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相关概念视频

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...

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相关实验视频

Updated: Jul 18, 2026

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
12:20

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends

Published on: March 15, 2014

微管通过依赖ATP的AAA酶卡塔宁的Oligomerization进行微管分解.

J J Hartman1, R D Vale

  • 1The Howard Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.

Science (New York, N.Y.)
|October 26, 1999
PubMed
概括

卡塔尼尼尼 在卡塔尼尼尼

科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学

背景情况:

  • 卡坦因是一种AAA腺三酸酶 (ATPase) 酶,可以分解微管.
  • 通过AAA酶分解蛋白质复合物的精确机制尚未完全理解.

研究的目的:

  • 为了研究卡塔宁介导的微管分解的机制.
  • 了解卡塔宁寡合化在其功能中的作用.

主要方法:

  • 使用光共振能量转移 (FRET) 试验来研究卡塔宁p60子单元的寡合化.
  • 测量ATPase活性和微管结合亲和力.

主要成果:

  • 卡坦因p60亚单元的寡合化取决于腺三酸盐 (ATP) 和微管.
  • 氧化增强了卡塔宁对微管的亲和力,并刺激了其ATPase活性.
  • 通过寡合化卡塔宁对ATP的水解导致微管的分解和卡塔宁单体的解离.

结论:

  • 卡坦因利用核酸依赖的寡合化循环来拆解微管.
  • 这种将寡合化合到目标分解的机制可能在ATP-化AAA域中很常见.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
10:19

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

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相关实验视频

Last Updated: Jul 18, 2026

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
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Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
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Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

Published on: January 24, 2025