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Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells. [PDF]
J Zhejiang Univ Sci BCao H +8 more
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A technique for delineating the unfolding requirements for substrate entry into retrotranslocons during endoplasmic reticulum-associated degradation. [PDF]
J Biol Chem, 2019 Shi J +6 more
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Isolation and characterization of a functionally active protein translocation apparatus from chloroplasts envelopes [PDF]
, 1993 Morré, D. James +2 more
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Endoplasmic Reticulum–Associated Protein Degradation
Cold Spring Harbor Perspectives in Biology, 2022Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated degradation (ERAD). The ERAD process involves the recognition of substrates in the lumen and membrane of the ER, their translocation into the cytosol, ubiquitination, and delivery to the ...
Logesvaran, Krshnan +2 more
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Endoplasmic reticulum-associated protein degradation
Seminars in Cell & Developmental Biology, 2000The quality control system in the endoplasmic reticulum of eukaryotic cells ensures that newly synthesized proteins that fail to fold into the correct conformation or unassembled orphan subunits of oligomeric proteins are rapidly eliminated by proteolytic degradation.
J M, Lord +3 more
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Endoplasmic reticulum-associated protein degradation
2002Proteins that fail to fold properly as well as constitutive or regulated short-lived proteins of the endoplasmatic reticulum (ER) are subjected to proteolysis by cytosolic 26 S proteasomes. This process, termed ER-associated protein degradation (ERAD), has also been implicated in the generation of some important human disorders, for example, cystic ...
Ernst, Jarosch +2 more
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ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION
Annual Review of Cell and Developmental Biology, 2005Secretory and transmembrane proteins enter the secretory pathway through the protein-conducting Sec61 channel in the membrane of the endoplasmic reticulum. In the endoplasmic reticulum, proteins fold, are frequently covalently modified, and oligomerize before they are packaged into transport vesicles that shuttle them to the Golgi complex.
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Endoplasmic Reticulum-associated Protein Degradation in Plant Cells
2006The endoplasmic reticulum is equipped with a quality control function that retains misfolded and unassembled proteins and allows only structurally mature polypeptides to be transported to their final destination. The retained proteins are eventually retro-translocated to the cytosol and destroyed by a process called endoplasmic reticulum-associated ...
Ceriotti A, Roberts LM
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The Endoplasmic Reticulum-Associated Degradation and Disulfide Reductase ERdj5
2011The endoplasmic reticulum (ER) is an organelle where secretory or membrane proteins are correctly folded with the aid of various molecular chaperones and oxidoreductases. Only correctly folded and assembled proteins are enabled to reach their final destinations, which are called as ER quality control (ERQC) mechanisms.
Ryo, Ushioda, Kazuhiro, Nagata
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