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

Mismatch Repair01:36

Mismatch Repair

Overview
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
DNA Helicases00:55

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...

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

J-domain proteins: from molecular mechanisms to diseases.

Cell stress & chaperones·2025
Same author

The Use of Small Molecules to Correct Defects in CFTR Folding, Maturation, and Channel Activity.

Current chemical biology·2025
Same author

Type I Hsp40s/DnaJs aggregates exhibit features reminiscent of amyloidogenic structures.

The FEBS journal·2024
Same author

Novel functions of the ER-located Hsp40s DNAJB12 and DNAJB14 on proteins at the outer mitochondrial membrane under stress mediated by CCCP.

Molecular and cellular biochemistry·2023
Same author

DNAJB12 and Hsp70 Mediate Triage of Misfolded Membrane Proteins for Proteasomal versus Lysosomal Degradation.

Autophagy reports·2023
Same author

Specification of Hsp70 Function by Hsp40 Co-chaperones.

Sub-cellular biochemistry·2022

相关实验视频

Updated: May 7, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

交换核酸,调整 Hsp70 的调整.

Douglas M Cyr1

  • 1Department of Cell and Developmental Biology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. dmcyr@med.unc.edu

Cell
|June 17, 2008
PubMed
概括
此摘要是机器生成的。

新的晶体结构揭示了热冲击蛋白70 (Hsp70) 如何与其核酸交换因子 (NEF) Hsp110.0相互作用. 这些发现澄清了NEF行动是如何指导Hsp70的.

更多相关视频

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Tuning Degradation to Achieve Specific and Efficient Protein Depletion
05:11

Tuning Degradation to Achieve Specific and Efficient Protein Depletion

Published on: July 20, 2019

相关实验视频

Last Updated: May 7, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Tuning Degradation to Achieve Specific and Efficient Protein Depletion
05:11

Tuning Degradation to Achieve Specific and Efficient Protein Depletion

Published on: July 20, 2019

科学领域:

  • 分子生物学分子生物学
  • 蛋白质的生物化学 蛋白质的生物化学
  • 结构生物学是结构生物学.

背景情况:

  • 分子伴侣,包括热冲击蛋白70 (Hsp70),对于适当的蛋白质折叠和细胞功能至关重要.
  • 热冲击蛋白110 (Hsp110) 作为Hsp70的核酸交换因子 (NEF),调节其活性.
  • 了解Hsp70和NEF之间的相互作用对于破译伴侣介导蛋白质平衡至关重要.

研究的目的:

  • 阐明Hsp70-Hsp110相互作用的结构基础.
  • 提供关于NEF活动如何指定Hsp70细胞功能的机制性见解.
  • 在原子层面提供Hsp70-NEF复合物的详细视图.

主要方法:

  • 采用X射线晶体学,确定了Hsp70与Hsp110.0复合的三维结构.
  • 对Hsp70-Hsp110复合物的比较结构分析.

主要成果:

  • 确定了与Hsp110复合的Hsp70的晶体结构.
  • 这些结构揭示了Hsp70及其NEF,Hsp110.0之间的精确原子相互作用.
  • 这些结构数据为理解NEF介导的Hsp70调节机制提供了基础.

结论:

  • 晶体结构为Hsp70-Hsp110陪伴机械提供了前所未有的洞察力.
  • 这些发现提升了我们对NEF作用如何决定Hsp70在细胞过程中的作用的理解.
  • 这项研究为未来对陪伴者功能和功能障碍的调查提供了一个结构框架.