Skip to main content
뒤로

Protein Degradation definitions

컨트롤 버튼이 '내비게이션' 모드로 변경되었습니다.
1/15
  • Proteasome
    Multi-subunit cylindrical complex that unfolds and degrades ubiquitin-tagged proteins into short peptides using ATP.
  • Ubiquitin
    Small, 76-amino acid protein found in all eukaryotes, used to tag proteins for selective degradation.
  • E1 Enzyme
    Catalyst responsible for activating ubiquitin in the initial step of the ubiquitin-proteasome pathway.
  • E2 Enzyme
    Conjugating enzyme that binds activated ubiquitin and collaborates with E3 ligase for protein tagging.
  • E3 Ligase
    Protein responsible for recognizing specific substrates and attaching ubiquitin to target proteins.
  • Polyubiquitination
    Attachment of multiple ubiquitin molecules to a protein, signaling it for proteasomal degradation.
  • Lysosome
    Membrane-bound organelle containing proteases that degrade proteins and other cellular components.
  • Protease
    Enzyme that catalyzes the breakdown of proteins into amino acids or peptides within degradation pathways.
  • Autophagy
    Cellular process involving lysosomal degradation of cytoplasmic components, especially during stress or starvation.
  • Degradation Signal
    Hidden or exposed sequence within a protein that marks it for destruction when revealed.
  • Peptide
    Short chain of amino acids produced as an intermediate during protein breakdown.
  • Protein Aggregation
    Accumulation of misfolded proteins in the cell, potentially leading to dysfunction or disease.
  • Homeostasis
    Cellular state maintained by regulated protein levels through controlled degradation mechanisms.
  • Misfolded Protein
    Abnormally structured polypeptide that can disrupt cellular function if not efficiently degraded.
  • Amino Acid
    Basic building block released from proteins during lysosomal or proteasomal degradation.