Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Drugs that Stabilize Microtubules01:15

Drugs that Stabilize Microtubules

2.1K
Microtubules are dynamic structures that undergo cycles of catastrophe and rescue. The microtubules play a central role in cell division by forming the spindle apparatus for segregating the chromosomes. This makes them ideal targets for regulating dividing cells in tumors and malignant cancer cells. Microtubule stabilizing drugs help stabilize the microtubule formation and promote its polymerization. Paclitaxel was the first microtubule stabilizing agent used as anticancer drug in chemotherapy...
2.1K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

4.4K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
4.4K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.

Science advances·2026
Same author

A functional amyloid scaffold shapes insect egg coats.

bioRxiv : the preprint server for biology·2026
Same author

Reverse-engineering amyloid strains with generative protein design.

bioRxiv : the preprint server for biology·2026
Same author

Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.

Research square·2026
Same author

Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.

bioRxiv : the preprint server for biology·2026
Same author

A repeat expansion in GOLGA8A is a major risk factor for atypical frontotemporal lobar degeneration with ubiquitin-positive inclusions.

Nature genetics·2026

相关实验视频

Updated: Jul 25, 2025

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
12:31

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

15.1K

DnaJC7 特别调节了 tau 的播种.

Valerie Ann Perez1, David W Sanders1, Ayde Mendoza-Oliva1

  • 1Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, United States.

eLife
|June 30, 2023
PubMed
概括
此摘要是机器生成的。

J域蛋白DnaJC7特别结合tau,防止神经退行性疾病中的有毒蛋白质聚合. 它的J域对刺激Hsp70活动至关重要,突出了病调节的关键机制.

关键词:
在 DnaJC7 中使用.J域蛋白质是J域蛋白质的组成部分.氨基化物 氨基化物生物化学 生物化学陪伴者 (chaperones) 是指一个陪伴者.化学生物学 化学生物学人类 人类 人类 人类 人类 人类 人类神经科学 神经科学播种播种 播种播种知道的 知道的 知道的

更多相关视频

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
05:51

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

6.0K
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

18.4K

相关实验视频

Last Updated: Jul 25, 2025

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
12:31

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

15.1K
An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
05:51

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

6.0K
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

18.4K

科学领域:

  • 神经生物学 神经生物学 神经生物学
  • 分子生物学分子生物学
  • 蛋白质生物化学 蛋白质生物化学

背景情况:

  • 神经退行性陶病是由于有毒的陶蛋白积累而产生的.
  • 像Hsp70s和J域蛋白 (JDPs) 这样的伴侣蛋白调节蛋白质折叠,包括tau.
  • 参与协调tau折叠和聚合的具体JDP在很大程度上是未知的.

研究的目的:

  • 研究JDPs在调节细胞内聚的作用.
  • 为了确定DnaJC7与tau的相互作用是特定的还是其他JDP共享的.
  • 阐明DnaJC7抑制陶聚合的机制.

主要方法:

  • 在细胞模型中进行蛋白质组学分析,以识别与相互作用的蛋白质.
  • 细胞测试以评估JDP淘汰对tau聚合和播种的影响.
  • 位点定向突变发生,以评估DnaJC7的J域和基质结合位点的功能重要性.

主要成果:

  • 发现DnaJC7与不溶性合物共同净化,并与合物同位化.
  • 淘汰DnaJC7导致总体清除降低,细胞内种植增加.
  • 在DnaJC7的J域或基质结合部位的突变取消了其对tau聚合的保护功能.

结论:

  • DnaJC7 通过与 Hsp70.0 的合作,专门调节 tau 聚合.
  • DnaJC7的J域对于刺激Hsp70 ATPase活性至关重要,这对其抗聚合功能至关重要.
  • 与疾病相关的DnaJC7突变损害了它调节陶聚合的能力,这表明它是一个潜在的治疗标.