Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Tatlock, John H."'
Autor:
Karen A. Maegley, Kephart Susan Elizabeth, Christopher P. Dillon, Manli Shi, Kristen Jensen-Pergakes, Prakash B. Palde, Ya-Li Deng, Chi-Yeh Chung, Natalie Miller, John Sherrill, Wei Liu, Ryan L. Patman, Shinji Yamazaki, Tao Xie, Fen Wang, Hieu Lam, Eleanore Hendrickson, John F. Braganza, Yuli Wang, Robert Arnold Kumpf, Shannon Karlicek Bryant, Thomas A Paul, Noah Spiegel, Martin James Wythes, Amy Nemeth, Stephanie Scales, Elizabeth A. McMillan, Michelle Tran-Dubé, Alexei Brooun, Vesta Goshtasbi, Eugene Rui, Michele McTigue, Indrawan James Mcalpine, Tatlock John H
Publikováno v:
Molecular Cancer Therapeutics. 21:3-15
Protein arginine methyltransferase 5 (PRMT5) overexpression in hematologic and solid tumors methylates arginine residues on cellular proteins involved in important cancer functions including cell-cycle regulation, mRNA splicing, cell differentiation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::621805778a73d6732ba64af7ea279a54
https://doi.org/10.1158/1535-7163.mct-21-0620
https://doi.org/10.1158/1535-7163.mct-21-0620
Autor:
Barsyte-Lovejoy, Dalia, Li, Fengling, Oudhoff, Menno J., Tatlock, John H., Dong, Aiping, Zeng, Hong, Wu, Hong, Freeman, Spencer A., Schapira, Matthieu, Senisterra, Guillermo A., Kuznetsova, Ekaterina, Marcellus, Richard, Allali-Hassani, Abdellah, Kennedy, Steven, Lambert, Jean-Philippe, Couzens, Amber L., Aman, Ahmed, Gingras, Anne-Claude, Al-Awar, Rima, Fish, Paul V., Gerstenberger, Brian S., Roberts, Lee, Benn, Caroline L., Grimley, Rachel L., Braam, Mitchell J. S., Rossi, Fabio M. V., Sudol, Marius, Brown, Peter J., Bunnage, Mark E., Owen, Dafydd R., Zaph, Colby, Vedadi, Masoud, Arrowsmith, Cheryl H.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2014 Sep 01. 111(35), 12853-12858.
Externí odkaz:
https://www.jstor.org/stable/43043421
Autor:
Eleanore Hendrickson, Martin James Wythes, Indrawan James Mcalpine, Karen A. Maegley, Christopher P. Dillon, Fen Wang, Kephart Susan Elizabeth, Amy Nemeth, Prakash B. Palde, Manli Shi, Kristen Jensen-Pergakes, Shinji Yamazaki, Tao Xie, Chi-Yeh Chung, Michelle Tran-Dubé, Tatlock John H, Stephanie Scales, Hieu Lam, Eugene Rui, Thomas A Paul, Elizabeth A. McMillan, Robert Arnold Kumpf, Ryan L. Patman, Michele McTigue, Natalie Miller, Ya-Li Deng, Yuli Wang, Noah Spiegel, Alexei Brooun, John Sherrill, Wei Liu, John F. Braganza
Publikováno v:
Cancer Research. 81:1160-1160
Protein arginine methyltransferase 5 (PRMT5) overexpression in hematological and solid tumors promotes symmetrical di-methyl arginine (SDMA) on cellular proteins involved in important cancer functions including cell cycle regulation, mRNA splicing, c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ffac773af19496024ab15b63ff654a26
https://doi.org/10.1158/1538-7445.am2021-1160
https://doi.org/10.1158/1538-7445.am2021-1160
Akademický článek
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Autor:
Dafydd R. Owen, Aiping Dong, Martin James Wythes, Steven Kennedy, Dalia Barsyte-Lovejoy, Matthieu Schapira, Hong Wu, Rajiah Aldrin Denny, Viacheslav V. Trush, Mihir D. Parikh, Agustin Casimiro-Garcia, Renato Ferreira de Freitas, Masoud Vedadi, Magdalena Swewczyk, Hong Zeng, Tatlock John H, Fengling Li, Alexandria P. Taylor, Robert Arnold Kumpf, Peter Brown, Cheryl H. Arrowsmith
Publikováno v:
Journal of medicinal chemistry. 62(17)
The first chemical probe to primarily occupy the co-factor binding site of a Su(var)3-9, enhancer of a zeste, trithorax (SET) domain containing protein lysine methyltransferase (PKMT) is reported. Protein methyltransferases require S-adenosylmethioni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e491e646b8409403d237931a50d510f6
https://pubmed.ncbi.nlm.nih.gov/31415173
https://pubmed.ncbi.nlm.nih.gov/31415173
Autor:
Tao Xie, Paulina Delgado Cuenca, Brion W. Murray, Keith A. Ching, Tatlock John H, Sherry Niessen, Patrick J. Metz, Kristen Jensen-Pergakes
Publikováno v:
