Zobrazeno 1 - 10
of 71
pro vyhledávání: '"S. Eram"'
Autor:
Abdellah Allali-Hassani, Magdalena M. Szewczyk, Danton Ivanochko, Shawna L. Organ, Jabez Bok, Jessica Sook Yuin Ho, Florence P. H. Gay, Fengling Li, Levi Blazer, Mohammad S. Eram, Levon Halabelian, David Dilworth, Genna M. Luciani, Evelyne Lima-Fernandes, Qin Wu, Peter Loppnau, Nathan Palmer, S. Zakiah A. Talib, Peter J. Brown, Matthieu Schapira, Philipp Kaldis, Ronan C. O’Hagan, Ernesto Guccione, Dalia Barsyte-Lovejoy, Cheryl H. Arrowsmith, John M. Sanders, Solomon D. Kattar, D. Jonathan Bennett, Benjamin Nicholson, Masoud Vedadi
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
PRDM9 is a PR domain containing histone methyl transferase which expression is normally restricted to the germline that has also been linked to a number of somatic cancers. Here the authors describe the identification of a small molecule that selecti
Externí odkaz:
https://doaj.org/article/38d967925aeb49498c5e1209a2983c26
Autor:
Elvin D. de Araujo, Fettah Erdogan, Heidi A. Neubauer, Deniz Meneksedag-Erol, Pimyupa Manaswiyoungkul, Mohammad S. Eram, Hyuk-Soo Seo, Abdul K. Qadree, Johan Israelian, Anna Orlova, Tobias Suske, Ha T. T. Pham, Auke Boersma, Simone Tangermann, Lukas Kenner, Thomas Rülicke, Aiping Dong, Manimekalai Ravichandran, Peter J. Brown, Gerald F. Audette, Sarah Rauscher, Sirano Dhe-Paganon, Richard Moriggl, Patrick T. Gunning
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Hyper-activated STAT5B and its disease-causing variants are of interest as cancer drug targets. Here the authors combine cell based studies, X-ray crystallography, biophysical experiments and MD simulations to structurally and functionally characteri
Externí odkaz:
https://doaj.org/article/f8b672c48f8f4b91911646f53ce84f0b
Publikováno v:
Data in Brief, Vol 5, Iss C, Pp 489-497 (2015)
The data provide additional support of the characterization of the biophysical and biochemical properties of the enzyme acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima (Eram et al., 2015) [1]. The genes encoding the
Externí odkaz:
https://doaj.org/article/3c7a0f63181a4359863bd3df2757b81c
Akademický článek
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Autor:
Jian Jin, Levon Halabelian, Fengling Li, Masoud Vedadi, Rima Al-awar, Carlo C. dela Seña, Mohammad S. Eram, Aiping Dong, Carlos Zepeda-Velázquez, He Chen, Matthieu Schapira, Robert M. Campbell, Dalia Barsyte-Lovejoy, David McLeod, Cheryl H. Arrowsmith, Hong Zeng, Hong Wu, Yudao Shen, Mary M. Mader, Viacheslav V. Trush, Brian Morgan Watson, Kwang-Su Park, Irene Chau, Fanye Meng, Peter Brown, H. Ümit Kaniskan, Magdalena M. Szewczyk
Publikováno v:
J Med Chem
Protein arginine methyltransferase 6 (PRMT6) catalyzes monomethylation and asymmetric dimethylation of arginine residues in various proteins, plays important roles in biological processes, and is associated with multiple cancers. To date, a highly se
Autor:
Mohammad S. Eram, Kesen Ma
Publikováno v:
Biomolecules, Vol 3, Iss 3, Pp 578-596 (2013)
Pyruvate decarboxylase (PDC encoded by pdc) is a thiamine pyrophosphate (TPP)-containing enzyme responsible for the conversion of pyruvate to acetaldehyde in many mesophilic organisms. However, no pdc/PDC homolog has yet been found in fully sequenced
Externí odkaz:
https://doaj.org/article/f7f7c85aaf4b4f5e9a13aa0a2c3646f6
Autor:
Richard Moriggl, Manimekalai Ravichandran, Thomas Rülicke, Lukas Kenner, Peter Brown, Sarah Rauscher, Mohammad S. Eram, Ha T. T. Pham, Fettah Erdogan, Deniz Meneksedag-Erol, Simone Tangermann, Aiping Dong, Auke Boersma, Patrick T. Gunning, Pimyupa Manaswiyoungkul, Elvin D. de Araujo, Hyuk-Soo Seo, Sirano Dhe-Paganon, Abdul K. Qadree, Gerald F. Audette, Johan Israelian, Anna Orlova, Heidi A. Neubauer, Tobias Suske
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Hyper-activated STAT5B variants are high value oncology targets for pharmacologic intervention. STAT5BN642H, a frequently-occurring oncogenic driver mutation, promotes aggressive T-cell leukemia/lymphoma in patient carriers, although the molecular or
Publikováno v:
Archaea, Vol 2014 (2014)
The hyperthermophilic archaeon Thermococcus guaymasensis produces ethanol as a metabolic end product, and an alcohol dehydrogenase (ADH) catalyzing the reduction of acetaldehyde to ethanol has been purified and characterized. However, the enzyme cata
Externí odkaz:
https://doaj.org/article/aea6b6b5f5b14d7cbbc2d41adee66e69
Autor:
Fengling Li, Masoud Vedadi, Magdalena Szewczyk, Hong Zeng, H. Ümit Kaniskan, David McLeod, Mohammad S. Eram, Rima Al-awar, Kwang-Su Park, Brian Morgan Watson, Carlo Dela Sena, Mary M. Mader, Carlos Zepeda-Velázquez, He Chen, Matthieu Schapira, Robert M. Campbell, Yudao Shen, Irene Chau, Peter Brown, Cheryl H. Arrowsmith, Jian Jin, Dalia Barsyte-Lovejoy, Levon Halabelian, Fanye Meng
PRMT6 catalyzes monomethylation and asymmetric dimethylation of arginine residues in various proteins, plays important roles in biological processes and is associated with multiple cancers. While there are several reported PRMT6 inhibitors, a highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c02a7bc147f729d2d3ae77ade37b61a
https://doi.org/10.1101/2020.12.04.412569
https://doi.org/10.1101/2020.12.04.412569
Autor:
Levon Halabelian, Nozomu Sakai, David McLeod, Anne-Claude Gingras, Rima Al-awar, Hiroshi Nara, Dalia Barsyte-Lovejoy, Masoud Vedadi, David Dilworth, Hideto Fukushi, Stéphane Richard, Carlos Zepeda, Cheryl H. Arrowsmith, María Sánchez-Osuna, Ahmed Aman, Carlo C. dela Seña, Kozo Hayashi, Suzanne Ackloo, Magdalena M. Szewczyk, Yoshinori Ishikawa, Peter Brown, Fengling Li, Eric Bonneil, Mike Tyers, Mohammad S. Eram, Masayuki Takizawa, Amber L. Couzens, Shawna Organ, Rachel Harding, Shinji Takagi, Tsukasa Sugo
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-1 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-1 (2020)
Protein arginine methyltransferases (PRMTs) regulate diverse biological processes and are increasingly being recognized for their potential as drug targets. Here we report the discovery of a potent, selective, and cell-active chemical probe for PRMT7