morinlab.bib
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+@article{sneeringerCoordinatedActivitiesWildtype2010,
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+ title = {Coordinated Activities of Wild-Type plus Mutant {{EZH2}} Drive Tumor-Associated Hypertrimethylation of Lysine 27 on Histone {{H3}} ({{H3K27}}) in Human {{B-cell}} Lymphomas},
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+ author = {Sneeringer, Christopher J. and Scott, Margaret Porter and Kuntz, Kevin W. and Knutson, Sarah K. and Pollock, Roy M. and Richon, Victoria M. and Copeland, Robert A.},
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+ date = {2010-12-07},
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+ journaltitle = {Proceedings of the National Academy of Sciences of the United States of America},
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+ shortjournal = {Proc Natl Acad Sci U S A},
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+ volume = {107},
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+ number = {49},
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+ eprint = {21078963},
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+ eprinttype = {pmid},
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+ pages = {20980--20985},
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+ issn = {1091-6490},
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+ doi = {10.1073/pnas.1012525107},
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+ abstract = {EZH2, the catalytic subunit of the PRC2 complex, catalyzes the mono- through trimethylation of lysine 27 on histone H3 (H3K27). Histone H3K27 trimethylation is a mechanism for suppressing transcription of specific genes that are proximal to the site of histone modification. Point mutations of the EZH2 gene (Tyr641) have been reported to be linked to subsets of human B-cell lymphoma. The mutant allele is always found associated with a wild-type allele (heterozygous) in disease cells, and the mutations were reported to ablate the enzymatic activity of the PRC2 complex for methylating an unmodified peptide substrate. Here we demonstrate that the WT enzyme displays greatest catalytic efficiency (k(cat)/K) for the zero to monomethylation reaction of H3K27 and diminished efficiency for subsequent (mono- to di- and di- to trimethylation) reactions. In stark contrast, the disease-associated Y641 mutations display very limited ability to perform the first methylation reaction, but have enhanced catalytic efficiency for the subsequent reactions, relative to the WT enzyme. These results imply that the malignant phenotype of disease requires the combined activities of a H3K27 monomethylating enzyme (PRC2 containing WT EZH2 or EZH1) together with the mutant PRC2s for augmented conversion of H3K27 to the trimethylated form. To our knowledge, this is the first example of a human disease that is dependent on the coordinated activities of normal and disease-associated mutant enzymatic function.},
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+ langid = {english},
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+ pmcid = {PMC3000297},
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+ file = {/Users/rmorin/Zotero/storage/QKW38HUB/Sneeringer et al. - 2010 - Coordinated activities of wild-type plus mutant EZ.pdf}
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+}
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@article{fangazioGeneticMechanismsHLAI2021,
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title = {Genetic Mechanisms of {{HLA-I}} Loss and Immune Escape in Diffuse Large {{B}} Cell Lymphoma},
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author = {Fangazio, Marco and Ladewig, Erik and Gomez, Karen and Garcia-Ibanez, Laura and Kumar, Rahul and Teruya-Feldstein, Julie and Rossi, Davide and Filip, Ioan and Pan-Hammarström, Qiang and Inghirami, Giorgio and Boldorini, Renzo and Ott, German and Staiger, Annette M. and Chapuy, Björn and Gaidano, Gianluca and Bhagat, Govind and Basso, Katia and Rabadan, Raul and Pasqualucci, Laura and Dalla-Favera, Riccardo},