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相关概念视频

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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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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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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相关实验视频

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Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
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当热 (pytosis) 与棕 (itoylation) 相遇时

Lu Jiang1, Zirui Wang1, Ting Xu2

  • 1Department of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan, Shandong 250013, China; Department of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, Shandong 250117, China; Medical Science and Technology Innovation Center, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, Shandong 250117, China.

Cytokine & growth factor reviews
|March 12, 2024
PubMed
概括

蛋白质棕化调节热致死,这是一个关键的免疫过程. 这种修改会影响诸如cGAS,NLRP3,STING,GSDMD和NOD等关键蛋白质,影响炎症和细胞死亡途径.

关键词:
GSDMDMD的总体发展目标是什么在NLRP3中,NLRP3是NLRP3中的一个.cGAS 是一个气体.棕细胞代谢的发生热致灭 (pyroptosis) 是一种致的过程.

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Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
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相关实验视频

Last Updated: Jul 1, 2025

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
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Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
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科学领域:

  • 免疫学 免疫学 免疫学
  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学

背景情况:

  • 热是免疫反应中关键的编程细胞死亡途径.
  • 蛋白质棕化,即脂肪酸添加到氨酸残留物中,越来越被认为是细胞过程的关键调节者.
  • 烧的失调与各种炎症性疾病和感染有关.

研究的目的:

  • 审查蛋白质棕化在调节参与热的关键蛋白质中的重要作用.
  • 阐明棕化如何影响与热致死相关的蛋白质功能和下游信号传递的机制.
  • 突出棕化对免疫反应和炎症的影响.

主要方法:

  • 关于蛋白质棕化和热的最近研究的文献综述.
  • 分析特定的棕化位点及其对蛋白质功能的影响 (例如,cGAS,NLRP3,STING,GSDMD,NOD1/2).
  • 整合研究结果,以全面概述棕甲基化在热灭菌调节中的作用.

主要成果:

  • 特定ZDHHC酶的棕化调节了cGAS,NLRP3和STING的活性和局部化.
  • GSDMD和GSDME的棕化对于烧灭的执行至关重要,包括孔隙形成和膜转移.
  • NOD1和NOD2的棕化会影响它们的免疫信号通路,以应对细菌刺激.

结论:

  • 蛋白质棕化是一种关键的翻译后修改,可以微调热灭.
  • 了解这些棕化事件为免疫调节和炎症疾病的潜在治疗点提供了洞察力.
  • 需要进一步的研究来澄清相互矛盾的发现,例如ZDHHC5在NLRP3棕化中的作用.