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iNew Medicine, EarlyView.ABSTRACT Human papillomavirus (HPV) is a double‐stranded DNA virus that infects human skin and mucosal tissues exclusively. The German scientist Harald zur Hausen was awarded the 2008 Nobel Prize in Physiology or Medicine for his discovery of the link between HPV infection and cervical cancer.
Fang Zhu +5 more
wiley +1 more source
Adss1–HDAC3 Interaction: A Novel Mechanism for Epigenetic Regulation of Metabolism in Adipose Tissue
iNew Medicine, EarlyView.ABSTRACT Obesity and its related metabolic disorders have emerged as global public health challenges with underlying mechanisms involving an imbalance between energy storage and expenditure in the adipose tissue. In recent years, with the deepening research on adipose tissue metabolism, the cross talk between metabolic enzymes and epigenetic regulation
Jiarui Zhao +3 more
wiley +1 more source
TorsinA participates in endoplasmic reticulum-associated degradation [PDF]
Nature Communications, 2011 TorsinA is an AAA+ ATPase located within the lumen of the endoplasmic reticulum and nuclear envelope, with a mutant form causing early onset torsion dystonia (DYT1). Here we report a new function for torsinA in endoplasmic reticulum-associated degradation (ERAD).
Xandra Breakefield +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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IRE1α is an endogenous substrate of endoplasmic-reticulum-associated degradation [PDF]
Nature Cell Biology, 2015 Endoplasmic reticulum (ER)-associated degradation (ERAD) represents a principle quality control mechanism to clear misfolded proteins in the ER; however, its physiological significance and the nature of endogenous ERAD substrates remain largely unexplored.
John R Yates +2 more
exaly +3 more sources
Endoplasmic reticulum-associated protein degradation
Seminars in Cell and 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.
Lorenzo Frigerio +2 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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Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation [PDF]
Seminars in Cell and Developmental Biology, 2007 Endoplasmic reticulum-associated degradation (ERAD) represents the primary means of quality control within the secretory pathway. Critical to this process are ubiquitin protein ligases (E3s) which, together with ubiquitin conjugating enzymes (E2s), mediate the ubiquitylation of proteins targeted for degradation from the ER.
Yien Che Tsai +2 more
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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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