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相关概念视频

¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Spindle Assembly02:50

Spindle Assembly

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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...
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相关实验视频

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Origami Inspired Self-assembly of Patterned and Reconfigurable Particles
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p14ARF在与NPM1相隔时形成中等尺度组件.

Eric Gibbs1, Qi Miao1, Mylene Ferrolino1

  • 1Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.

Nature communications
|November 11, 2024
PubMed
概括
此摘要是机器生成的。

核蛋白NPM1通过形成凝状网络来稳定瘤抑制剂p14ARF. 这种NPM1-p14ARF相互作用调节核细胞应激反应并减少细胞增殖,为癌症抑制机制提供了洞察力.

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ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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科学领域:

  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学
  • 生物化学 生物化学

背景情况:

  • 核蛋白NPM1是一种参与核糖体生物发生,核糖体应激反应和瘤抑制的核细胞陪伴者.
  • NPM1调节p14替代阅读框架 (p14ARF) 瘤抑制蛋白,抑制MDM2,稳定p53,并在致癌性压力下停止细胞循环.
  • 在正常情况下,NPM1稳定核细胞中的p14ARF,防止p53的激活.

研究的目的:

  • 阐明NPM1调节p14的结构机制.
  • 了解NPM1介导的p14ARF调节如何影响细胞核功能和细胞过程.

主要方法:

  • 对p14ARF-NPM1复合物的结构分析.
  • 研究分子间接触和疏水相互作用在复杂形成中的作用.
  • 评估NPM1-p14ARF组件对核分裂和细胞增殖的影响.

主要成果:

  • 通过与NPM1.1相隔,ARF通过相隔形成一种凝状的中等尺度网络.
  • 在p14ARF的部分折叠的N端区域内的分子间疏水接触介导了这种组合.
  • 这种相位分离增强了p14ARF的核定位,限制了NPM1的扩散,并减少了细胞的增殖.

结论:

  • NPM1通过促进p14ARF阶段分离和组装成一个中等尺度网络,充当一个陪伴者.
  • 这种机制将p14ARF的部分折叠和核细胞定位与其调节细胞增殖和应激反应的功能联系在一起.
  • 这些发现为NPM1在核细胞生物学和瘤抑制中的多方面的作用提供了结构性的见解.