Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Allosteric Regulation01:08

Allosteric Regulation

57.8K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
57.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
The Two-State Receptor Model01:29

The Two-State Receptor Model

1.9K
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with...
1.9K
Drug-Receptor Interaction: Antagonist01:28

Drug-Receptor Interaction: Antagonist

2.8K
An antagonist is a drug that binds strongly to a receptor without activating it. An antagonist prevents other molecules, such as neurotransmitters or hormones, from binding to the receptor and triggering a cellular response. Such interaction effectively hinders the normal physiological processes mediated by the receptor, resulting in various pharmacological effects depending on the specific receptor targeted.
Antagonists can be classified as competitive or noncompetitive based on their...
2.8K
Combined Effects of Drugs: Antagonism01:30

Combined Effects of Drugs: Antagonism

8.4K
The combined effects of drugs can result in various interactions, of which an important type is antagonism. Antagonism is a mechanism where one drug inhibits or counteracts the effects of another drug. Antagonism can occur through various means, including receptor binding, allosteric modulation, functional interaction, chemical reactions, and pharmacokinetic processes.
The most common type is receptor antagonism, where one drug acts as an antagonist to block the effects of another drug by...
8.4K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

2.0K
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.0K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Synthetic Approaches to the New Drugs Approved During 2024.

Journal of medicinal chemistry·2026
Same author

The effects of micronutrients on the risk of upper gastrointestinal diseases: a two-sample Mendelian randomization study.

European journal of nutrition·2026
Same author

Discovery of an ITK and TRK kinase inhibitor for the potential topical treatment of atopic dermatitis.

Nature communications·2026
Same author

Do Amino-Oxetanes Resemble Amides? A Matched Molecular Pairs Property and Structural Comparison.

Journal of medicinal chemistry·2026
Same author

Advances in Therapeutic Antibody Discovery and Development Targeting G Protein-Coupled Receptors.

Pharmacology research & perspectives·2026
Same author

The Concise Guide to PHARMACOLOGY 2025/26: G protein-coupled receptors.

British journal of pharmacology·2025
Same journal

Demonstration of a quantum C-NOT gate in a time-multiplexed fully reconfigurable photonic processor.

Nature communications·2026
Same journal

Nonlinear quantum light source with van der Waals ferroelectric NbOX<sub>2</sub> (X = Br, I).

Nature communications·2026
Same journal

Antagonistic histone H2A variants and autonomous heterochromatin formation shape epigenomic patterns in Arabidopsis.

Nature communications·2026
Same journal

The long tail of nitrate pollution in groundwater challenges governance of global water quality.

Nature communications·2026
Same journal

Select microbial metabolites promote tau aggregation in a murine tauopathy model.

Nature communications·2026
Same journal

Warming climate has lengthened global intense tropical cyclone seasons.

Nature communications·2026
查看所有相关文章

相关实验视频

Updated: Jun 14, 2025

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

8.9K

通过全osteric 抗剂调节 CCR6 的结构基础.

David Jonathan Wasilko1, Brian S Gerstenberger2, Kathleen A Farley1

  • 1Discovery Sciences, Medicine Design, Pfizer Inc., Groton, CT, USA.

Nature communications
|August 31, 2024
PubMed
概括
此摘要是机器生成的。

研究人员确定了CC化学因子受体6 (CCR6) 与新型抗体结合的非活性结构. 这揭示了小分子如何阻断受体激活,为治疗炎症疾病提供了新的途径.

更多相关视频

A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4
06:56

A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4

Published on: March 10, 2018

13.6K
High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

11.8K

相关实验视频

Last Updated: Jun 14, 2025

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

8.9K
A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4
06:56

A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4

Published on: March 10, 2018

13.6K
High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

11.8K

科学领域:

  • 结构生物学是结构生物学.
  • 药理学 药理学是指药理学的学科.
  • 免疫学 免疫学 免疫学

背景情况:

  • CC化学因子受体6 (CCR6) 是慢性炎症疾病的关键标.
  • 以前的研究阐明了与CCL20结合的活性CCR6结构,详细说明了受体激活机制.

研究的目的:

  • 为了呈现不活跃的CCR6结构与新型全抗体复合.
  • 通过小分子阐明CCR6对抗性的分子基础.
  • 在对抗剂结合时探索CCR6内部的全osteric通信.

主要方法:

  • 使用X射线结晶学测定了CCR6的三元结构,使用对抗剂SQA1/OXM1和SQA1/OXM2.
  • 生物物理技术被用来描述对手的结合和构成状态.
  • 计算建模被用来评估溶液中的形状偏好.

主要成果:

  • 解决了两个截然不同的非活性CCR6结构,复杂化与氧态素 (OXM1,OXM2) 和胺 (SQA1) 衍生物.
  • 反抗剂结合到单独的细胞外和细胞内口袋,破坏受体激活网络.
  • 在两个对抗剂结合部位之间观察到最小的全osteric 通信,挑战了传统的 GPCR 合作模式.

结论:

  • 小分子可以通过通过不同的结合口袋稳定不活跃的构造来有效地对抗CCR6.
  • 这些发现提供了对CCR6全抗性的结构性见解,补充了对受体激活的知识.
  • 这项工作支持开发针对CCR6的新疗法,用于治疗炎症疾病.