ubiquitination

简明释义

英[juːˌbɪkwɪtɪˈneɪʃən]美[juˌbɪkwɪtəˈneɪʃən]

n. 泛素化；遍在蛋白化（作用）

英英释义

单词用法

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例句

1.The recent data indicating that some TRIM proteins are implicated in ubiquitination, as a novel class of RING finger ubiquitin E3 ligases.

最近的一些研究显示TRIM家族可能是一类新的RING指泛素连接酶。

2.Ubiquitination plays important roles in regulating diverse cellular process in plants, including perception and signal transduction of various hormone and external environmental signals.

泛素化在细胞生命活动的许多进程中发挥着至关重要的作用，其中包括激素信号和极端环境信号的感受和传导。

3.Research studies suggest that activated E2 associates transiently with E3, and the dissociation is a critical step for ubiquitination (4).

研究表明，激活的E2与E3迅速结合然后分离是一个关键步骤（4）。

4.The degradation of AUX/IAA protein by ubiquitination plays essential role in auxin response, and the interaction between ARF and AUX/IAA protein regulates the transcription of auxin-response genes.

IAA蛋白的泛素化降解在生长素反应中发挥关键性作用，ARF和AUX/IAA蛋白相互作用调节生长素响应基因的转录。

5.The degradation of AUX/IAA protein by ubiquitination plays essential role in auxin response, and the interaction between ARF and AUX/IAA protein regulates the transcription of auxin-response genes.

IAA蛋白的泛素化降解在生长素反应中发挥关键性作用，ARF和AUX/IAA蛋白相互作用调节生长素响应基因的转录。

6.Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26s proteasome.

泛素能与许多细胞蛋白共价连接，并被26s蛋白酶降解。

7.The process of ubiquitination is essential for protein degradation in cells.

在细胞中，泛素化过程对于蛋白质降解至关重要。

8.Defects in the ubiquitination process can lead to various diseases.

在泛素化过程中出现缺陷可能导致各种疾病。

9.The enzyme responsible for ubiquitination is called ubiquitin ligase.

负责泛素化的酶称为泛素连接酶。

10.Researchers are studying how ubiquitination affects cell signaling pathways.

研究人员正在研究泛素化如何影响细胞信号通路。

11.In cancer research, ubiquitination plays a critical role in tumor suppression.

在癌症研究中，泛素化在肿瘤抑制中起着关键作用。

作文

Ubiquitination is a critical biological process that plays a vital role in regulating various cellular functions. In essence, it is the attachment of a small protein called ubiquitin to a target protein, which can lead to different outcomes depending on the context. The term 'ubiquitination' refers to this modification process, where ubiquitin tags proteins for degradation, alters their cellular location, or modifies their activity. Understanding ubiquitination (泛素化) is essential for comprehending how cells maintain homeostasis and respond to environmental changes.The process of ubiquitination (泛素化) involves a series of enzymatic reactions that can be divided into three main steps: activation, conjugation, and ligation. First, ubiquitin is activated by an enzyme called E1, which forms a high-energy thioester bond with ubiquitin. Next, the activated ubiquitin is transferred to a conjugating enzyme known as E2. Finally, the E3 ligase enzyme facilitates the transfer of ubiquitin from E2 to the target protein, resulting in the formation of an isopeptide bond between ubiquitin and the lysine residue of the target protein. This intricate mechanism ensures that the right proteins are modified at the right time, highlighting the importance of ubiquitination (泛素化) in cellular regulation.One of the most well-known functions of ubiquitination (泛素化) is its role in the proteasomal degradation pathway. When a protein is tagged with multiple ubiquitin molecules, it is recognized by the 26S proteasome, a large proteolytic complex responsible for degrading unneeded or damaged proteins. This selective degradation is crucial for maintaining protein homeostasis within the cell, allowing for the removal of misfolded proteins and the regulation of various signaling pathways.Moreover, ubiquitination (泛素化) is not solely associated with protein degradation. It also plays a significant role in regulating protein activity and localization. For instance, some proteins may undergo monoubiquitination, where only one ubiquitin molecule is attached. This modification can alter the protein's function, influencing processes such as DNA repair, endocytosis, and immune responses. Additionally, polyubiquitination, characterized by the attachment of a chain of ubiquitin molecules, can dictate the fate of the target protein, determining whether it will be degraded or involved in other cellular processes.The study of ubiquitination (泛素化) has profound implications for understanding various diseases, including cancer, neurodegenerative disorders, and infectious diseases. Dysregulation of the ubiquitin-proteasome system can lead to the accumulation of harmful proteins, contributing to disease progression. For example, in many cancers, abnormal expression of E3 ligases can result in the improper degradation of tumor suppressor proteins, promoting uncontrolled cell growth. Furthermore, research into ubiquitination (泛素化) pathways has opened new avenues for therapeutic interventions, with drugs targeting specific components of the ubiquitin system showing promise in preclinical studies.In conclusion, ubiquitination (泛素化) is a fundamental biological process that underpins many aspects of cellular function. Its role in protein degradation, activity modulation, and localization highlights its significance in maintaining cellular homeostasis. As our understanding of ubiquitination (泛素化) continues to evolve, it holds the potential to unveil novel therapeutic targets for a range of diseases, ultimately advancing our knowledge of cellular biology and medicine.

