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Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing

Article Abstract:

Protein disulfide isomerase (PDI), an enzyme critical for correct protein disulfide bond formation, functions as part of the peptide-loading complex to control optimal peptide loading by regulating the redox state of disulfide bonds in the MHC peptide-binding groove. These findings reveal a mechanism by which thiol-based redox reactions regulate antigen processing and presentation.

Author: Boyoun Park, Sungwook Lee, Eukyung Kim, Kwangmin Cho, Riddell, Stanley R., Sunglim Cho, Kwangseog Ahn
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Peptides, Antigens

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Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen

Article Abstract:

A high-resolution structures(~1.9 angstrom) of large tumor antigen (LTag) hexamers in distinct nucleotide binding states is determined to understand the way in which ATP binding and hydrolysis are coupled to conformational changes. The LTag of simian virus 40 an AAA+ protein is a hexameric helicase essential for viral DNA replication in eukaryotic cells.

Author: Li, Dawei, Zhao, Rui, Gai, Dahai, Chen, Xiaojiang S., Finkielstein, carla V.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
Biological Product (except Diagnostic) Manufacturing, Nucleic Acid Derivatives, Nucleotides, DNA replication

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The human tumor antigen PRAME is a dominant repressor of retinoic acid receptor signaling

Article Abstract:

PRAME is identified as a ligand-dependent corepressor of retinoic acid receptor signaling (RAR). It is suggested that overexpression of PRAME frequently observed in human cancers confer growth or survival advantages by antagonizing RAR signaling.

Author: Bernards, Rene, Epping, Mirjam T., Wang, Liming, Edel, Michael J., Carlee, Leone, Hernandez, Maria
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
Cancer, Cancer genetics, Tretinoin

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Subjects list: Research, Protein binding, Tumor antigens, Tumour antigens
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