Cell Reports, Vol 30, Iss 6, Pp 1935-1950.e8 (2020)
Summary: Alternative splicing is well understood to enhance proteome diversity as cells respond to stimuli. However, mechanistic understanding for how the spliceosome processes precursor messenger RNA (mRNA) transcripts to achieve template diversific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f4152d5b1a3e729e3a430f7a84d6886
https://doi.org/10.1016/j.celrep.2020.01.054
https://doi.org/10.1016/j.celrep.2020.01.054
Autor:
Robert Steven Kania, Eric Johnson, Tatlock John H, Luping Qiu, Timothy L. Foley, Shaoxian Sun, Kymberly Levine, Ketan S. Gajiwala, Ciarán N. Cronin, Michelle Kraus, Asako Nagata
Publikováno v:
PLoS ONE
PLoS ONE, Vol 13, Iss 6, p e0198374 (2018)
PLoS ONE, Vol 13, Iss 6, p e0198374 (2018)
Protein tyrosine kinase 6 (PTK6, or BRK) is aberrantly expressed in breast cancers, and emerging as an oncogene that promotes tumor cell proliferation, migration and evasion. Both kinase-dependent and -independent functions of PTK6 in driving tumor g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ed360b0109ea048c220a42f22b9203e
http://europepmc.org/articles/PMC5991704
http://europepmc.org/articles/PMC5991704
Autor:
Patrick Bingham, Wade Diehl, Karen A. Maegley, Cody Krivacic, Buwen Huang, Zehnder Luke Raymond, Xiu Yu, Pei-Pei Kung, Tatlock John H, Ketan S. Gajiwala
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 25:1532-1537
A series of novel enhancer of zeste homolog 2 (EZH2) inhibitors was designed based on the chemical structure of the histone methyltransferase (HMT) inhibitor SAH (S-adenosyl-l-homocysteine). These nucleoside-based EZH2 inhibitors blocked the methylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d620a08a912858b8dddc12537ce993f7
https://doi.org/10.1016/j.bmcl.2015.02.017
https://doi.org/10.1016/j.bmcl.2015.02.017
Autor:
Abdellah Allali-Hassani, Marius Sudol, Amber L. Couzens, Menno J. Oudhoff, Hong Zeng, Peter Brown, Masoud Vedadi, Mitchell J.S. Braam, Aiping Dong, Anne-Claude Gingras, Brian S. Gerstenberger, Fengling Li, Richard Marcellus, Spencer A. Freeman, Fabio M.V. Rossi, Dafydd R. Owen, Rima Al-awar, Lee R. Roberts, Tatlock John H, Hong Wu, Paul V. Fish, Steven Kennedy, Ahmed Aman, Colby Zaph, Guillermo A. Senisterra, Matthieu Schapira, Jean-Philippe Lambert, Ekaterina Kuznetsova, Cheryl H. Arrowsmith, Mark E. Bunnage, Rachel L. Grimley, Dalia Barsyte-Lovejoy, Caroline L. Benn
Publikováno v:
Proceedings of the National Academy of Sciences. 111:12853-12858
SET domain containing (lysine methyltransferase) 7 (SETD7) is implicated in multiple signaling and disease related pathways with a broad diversity of reported substrates. Here, we report the discovery of (R)-PFI-2-a first-in-class, potent (Ki (app) =
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d23770c64651903f028988e2aa7651df
https://doi.org/10.1073/pnas.1407358111
https://doi.org/10.1073/pnas.1407358111
Autor:
Hovhannes J. Gukasyan, Michael R. Collins, Sutton Scott Channing, Kephart Susan Elizabeth, Shinji Yamazaki, Sacha Ninkovic, Simon Bergqvist, Fen Wang, Robert Arnold Kumpf, Michael Ryskin, Patrick Bingham, Pei-Pei Kung, Dominique Verhelle, Brian Yip, Karen A. Maegley, Robert A. Rollins, Peter A. Wells, Martha A. Ornelas, Buwen Huang, Valeria Fantin, Xiu Yu, Stephanie Scales, Wade Diehl, Indrawan James Mcalpine, Cody Krivacic, Mei Cui, Lisa Nguyen, Wenyue Hu, Tatlock John H, Dac M. Dinh, Martin James Wythes, Connie Fan, Gary Li, Martin Paul Edwards, Rui Eugene Yuanjin, John F. Braganza, Zehnder Luke Raymond, Wei-Guo Zhang
Publikováno v:
Journal of medicinal chemistry. 59(18)
A new enhancer of zeste homolog 2 (EZH2) inhibitor series comprising a substituted phenyl ring joined to a dimethylpyridone moiety via an amide linkage has been designed. A preferential amide torsion that improved the binding properties of the compou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f62bbe5fc41702928ba23fd544b9fadd
https://pubmed.ncbi.nlm.nih.gov/27936698
https://pubmed.ncbi.nlm.nih.gov/27936698