Search research articles

お問い合わせ

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 Journal Methods Collections JoVE Encyclopedia of Experiments アーカイブ

教育

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual 教員リソースセンター教員サイト

プライバシーポリシー

関連する概念動画

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein Networks

Protein Networks

Protein Kinases and Phosphatases

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...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Amplifying Signals via Enzymatic Cascade

Amplifying Signals via Enzymatic Cascade

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...

Phosphorylation

Phosphorylation

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...

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

Engineering drug-responsive replication machinery for precise control of self-amplifying RNA.

Nature biomedical engineering·2026

Same author

Promera: a unified model for biomolecular structure prediction, filtering, and design.

bioRxiv : the preprint server for biology·2026

Same author

Evolutionary dynamics under phenotypic uncertainty.

bioRxiv : the preprint server for biology·2026

Same author

Profile of David Baker, Demis Hassabis, and John Jumper: 2024 Nobel laureates in chemistry.

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

Same author

Learning the language of protein-protein interactions.

Nature communications·2026

Same author

Single-cell and spatial profiling highlights TB-induced myofibroblasts as drivers of lung pathology.

The Journal of experimental medicine·2026

Same journal

Erratum for the Research Article "Detecting supramolecular organic nanoparticles during heat wave".

Science (New York, N.Y.)·2026

Same journal

Local signals, systemic decline.

Science (New York, N.Y.)·2026

Same journal

The mechanics of liver regeneration.

Science (New York, N.Y.)·2026

Same journal

Computing in a memory with physics.

Science (New York, N.Y.)·2026

Same journal

Retraction.

Science (New York, N.Y.)·2026

Same journal

Making time.

Science (New York, N.Y.)·2026

関連記事をすべて見る

Search research articles

関連する実験動画

Updated: Oct 30, 2025

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

エンジニアリングされたタンパク質-リン酸化切り替えネットワークと内生ネットワークの発見への影響

Deepak Mishra^1,2,3, Tristan Bepler^3,4,5, Brian Teague⁶

¹Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.

Science (New York, N.Y.)

|July 2, 2021

まとめ

この要約は機械生成です。

研究者はタンパク質のリン酸化を用いて酵母の中で素早く合成可能な切り替えスイッチを設計しましたこの研究はまた,合成生物学と細胞工学を進歩させ,自然に発生する5つの新しいビスタブルな生物学的ネットワークを特定しました.

さらに関連する動画

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

関連する実験動画

Last Updated: Oct 30, 2025

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

科学分野:

合成生物学
分子生物学と細胞生物学
生物化学

背景:

細胞の新しい行動を設計する鍵となるものです細胞の新しい行動を設計する鍵となるものです
既存の規制システムは遅いメカニズムに依存しています
合成生物学的ネットワークは細胞の急速な制御の可能性を秘めています

研究の目的:

タンパク質-タンパク質のリン酸化を用いて,サッカロミセア (Saccharomyces cerevisiae) の合成ビスタブルスイッチを設計する.
内生バイスタブルネットワークを識別するための計算フレームワークを開発する.
新しく発見された内生ビスタブルネットワークを実験的に検証する.

主な方法:

11つのタンパク質-タンパク質リン酸化要素を用いた交差抑制トポロジーを利用した合成の切り替えスイッチの構築.
ビスタブルなネットワークのための内生タンパク質経路の検索のためのコンピューティングフレームワークの開発.
特定された内生ネットワークのビスタビリティの実験的検証

主要な成果:

酵母に超敏感な合成タグリングスイッチを成功裏に作りました状態を数秒で切り替えて長期的なビスタビリティを維持します
ビスタビリティを示す,以前に報告されていない5つの内生生物学的ネットワークを特定し,実験的に検証した.
機能的な生物学的ネットワークを発見するための計算フレームワークの有用性を実証した.

結論:

合成タンパク質ネットワークは複雑な細胞調節のために迅速に設計できます
開発された計算フレームワークは,特定の機能を持つ内生ネットワークの発見に役立ちます.
この研究は生物工学における急速なセンサーと処理システムの設計に基礎を築きます