the average number of ATP consumed per kinesin-bead per micron of travel along microtubule.

摘要

我们测量了在微管存在的情况下,与聚苯乙烯珠结合的鱿鱼视叶驱动蛋白的ATP酶活性。我们发现,与游离驱动蛋白相比,珠结合的驱动蛋白的微管激活ATP酶活性有显著增加(>10倍)。我们初步将这种货物激活的ATP酶活性归因于溶液中存在一种自我抑制形式的驱动蛋白,当在α-酪蛋白存在的情况下与珠子结合时,它会被激活。进一步的实验正在进行中,以揭示这一现象,此外,将珠子的移动距离与观察到的ATP酶速率联系起来,以确定每微米沿微管移动的驱动蛋白-珠子消耗的ATP平均数量。