Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

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...

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
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
Same journal

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026
Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026
Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026
Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026
Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
関連記事をすべて見る

関連する実験動画

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

核酸を交換し,Hsp70をチューニングする.

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
まとめ
この要約は機械生成です。

新しい結晶構造は,熱ショックタンパク質70 (Hsp70) がその核酸交換因子 (NEF) Hsp110.0とどのように相互作用するかを明らかにしています. これらの発見は,NEFの行動がHsp70をどのように指向するかを明らかにしています.

さらに関連する動画

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

関連する実験動画

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

科学分野:

  • 分子生物学は分子生物学である.
  • タンパク質の生化学
  • 構造生物学 構造生物学とは

背景:

  • 熱ショックタンパク質70 (Hsp70) を含む分子チャペロンは,適切なタンパク質の折りたたみと細胞機能に不可欠です.
  • 熱ショックタンパク質110 (Hsp110) は,Hsp70の核酸交換因子 (NEF) として作用し,その活性を調節する.
  • Hsp70とNEFの相互作用を理解することは,チャペロン媒介タンパク質ホメオスタシスの解読に不可欠です.

研究 の 目的:

  • Hsp70-Hsp110相互作用の構造的基礎を解明する.
  • NEFの活動がHsp70の細胞機能をどのように規定するかについてのメカニズム的洞察を提供するために.
  • 原子レベルでのHsp70-NEF複合体の詳細な見方を提供するために.

主な方法:

  • X線結晶学を用いて,Hsp70とHsp110.0の複合体内の3次元構造を決定した.
  • Hsp70-Hsp110複合体の比較構造分析について.

主要な成果:

  • Hsp110と複合したHsp70の結晶構造が決定されました.
  • これらの構造は,Hsp70とそのNEF,Hsp110.0との間の正確な原子相互作用を明らかにします.
  • 構造データは,NEF媒介によるHsp70規制の仕組みを理解するための基礎を提供します.

結論:

  • 結晶構造は,Hsp70-Hsp110のシェパロン機構に前例のない洞察を提供しています.
  • これらの発見は,NEFの作用が細胞プロセスにおけるHsp70の役割をどのように支配するかを理解する上で前進しています.
  • この研究は,シャパロン機能と機能不全に関する将来の調査のための構造的枠組みを提供します.