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  2. Unfolded protein response - Wikipedia

    en.wikipedia.org/wiki/Unfolded_protein_response

    The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. [1] It has been found to be conserved between mammalian species, [2] as well as yeast [1] [3] and worm organisms. The UPR is activated in response to an accumulation of unfolded or misfolded proteins in the lumen of the

  3. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Inside cells, the process of folding often begins co-translationally, so that the N-terminus of the protein begins to fold while the C-terminal portion of the protein is still being synthesized by the ribosome; however, a protein molecule may fold spontaneously during or after biosynthesis. [18]

  4. Mitochondrial unfolded protein response - Wikipedia

    en.wikipedia.org/wiki/Mitochondrial_unfolded...

    The mitochondrial unfolded protein response (UPR mt) is a cellular stress response related to the mitochondria. The UPR mt results from unfolded or misfolded proteins in mitochondria beyond the capacity of chaperone proteins to handle them. [1] The UPR mt can occur either in the mitochondrial matrix or in the mitochondrial inner membrane. [1]

  5. Spindle apparatus - Wikipedia

    en.wikipedia.org/wiki/Spindle_apparatus

    It is referred to as the mitotic spindle during mitosis, a process that produces genetically identical daughter cells, or the meiotic spindle during meiosis, a process that produces gametes with half the number of chromosomes of the parent cell. Besides chromosomes, the spindle apparatus is composed of hundreds of proteins.

  6. Protein aggregation - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation

    Misfolded proteins can form protein aggregates or amyloid fibrils, get degraded, or refold back to its native structure. In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly.

  7. Proteasome - Wikipedia

    en.wikipedia.org/wiki/Proteasome

    Proteasomes are part of a major mechanism by which cells regulate the concentration of particular proteins and degrade misfolded proteins. Proteins are tagged for degradation with a small protein called ubiquitin. The tagging reaction is catalyzed by enzymes called ubiquitin ligases. Once a protein is tagged with a single ubiquitin molecule ...

  8. Spindle checkpoint - Wikipedia

    en.wikipedia.org/wiki/Spindle_checkpoint

    Three types of cell division: binary fission (taking place in prokaryotes), mitosis and meiosis (taking place in eukaryotes).. When cells are ready to divide, because cell size is big enough or because they receive the appropriate stimulus, [20] they activate the mechanism to enter into the cell cycle, and they duplicate most organelles during S (synthesis) phase, including their centrosome.

  9. Endoplasmic-reticulum-associated protein degradation - Wikipedia

    en.wikipedia.org/wiki/Endoplasmic-reticulum...

    Because the ubiquitin–proteasome system (UPS) is located in the cytosol, terminally misfolded proteins have to be transported from the endoplasmic reticulum back into cytoplasm. Most evidence suggest that the Hrd1 E3 ubiquitin-protein ligase can function as a retrotranslocon or dislocon to transport substrates into the cytosol.

  1. Related searches where do misfolded proteins go in the water molecule during mitosis and reproduction

    mitochondrial unfolded proteinmitochondrial unfolded protein reaction