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相关概念视频

Phosphorylation01:02

Phosphorylation

53.6K
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...
53.6K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

14.9K
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...
14.9K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.3K
4.3K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.6K

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相关实验视频

Updated: Jan 11, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

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信号4.0:2025年更新,重点是酸化数据.

Prisca Lo Surdo1, Marta Iannuccelli2, Klas Karis3

  • 1Department of Biology and Biotechnologies "Charles Darwin", Laboratory affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, La Sapienza University of Rome, Rome 00185, Italy.

Nucleic acids research
|November 17, 2025
PubMed
概括

现在,SIGNOR 4.0数据库提供了增强的信号网络数据,包括一个新的PhosphoSIGNOR接口,用于详细的酸化分析. 这种资源有助于绘制细胞信号的变化和了解疾病机制.

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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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科学领域:

  • 系统生物学 系统生物学
  • 分子生物学分子生物学
  • 生物信息学是一种生物信息学.

背景情况:

  • 信号网络开放资源 (SIGNOR) 是一个手动策划的生物因果相互作用数据库.
  • 信号事件以效应 (激活/非激活) 和机制 (例如酸化) 进行注释.

研究的目的:

  • 为了展示SIGNOR数据库的最新更新 (4.0版本).
  • 介绍 PhosphoSIGNOR,一个专门用于酸化数据的子域.
  • 增强数据策划和扩大信号网络分析的范围.

主要方法:

  • 生物实体之间的因果相互作用的手动策划.
  • 整合文本挖掘工具用于辅助策划.
  • 为酸化数据开发一个专门的用户界面 (PhosphoSIGNOR).
  • 扩大策划工作,重点关注酸化事件.

主要成果:

  • "SIGNOR 4.0"具有改进的策划工具和增加的内容,重点是酸化.
  • PhosphoSIGNOR提供针对性访问和可视化酸化特定信息.
  • 扩展的数据集有助于全面地绘制信号变化及其与细胞过程的联系.

结论:

  • SIGNOR 4.0 和 PhosphoSIGNOR 为探索信号网络提供了一个强大的资源.
  • 该平台支持假设生成和机制性见解,特别是在癌症系统生物学中.
  • 增强的数据可访问性和可视化使研究人员能够理解复杂的细胞信号.