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関連する概念動画

Protein Networks02:26

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 Networks02:26

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,...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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関連する実験動画

Updated: Jul 2, 2026

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

C. elegans の早期胚形成のためのタンパク質領域ベースのインタラクトームネットワーク.

Mike Boxem1, Zoltan Maliga, Niels Klitgord

  • 1Center for Cancer Systems Biology and Department of Cancer Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA. mboxem@partners.org

Cell
|August 12, 2008
PubMed
まとめ

研究者は,モジュールドメインに焦点を当ててタンパク質の相互作用をマッピングし,C. elegansの発達のためにより完全なインタラクトームネットワークを作成しました. このドメインベースのアプローチは,細胞の組織と機能に関する新しい洞察を提供します.

さらに関連する動画

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging
12:15

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

Published on: October 3, 2017

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
07:22

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

関連する実験動画

Last Updated: Jul 2, 2026

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging
12:15

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

Published on: October 3, 2017

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
07:22

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

科学分野:

  • 分子生物学は分子生物学である.
  • システム生物学 システム生物学
  • 発達生物学 発達生物学とは

背景:

  • タンパク質とタンパク質の相互作用は,細胞機能にとって極めて重要です.
  • 既存のインタラクトームネットワークは,タンパク質のモジュラードメイン組織をしばしば無視しています.
  • ドメイン媒介の相互作用を理解することは,複雑な生物学的ネットワークの解読の鍵です.

研究 の 目的:

  • タンパク質相互作用ドメインを特定するための実験戦略を開発する.
  • C. elegansの早期胚性タンパク質のためのドメインベースのインタラクトームネットワークを構築する.
  • インタラクトームモデリングを通じて,C. elegansのセンターソーム機能に関する洞察を明らかにする.

主な方法:

  • タンパク質相互作用ドメインを効率的に特定するための新しい実験戦略を開発しました.
  • C. elegansの早期胚細胞分裂からのタンパク質を使用して,ドメインベースのインタラクトームネットワークを生成しました.
  • 200以上のタンパク質の最小相互作用領域を特定しました.

主要な成果:

  • 200以上のタンパク質の相互作用ドメインを成功裏に特定し,ドメインベースの相互作用をマッピングしました.
  • 開発されたアプローチは2つのハイブリッドシステムの感受性を高め,より包括的なインタラクトームにつながった.
  • ドメインベースのインタラクトームネットワークは,C. elegansのセンターソーム機能に関する新しい洞察を提供しました.

結論:

  • タンパク質のモジュール性は,タンパク質とタンパク質の相互作用とネットワークの組織を理解するために重要です.
  • 開発されたドメインベースのインタラクトームモデリング戦略は,様々な生物学的プロセスに有効かつ適用可能です.
  • このアプローチは,インタラクトームの研究を前進させ,C. elegansや他の生物に関する将来の研究のための基盤を提供します.