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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
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Related Experiment Video

Updated: Sep 16, 2025

Investigating Bacterial-Fungal Interactions using Fungal Highway Columns in Diverse Environments and Substrates
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Correction to "Exploring Bioactive Fungal RiPPs: Advances, Challenges, and Future Prospects"

Qiuyue Nie1,2, Chunxiao Sun1,2, Shuai Liu1,2

  • 1Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

Biochemistry
|July 9, 2025
PubMed
Summary

No abstract available in PubMed .

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