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相关概念视频

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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MAPK Signaling Cascades01:07

MAPK Signaling Cascades

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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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相关实验视频

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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PhosX:从蛋白学实验中推断数据驱动的激酶活性.

Alessandro Lussana1, Sophia Müller-Dott2, Julio Saez-Rodriguez1,2

  • 1European Bioinformatics Institute, European Molecular Biology Laboratory, Wellcome Genome Campus, Hinxton CB10 1SD, United Kingdom.

Bioinformatics (Oxford, England)
|November 20, 2024
PubMed
概括
此摘要是机器生成的。

PhosX是一种新的计算方法,可以从蛋白质组学数据中推断酶活性. 它使用基质序列特异性准确识别激酶活性的变化,优于现有的方法.

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相关实验视频

Last Updated: Jun 7, 2025

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科学领域:

  • 生物化学 生物化学
  • 计算生物学 计算生物学
  • 蛋白质组学是指蛋白质组学.

背景情况:

  • 从蛋白质组学上推断酶活性对于理解信号通路和识别药物点至关重要.
  • 目前的方法受到手工策划的酶-基质关联数据库的限制.

研究的目的:

  • 用实验确定的基质序列特异性开发一种可靠的方法来估计差异性激酶活性.
  • 解决酶活性推断现有方法的局限性.

主要方法:

  • PhosX将统计丰富分析与酶基质序列特异性信息相结合.
  • 该方法利用蛋白质序列和强度变化从蛋白质组学数据.

主要成果:

  • PhosX能够准确地识别上调和下调的激酶.
  • 该方法优于依赖已知的酶-基质关联的当前方法.
  • PhosX的性能与先进的方法相提并论,这些方法使用了对激酶-基质关联的先前知识.

结论:

  • PhosX提供了一种数据驱动的方法来推断酶活性.
  • 该方法提高了对信号机制的理解,并有助于识别潜在的药物点.
  • 建议使用PhosX来从蛋白质组学数据中推断酶活性.