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These flashcards cover key terms and concepts related to protein folding and quality control in the Rough Endoplasmic Reticulum as discussed in the lecture.
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ERAD
ER Associated protein Degradation, a quality-control pathway in the Rough Endoplasmic Reticulum.
Chaperone proteins
Proteins that assist in the proper folding of other proteins in the ER.
Glycosylation
The addition of sugar molecules to proteins, which is crucial for their folding and function.
UPR
Unfolded Protein Response, a cellular response to the accumulation of misfolded proteins in the ER.
Calreticulin
A multifunctional chaperone in the ER that aids in protein folding and quality control.
UGGT
A protein folding sensor that adds glucose to misfolded proteins, allowing them to refold.
Proteasome
A large protein complex that degrades unneeded or misfolded proteins.
Retrotranslocon
The channel through which misfolded proteins are transported back into the cytosol for degradation.
Ubiquitinylation
A process where ubiquitin molecules are attached to a protein, marking it for degradation.
Disulfide bonds
Covalent bonds that stabilize protein structure, formed between cysteine residues.