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

PCR01:32

PCR

Overview
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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

Structure and mechanism of inhibition of lysine demethylase 2A (KDM2A) by compound 183c.

Communications chemistry·2026
Same author

Structural Transformation of a BRAF Inhibitor into a Selective PKR Inhibitor.

Journal of medicinal chemistry·2026
Same author

The molecular glue CLEO4-88 inhibits the ACAA1 thiolase by induced binding to GID4.

Nature chemical biology·2026
Same author

Discovery and development of potent and selective dual NUAK/MARK inhibitors as Hippo pathway modulators for the treatment of cancer.

European journal of medicinal chemistry·2026
Same author

Design of a Targeted Covalent Probe to Interrogate the DNA Polymerase Activity of Polθ.

ACS medicinal chemistry letters·2026
Same author

A Chemical-Genetic Interaction Matrix Reveals Drug Mechanism and Genetic Architecture.

bioRxiv : the preprint server for biology·2026

関連する実験動画

Updated: Jul 6, 2026

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

Plk1のポーロ試合でした.

Genie C Leung1, Frank Sicheri

  • 1Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario, M5G 1X5, Canada.

Cell
|October 9, 2003
PubMed
まとめ
この要約は機械生成です。

研究者らは,ポロドメインがフォスフォペプチドを認識する方法を明らかにした. このドメインは,キナーゼを特定の細胞部位に誘導し,タンパク質キナーゼの触媒ドメインを調節する二重の役割を持っています.

さらに関連する動画

Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases
09:13

Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases

Published on: November 22, 2024

A Bilingual Computational Workflow for Identifying Potential PLK1 Inhibitors in American Sign Language and English
14:34

A Bilingual Computational Workflow for Identifying Potential PLK1 Inhibitors in American Sign Language and English

Published on: April 3, 2026

関連する実験動画

Last Updated: Jul 6, 2026

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases
09:13

Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases

Published on: November 22, 2024

A Bilingual Computational Workflow for Identifying Potential PLK1 Inhibitors in American Sign Language and English
14:34

A Bilingual Computational Workflow for Identifying Potential PLK1 Inhibitors in American Sign Language and English

Published on: April 3, 2026

科学分野:

  • 分子生物学は分子生物学である.
  • 細胞シグナリング
  • タンパク質の生化学

背景:

  • ポロドメインは,細胞信号伝達経路において極めて重要です.
  • その基板認識メカニズムを理解することは,キナーゼ調節を解読する鍵です.

研究 の 目的:

  • ポロドメインによるフォスフォペプチド認識の分子基礎を解明する.
  • キナーゼ活性と局所化におけるポロドメインの二重機能を調査する.

主な方法:

  • ポロドメインの構造を決定する構造生物学技術.
  • フォスフォペプチド結合を評価するための生化学的測定法.
  • キナーゼターゲティングを追跡するための細胞局所化研究.

主要な成果:

  • この研究は,ポロドメインによるフォスホペプチド結合のための特定の分子相互作用を明らかにしています.
  • ポロドメインがキナーゼをサブセルラー部位に誘導する役割を実証した.
  • 隣接する触媒ドメインに対するポロドメインの自己抑制効果を示した.

結論:

  • ポーロドメインは,キナーゼ活性と,フォスホペプチド認識による局所化の重要な調節体として作用する.
  • この二重機能は,信号伝達経路の正確な時空制御を保証する.