Search Results - "Meiners, Matthew J"

The histone mark H3K36me2 recruits DNMT3A and shapes the intergenic DNA methylation landscape by Weinberg, Daniel N., Papillon-Cavanagh, Simon, Chen, Haifen, Yue, Yuan, Chen, Xiao, Rajagopalan, Kartik N., Horth, Cynthia, McGuire, John T., Xu, Xinjing, Nikbakht, Hamid, Lemiesz, Agata E., Marchione, Dylan M., Marunde, Matthew R., Meiners, Matthew J., Cheek, Marcus A., Keogh, Michael-Christopher, Bareke, Eric, Djedid, Anissa, Harutyunyan, Ashot S., Jabado, Nada, Garcia, Benjamin A., Li, Haitao, Allis, C. David, Majewski, Jacek, Lu, Chao

“…Enzymes that catalyse CpG methylation in DNA, including the DNA methyltransferases 1 (DNMT1), 3A (DNMT3A) and 3B (DNMT3B), are indispensable for mammalian…”
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Nucleosome conformation dictates the histone code by Marunde, Matthew R, Fuchs, Harrison A, Burg, Jonathan M, Popova, Irina K, Vaidya, Anup, Hall, Nathan W, Weinzapfel, Ellen N, Meiners, Matthew J, Watson, Rachel, Gillespie, Zachary B, Taylor, Hailey F, Mukhsinova, Laylo, Onuoha, Ugochi C, Howard, Sarah A, Novitzky, Katherine, McAnarney, Eileen T, Krajewski, Krzysztof, Cowles, Martis W, Cheek, Marcus A, Sun, Zu-Wen, Venters, Bryan J, Keogh, Michael-C, Musselman, Catherine A

“…Histone post-translational modifications (PTMs) play a critical role in chromatin regulation. It has been proposed that these PTMs form localized 'codes' that…”
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Examining the Roles of H3K4 Methylation States with Systematically Characterized Antibodies by Shah, Rohan N., Grzybowski, Adrian T., Cornett, Evan M., Johnstone, Andrea L., Dickson, Bradley M., Boone, Brandon A., Cheek, Marcus A., Cowles, Martis W., Maryanski, Danielle, Meiners, Matthew J., Tiedemann, Rochelle L., Vaughan, Robert M., Arora, Neha, Sun, Zu-Wen, Rothbart, Scott B., Keogh, Michael-Christopher, Ruthenburg, Alexander J.

“…Histone post-translational modifications (PTMs) are important genomic regulators often studied by chromatin immunoprecipitation (ChIP), whereby their locations…”
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Separation and Characterization of Endogenous Nucleosomes by Native Capillary Zone Electrophoresis–Top-Down Mass Spectrometry by Jooß, Kevin, Schachner, Luis F, Watson, Rachel, Gillespie, Zachary B, Howard, Sarah A, Cheek, Marcus A, Meiners, Matthew J, Sobh, Amin, Licht, Jonathan D, Keogh, Michael-Christopher, Kelleher, Neil L

“…We report a novel platform [native capillary zone electrophoresis–top-down mass spectrometry (nCZE–TDMS)] for the separation and characterization of whole…”
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Decoding the protein composition of whole nucleosomes with Nuc-MS by Schachner, Luis F., Jooß, Kevin, Morgan, Marc A., Piunti, Andrea, Meiners, Matthew J., Kafader, Jared O., Lee, Alexander S., Iwanaszko, Marta, Cheek, Marcus A., Burg, Jonathan M., Howard, Sarah A., Keogh, Michael-Christopher, Shilatifard, Ali, Kelleher, Neil L.

“…Current proteomic approaches disassemble and digest nucleosome particles, blurring readouts of the ‘histone code’. To preserve nucleosome-level information, we…”
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A trivalent nucleosome interaction by PHIP/BRWD2 is disrupted in neurodevelopmental disorders and cancer by Morgan, Marc A J, Popova, Irina K, Vaidya, Anup, Burg, Jonathan M, Marunde, Matthew R, Rendleman, Emily J, Dumar, Zachary J, Watson, Rachel, Meiners, Matthew J, Howard, Sarah A, Khalatyan, Natalia, Vaughan, Robert M, Rothbart, Scott B, Keogh, Michael-C, Shilatifard, Ali

“…Mutations in the chromatin regulator cause the human neurodevelopmental disorder Chung-Jansen syndrome, while alterations in expression are linked to cancer…”
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Quantification of citrullinated histones: Development of an improved assay to reliably quantify nucleosomal H3Cit in human plasma by Thålin, Charlotte, Aguilera, Katherina, Hall, Nathan W., Marunde, Matthew R., Burg, Jonathan M., Rosell, Axel, Daleskog, Maud, Månsson, Maja, Hisada, Yohei, Meiners, Matthew J., Sun, Zu‐Wen, Whelihan, Matthew F., Cheek, Marcus A., Howard, Sarah A., Saxena‐Beem, Shruti, Noubouossie, Denis F., Key, Nigel S., Sheikh, Saira Z., Keogh, Michael‐Christopher, Cowles, Martis W., Lundström, Staffan, Mackman, Nigel, Wallén, Håkan, Johnstone, Andrea L.

