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相关概念视频

C4 Pathway and CAM01:27

C4 Pathway and CAM

49.2K
Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
C4 Pathway
The C4 pathway is used by plants such as...
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

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Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
607
Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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相关实验视频

Updated: Feb 7, 2026

The In ovo CAM-assay as a Xenograft Model for Sarcoma
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The In ovo CAM-assay as a Xenograft Model for Sarcoma

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与Nav1.5通过FGF12A和CaM结合的相互作用.

Lucy Woodbury, Anna Li, Paweorn Angsutararux

    bioRxiv : the preprint server for biology
    |February 6, 2026
    PubMed
    概括

    卡尔莫杜林 (CaM) 和纤维细胞生长因子12A (FGF12A) 以一种依赖的方式与心脏通道 (Nav1.5) 相互作用. 这种相互作用调节Nav1.5无活化,影响心脏动作潜力.

    科学领域:

    • 心血管生理学心血管生理学
    • 分子生物学分子生物学
    • 离子通道功能的功能

    背景情况:

    • 电压关闭的通道 (Nav) 对于动作潜力的启动至关重要.
    • 纳维1.5的无活化是由辅助蛋白调节的,例如模素 (CaM) 和纤维细胞生长因子 (iFGF).
    • 细胞内 ([Ca2+]i) 在调节通过CaM的Nav1.5门的作用受到争议.

    研究的目的:

    • 研究CaM和iFGF12A对Nav1.5无活化的协同作用.
    • 为了确定这种相互作用是否依赖.
    • 为了阐明Nav1.5 CTD:CaM:iFGF12A复合体的体几何学.

    主要方法:

    • 在活细胞中进行光共振能量转移 (FRET) 成像.
    • 观察Nav1.5α亚单元,CaM和iFGF12A之间的相互作用.
    • 在变化的[Ca2+]i下,对Nav1.5的电压依赖性门动力学的比较.

    主要成果:

    • 在静止[Ca2+]i时,2:1的FRET效率表明每Nav1.5 CTD与FGF12A每一个CaM.
    • 增加的[Ca2+]i导致均等的FRET效率,表明CaM:FGF12A:Nav1.5 CTD的比率为2:1:1.

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  • 在FGF12A的存在下,低[Ca2+]i将Nav1.5的稳定状态无活化转向超极化.
  • 结论:

    • FGF12A:CaM复合体以依赖的方式调节Nav1.5的稳定状态无活化.
    • 这种依赖的机制允许FGF12A调节Nav1.5的不活化.
    • 生物冗余存在,以保持Nav1.5在没有CaM的情况下保持失活稳定性.