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

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Micelles01:30

Micelles

Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...

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

An emergent disease-associated motor neuron state precedes cell death in ALS.

Cell·2026
Same author

Mutant SOD1 expressed by oligodendrocytes aggregates in myelinic nanochannels and accelerates disease progression in familial ALS mice.

bioRxiv : the preprint server for biology·2026
Same author

Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration.

Science (New York, N.Y.)·2026
Same author

Statins and genetic inhibition of the mevalonate pathway activate an ATF3-STMN2 regenerative program.

bioRxiv : the preprint server for biology·2026
Same author

Protein-only centromeric chromatin assembly streamlines human artificial chromosome formation.

bioRxiv : the preprint server for biology·2026
Same author

Human CRAMP1 specifically promotes the expression of histone H1 genes.

EMBO reports·2026
Same journal

Keep the Hubble and James Webb Space Telescopes alive - the science is worth the price tag.

Nature·2026
Same journal

Say hello to hard helium.

Nature·2026
Same journal

How to avoid dementia - what the science really says.

Nature·2026
Same journal

Save Hubble: the race to preserve the space telescope kicks off.

Nature·2026
Same journal

How long can humans live? All evidence points to a maximum of 125 years.

Nature·2026
Same journal

Listen to Gen Z when it comes to AI in education.

Nature·2026
関連記事をすべて見る

関連する実験動画

Updated: Jun 18, 2026

Improved Generation of Induced Cardiomyocytes Using a Polycistronic Construct Expressing Optimal Ratio of Gata4, Mef2c and Tbx5
10:05

Improved Generation of Induced Cardiomyocytes Using a Polycistronic Construct Expressing Optimal Ratio of Gata4, Mef2c and Tbx5

Published on: November 13, 2015

セントロメリッククロマチンの生成のための構造的決定因子

Ben E Black1, Daniel R Foltz, Srinivas Chakravarthy

  • 1Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, California 92093, USA.

Nature
|July 30, 2004
PubMed
まとめ
この要約は機械生成です。

セントロメア同一性は,固体核細胞を形成するユニークなヒストン変異体,CENP-A (セントロメアタンパク質A) によって維持されます. この構造的性質は,CENP-Aによって授与されています.

さらに関連する動画

CAPRRESI: Chimera Assembly by Plasmid Recovery and Restriction Enzyme Site Insertion
07:37

CAPRRESI: Chimera Assembly by Plasmid Recovery and Restriction Enzyme Site Insertion

Published on: June 25, 2017

Cardiac Muscle-cell Based Actuator and Self-stabilizing Biorobot - PART 1
11:22

Cardiac Muscle-cell Based Actuator and Self-stabilizing Biorobot - PART 1

Published on: July 11, 2017

関連する実験動画

Last Updated: Jun 18, 2026

Improved Generation of Induced Cardiomyocytes Using a Polycistronic Construct Expressing Optimal Ratio of Gata4, Mef2c and Tbx5
10:05

Improved Generation of Induced Cardiomyocytes Using a Polycistronic Construct Expressing Optimal Ratio of Gata4, Mef2c and Tbx5

Published on: November 13, 2015

CAPRRESI: Chimera Assembly by Plasmid Recovery and Restriction Enzyme Site Insertion
07:37

CAPRRESI: Chimera Assembly by Plasmid Recovery and Restriction Enzyme Site Insertion

Published on: June 25, 2017

Cardiac Muscle-cell Based Actuator and Self-stabilizing Biorobot - PART 1
11:22

Cardiac Muscle-cell Based Actuator and Self-stabilizing Biorobot - PART 1

Published on: July 11, 2017

科学分野:

  • 細胞生物学 細胞生物学
  • エピジェネティクス エピジェネティクス
  • 染色体生物学について

背景:

  • 染色体分離に不可欠なセントロメアには,哺乳類の定義されたDNA配列がない.
  • 機能性セントロメアは,ヒストンH3の変異体であるCENP-A (セントロメアタンパク質A) の存在によって特徴付けられます.

研究 の 目的:

  • 核細胞を含むCENP-Aの構造的性質を調査する.
  • CENP-Aのセントロメア標的と機能の構造的基盤を特定する.

主な方法:

  • デウテリウム交換/質量スペクトロメトリー
  • 水力動力学的測定は,水力動力学的測定である.
  • ヒストン変異体置換実験

主要な成果:

  • CENP-AとヒストンH4は,H3/H4テトラメールと比較して,よりコンパクトで頑丈なサブ核体テトラメールを形成します.
  • CENP-Aの特定の領域が,この凝縮と硬化に責任があります.
  • このドメインをヒストンH3に置き換えるだけで,それをセントロメアに誘導するのに十分です.

結論:

  • CENP-A核分子のユニークな構造的硬さは,特定のセントロメアターゲットドメインによって与えられます.
  • この硬さは,セントロメアアイデンティティの確立と維持に重要な役割を果たしている可能性が高い.
  • CENP-Aの構造特性は,適切な染色体分離を確保する機能の鍵です.