“…Background Recent data propose a diagnostic and prognostic capacity for citrullinated histone H3 (H3Cit), a marker of neutrophil extracellular traps (NETs), in…”
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The UvrD303 Hyper-helicase Exhibits Increased Processivity by Meiners, Matthew J., Tahmaseb, Kambiz, Matson, Steven W.

“…DNA helicases use energy derived from nucleoside 5′-triphosphate hydrolysis to catalyze the separation of double-stranded DNA into single-stranded…”
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An acetylation-mediated chromatin switch governs H3K4 methylation read-write capability by Jain, Kanishk, Marunde, Matthew R, Burg, Jonathan M, Gloor, Susan L, Joseph, Faith M, Poncha, Karl F, Gillespie, Zachary B, Rodriguez, Keli L, Popova, Irina K, Hall, Nathan W, Vaidya, Anup, Howard, Sarah A, Taylor, Hailey F, Mukhsinova, Laylo, Onuoha, Ugochi C, Patteson, Emily F, Cooke, Spencer W, Taylor, Bethany C, Weinzapfel, Ellen N, Cheek, Marcus A, Meiners, Matthew J, Fox, Geoffrey C, Namitz, Kevin E W, Cowles, Martis W, Krajewski, Krzysztof, Sun, Zu-Wen, Cosgrove, Michael S, Young, Nicolas L, Keogh, Michael-Christopher, Strahl, Brian D

“…In nucleosomes, histone N-terminal tails exist in dynamic equilibrium between free/accessible and collapsed/DNA-bound states. The latter state is expected to…”
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Structural basis of histone H2A lysine 119 deubiquitination by Polycomb repressive deubiquitinase BAP1/ASXL1 by Thomas, Jonathan F, Valencia-Sánchez, Marco Igor, Tamburri, Simone, Gloor, Susan L, Rustichelli, Samantha, Godínez-López, Victoria, De Ioannes, Pablo, Lee, Rachel, Abini-Agbomson, Stephen, Gretarsson, Kristjan, Burg, Jonathan M, Hickman, Allison R, Sun, Lu, Gopinath, Saarang, Taylor, Hailey F, Sun, Zu-Wen, Ezell, Ryan J, Vaidya, Anup, Meiners, Matthew J, Cheek, Marcus A, Rice, William J, Svetlov, Vladimir, Nudler, Evgeny, Lu, Chao, Keogh, Michael-Christopher, Pasini, Diego, Armache, Karim-Jean

“…Histone H2A lysine 119 (H2AK119Ub) is monoubiquitinated by Polycomb repressive complex 1 and deubiquitinated by Polycomb repressive deubiquitinase complex…”
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A chemical probe targeting the PWWP domain alters NSD2 nucleolar localization by Dilworth, David, Hanley, Ronan P., Ferreira de Freitas, Renato, Allali-Hassani, Abdellah, Zhou, Mengqi, Mehta, Naimee, Marunde, Matthew R., Ackloo, Suzanne, Carvalho Machado, Raquel Arminda, Khalili Yazdi, Aliakbar, Owens, Dominic D. G., Vu, Victoria, Nie, David Y., Alqazzaz, Mona, Marcon, Edyta, Li, Fengling, Chau, Irene, Bolotokova, Albina, Qin, Su, Lei, Ming, Liu, Yanli, Szewczyk, Magdalena M., Dong, Aiping, Kazemzadeh, Sina, Abramyan, Tigran, Popova, Irina K., Hall, Nathan W., Meiners, Matthew J., Cheek, Marcus A., Gibson, Elisa, Kireev, Dmitri, Greenblatt, Jack F., Keogh, Michael-C., Min, Jinrong, Brown, Peter J., Vedadi, Masoud, Arrowsmith, Cheryl H., Barsyte-Lovejoy, Dalia, James, Lindsey I., Schapira, Matthieu

“…Nuclear receptor-binding SET domain-containing 2 (NSD2) is the primary enzyme responsible for the dimethylation of lysine 36 of histone 3 (H3K36), a mark…”
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Abstract 4728: Biochemical and genomic approaches for high throughput drug discovery in chromatin remodeling research by Sun, Lu, Willis, Hannah, Marunde, Matthew R., Kumary, Vishnu U., Meiners, Matthew J., Gopinath, Saarang, Burg, Jonathan M., Venters, Bryan J., Hickman, Allison, Sun, Zu-Wen, Cowles, Martis W., Esteve, Pierre, Chin, Hang Gyeong, Ponnaluri, Chaithanya, Pradhan, Sriharsa, Keogh, Michael-Christopher

“…Abstract Chromatin remodeling is mediated by ATP-dependent enzymes that play key roles regulating gene expression and genome replication/repair. Aberrant…”
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The mechanism of modulation of the Escherichia coli DNA helicase II (UvrD) unwinding activity, a study of the 2B subdomain by Meiners, Matthew J

“…Helicases are ubiquitous motor proteins which catalyze the separation of double stranded DNA into single stranded DNA for the purposes of replication,…”
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The mechanism of modulation of the Escherichia coli DNA helicase II (UvrD) unwinding activity, a study of the 2B subdomain by Meiners, Matthew J

“…Helicases are ubiquitous motor proteins which catalyze the separation of double stranded DNA into single stranded DNA for the purposes of replication,…”
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