泛素化是一个关键的生物过程，在调节各种细胞功能中发挥着重要作用。实质上，它是将一种称为泛素的小蛋白附加到目标蛋白上的过程，这可能根据具体情况导致不同的结果。术语“泛素化”指的是这一修饰过程，其中泛素标记蛋白以进行降解，改变其细胞位置或修改其活性。理解ubiquitination（泛素化）对于理解细胞如何维持稳态和响应环境变化至关重要。泛素化的过程涉及一系列酶促反应，可以分为三个主要步骤：激活、结合和连接。首先，泛素通过一种称为E1的酶被激活，形成与泛素的高能硫酯键。接下来，活化的泛素被转移到称为E2的结合酶。最后，E3连接酶促进泛素从E2转移到目标蛋白，导致泛素与目标蛋白的赖氨酸残基之间形成异肽键。这一复杂机制确保了在合适的时间对合适的蛋白进行修饰，突显了泛素化在细胞调节中的重要性。泛素化最著名的功能之一是其在蛋白质降解途径中的作用。当一个蛋白被多个泛素分子标记时，它会被26S蛋白酶体识别，26S蛋白酶体是一个大型蛋白水解复合体，负责降解不需要或损伤的蛋白。这种选择性降解对于维持细胞内的蛋白质稳态至关重要，允许去除错误折叠的蛋白质并调节各种信号通路。此外，泛素化不仅仅与蛋白质降解相关。它在调节蛋白质活性和定位方面也发挥着重要作用。例如，一些蛋白可能经历单泛素化，即只附加一个泛素分子。这种修饰可以改变蛋白的功能，影响DNA修复、内吞作用和免疫反应等过程。此外，聚泛素化的特征是附加一条泛素分子链，可以决定目标蛋白的命运，决定其是否会被降解或参与其他细胞过程。对泛素化的研究对理解各种疾病有深远的影响，包括癌症、神经退行性疾病和传染病。泛素-蛋白酶体系统的失调可能导致有害蛋白的积累，从而促进疾病的进展。例如，在许多癌症中，E3连接酶的异常表达可能导致肿瘤抑制蛋白的不当降解，从而促进细胞的无控制生长。此外，对泛素化途径的研究开启了新的治疗干预途径，针对泛素系统特定组分的药物在临床前研究中显示出希望。总之，泛素化是一个基本的生物过程，支撑着细胞功能的许多方面。它在蛋白质降解、活性调节和定位中的作用突显了其在维持细胞稳态中的重要性。随着我们对泛素化的理解不断发展，它有潜力揭示一系列疾病的新治疗靶点，最终推动我们对细胞生物学和医学的认识。