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Updated: Nov 25, 2025

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
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グルタマートアルギニレーションがα-シヌクレインに及ぼす影響:半合成による異常な翻訳後の改変の研究

Buyan Pan1, Naoki Kamo1,2, Marie Shimogawa1

  • 1Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104, United States.

Journal of the American Chemical Society
|December 18, 2020
PubMed
まとめ

アルファシヌクレイン (αS) の翻訳後の修正 (PTM) であるグルタミン酸アルギニレーションが合成され,研究された. 特定の部位でのアルギニレーションはαSの蓄積を阻害し,パーキンソン病に対する潜在的な神経保護を提供します.

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Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Protein Modifications in the RER

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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Protein Folding Quality Check in the RER

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