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Peptide contributes to the specificity of positive selection of CD8+ T cells in the thymus

Article Abstract:

The residues involved in the interaction with TCRS were altered resulting in the conversion of a nonselecting peptide into a mixture of selecting peptides. Self-peptides were derived from C57 BL/6 and employed in the experiment which revealed that self-peptides influence the properties of CD8+ T cells. Mice lacking in the specific gene which encodes the peptide dealing with antigen processing have been found to have lower levels of MH4 class I molecular and fewer CD8+ T cells.

Author: Ploegh, Hidde L., Schumacher, Ton N.M., Ashton-Rickardt, Philip G., Luc Van Kaer, Susumu Tonegawa
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
Usage, Peptides

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The eS-Sense of -SH in the ER

Article Abstract:

Protein folding and S-S bond formation occur translationally in the endoplasmic reticulum. They are part of the protein primary structure that support the stable folding of proteins, wherein the net formation of the S-S bond is portrayed by mixed disulfide exchanges with oxidized glutathione. Moreover, their chemistry is associated with the development of disulfides that involve electron transfer from two thiols to an acceptor.

Author: Ploegh, Hidde L., Huppa, Johannes B.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Analysis, Genetic aspects, Endoplasmic reticulum, Proteins, Protein structure, Cell research, Cytological research

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The human cytomegalovirus US11 gene product dislocates MHC class 1 heavy chains from the endoplasmic reticulum to the cytosol

Article Abstract:

The human cytomegalovirus destroys cellular mechanisms for signalling T cells to recognize viral attack by preventing the formation of major histocompatibility molecules (MHC). They prevent MHC production by introducing a gene, US11, which causes the cell to displace MHC molecules that are in the endoplasmic reticulum into the cytosol where they are attacked by proteases such as N-glycanase.

Author: Ploegh, Hidde L., Geuze, Hans J., Wiertz, Emmanual J.H.J., Jones, Thomas R., Sun, Lei, Bogyo, Matthew
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Research, Major histocompatibility complex, Cytomegaloviruses, Cytomegalovirus

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