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

Phosphorylation01:02

Phosphorylation

53.3K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
53.3K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

9.9K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
9.9K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

16.5K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
16.5K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

14.5K
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...
14.5K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.2K
4.2K
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

3.6K
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
3.6K

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

<i>NRAS</i> mRNA-Degrading Bifunctional Small Molecules Induce Diverse Cellular Morphological Changes in Cancer Cells.

JACS Au·2026
Same author

Anti-CRISPR-mediated continuous directed evolution of CRISPR-Cas9 in human cells.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Proximity-Induced Rewiring of Oncogenic Kinase Triggers Apoptosis.

ACS central science·2026
Same author

Discovery of molecular glues that bind FKBP12 and structurally distinct targets using DNA-encoded libraries.

Nature communications·2026
Same author

Pyrazolylpyrimidinamines Decorated via Petasis Reaction as Small-Molecule Activators of the RNA-Degrading Ribonuclease IRE1α.

ACS bio & med chem Au·2026
Same author

A Scalable Design for Proximity-Inducing Molecules.

bioRxiv : the preprint server for biology·2026
Same journal

Gas-Responsive Metal-Organic Frameworks for Adaptive Thermal Energy Storage with Tunable Charge-Discharge Temperatures.

Journal of the American Chemical Society·2026
Same journal

Engineering a Thiamine-Dependent Benzoylformate Decarboxylase for Stereodivergent Radical C(sp<sup>3</sup>)-C(sp<sup>3</sup>) Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Accelerated Directional Proton-Coupled Electron Transfer Enabled by Intrinsic Dipole Field in Biomimetic α-Helical Structure.

Journal of the American Chemical Society·2026
Same journal

Alternating Current-Driven Hydrogen Isotope Labeling of Aliphatic Amines Using 1,3-Propanedithiol as an Efficient Hydrogen Atom Transfer Reagent.

Journal of the American Chemical Society·2026
Same journal

Two-Dimensional van der Waals Polar Metal MoOBr<sub>2</sub>.

Journal of the American Chemical Society·2026
Same journal

Negatively Curved Chiral Bilayer Nanographene.

Journal of the American Chemical Society·2026
関連記事をすべて見る

関連する実験動画

Updated: Dec 12, 2025

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries
08:49

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Published on: January 22, 2019

9.4K

リン酸化誘導キメリック小分子

Sachini U Siriwardena1,2, Dhanushka N P Munkanatta Godage1,2, Veronika M Shoba1,2

  • 1Chemical Biology and Therapeutics Science, Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02142, United States.

Journal of the American Chemical Society
|August 14, 2020
PubMed
まとめ
この要約は機械生成です。

リン酸化誘導キメリック小分子 (PHICS) と呼ばれる新しい二機能小分子は,標的タンパク質をリン酸化するためにキナーゼを勧誘することができる. このアプローチにより,研究および治療上の応用のために,タンパク質のリン酸化に対する新しい制御が可能になります.

さらに関連する動画

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

19.2K
Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

6.5K

関連する実験動画

Last Updated: Dec 12, 2025

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries
08:49

Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries

Published on: January 22, 2019

9.4K
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

19.2K
Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

6.5K

科学分野:

  • 化学生物学
  • 分子生物学
  • 薬物の発見

背景:

  • 小粒子は伝統的に酵素の活動を阻害します.
  • 新興戦略では,近接効果を通じて新しい酵素機能を誘導するために小さな分子を利用します.
  • タンパク質のリン酸化は,タンパク質の構造と機能を変化させる重要な規制メカニズムです.

研究 の 目的:

  • 標的タンパク質のリン酸化を誘導する新しい小分子を開発する.
  • キナーゼ活性を制御する技術的近接の可能性を調査する.
  • 基礎研究と医学における これらの分子の有用性を探求する.

主な方法:

  • リン酸化誘導キメリック小分子 (PHICS) の設計と合成
  • PHICSは,特定のキナーゼと標的タンパク質のための小分子結合剤をリンクします.
  • キナーゼ活性とタンパク質のリン酸化を測定するための開発試験.

主要な成果:

  • PHICSは,非基板タンパク質のリン酸化にAMPKとPKCを成功させた.
  • 投与量依存,時間制御,および近接依存のリン酸化が実証されています.
  • 細胞におけるBRD4の誘導されたネイティブおよび新リン酸化と,シグナル関連ブルトンチロシンキナーゼのリン酸化.

結論:

  • PHICSは,標的型タンパク質のリン酸化のための新しい二機能分子のクラスを表しています.
  • この技術は,ネイティブおよびネオフォスフォリレーションイベントの正確な制御を可能にします.
  • PHICS媒介によるリン酸化は,生物学的研究と治療戦略を前進させるのに重要な可能性を秘めています.