The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol
Emmanuel J. H. J. Wiertz,Thomas R. Jones,Lei Sun,Matthew Bogyo,Hans J. Geuze,Hidde L. Ploegh +5 more
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TLDR
Human cytomegalovirus (HCMV) down-regulates expression of MHC class I products by selective proteolysis by encodes an endoplasmic reticulum resident type-I transmembrane glycoprotein, which dislocates newly synthesized class I molecules from the ER to the cytosol, where they are acted upon by an N-glycanase and the proteasome.About:
This article is published in Cell.The article was published on 1996-03-08 and is currently open access. It has received 1085 citations till now. The article focuses on the topics: MHC class I & Transporter associated with antigen processing.read more
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The Ubiquitin System
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
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NATURAL KILLER CELLS IN ANTIVIRAL DEFENSE: Function and Regulation by Innate Cytokines
TL;DR: A detailed picture is developing of particular innate cytokines activating NK cell responses and their consorted effects in providing unique endogenous milieus promoting downstream adaptive responses, most beneficial in defense against viral infections.
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Aggresomes: A Cellular Response to Misfolded Proteins
TL;DR: The intracellular fate of cystic fibrosis transmembrane conductance regulator (CFTR) is investigated and it is demonstrated that undegraded CFTR molecules accumulate at a distinct pericentriolar structure which is termed the aggresome.
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The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
TL;DR: In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway, and the 26S proteasome is a 2-MDa molecular machine built from approximately 31 different subunits, which catalyzes protein degradation.
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Ubiquitin-dependent protein degradation
TL;DR: A growing number of cellular regulatory mechanisms are being linked to protein modification by the polypeptide ubiquitin, including key transitions in the cell cycle, class I antigen processing, signal transduction pathways, and receptor-mediated endocytosis.
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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
Kenneth L. Rock,Colette F. Gramm,Lisa Rothstein,Karen Clark,Ross L. Stein,Lawrence Dick,Daniel Hwang,Alfred L. Goldberg +7 more
TL;DR: Peptide aldehydes that inhibit major peptidase activities of the 20S and 26S proteasomes are shown to reduce the degradation of protein and ubiquitinated protein substrates by 26S particles.
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Inhibition of Proteasome Activities and Subunit-Specific Amino-Terminal Threonine Modification by Lactacystin
Gabriel Fenteany,Robert F. Standaert,William S. Lane,Soongyu Choi,E. J. Corey,Stuart L. Schreiber +5 more
TL;DR: Lactacystin appears to modify covalently the highly conserved amino-terminal threonine of the mammalian proteasome subunit X (also called MB1), a close homolog of the LMP7 proteasom subunit encoded by the major histocompatibility complex and may have a catalytic role.
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Degradation of CFTR by the ubiquitin-proteasome pathway
TL;DR: It is shown that the degradation of both wild-type and mutant CFTR is inhibited by two potent proteasome inhibitors that induce the accumulation of polyubiquitinated forms of immature CFTR, confirming that ubiquitination is required for rapid CFTR degradation.
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Antigen Recognition by Class I-Restricted T Lymphocytes
and A Townsend,Helen C. Bodmer +1 more
TL;DR: The work discussed here offers a unified view of T-cell recognition and suggests that class-I and class-II molecules have a closely related function in the presentation of peptides to T lymphocytes.
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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
Timothy J. Jensen,Melinda A. Loo,Steven Pind,David B. Williams,Alfred L. Goldberg,John R. Riordan +5 more
TL;DR: It is shown that this ER degradation is sensitive to inhibitors of the cytosolic proteasome, including lactacystin and certain peptide aldehydes, which completely blocks the ATP-dependent conversion of the wild-type precursor to the native folded form that enables escape from degradation.