Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Chamara Senevirathne"'
Autor:
Hairui Su, Ming Jiang, Chamara Senevirathne, Srinivas Aluri, Tuo Zhang, Han Guo, Juliana Xavier-Ferrucio, Shuiling Jin, Ngoc-Tung Tran, Szu-Mam Liu, Chiao-Wang Sun, Yongxia Zhu, Qing Zhao, Yuling Chen, LouAnn Cable, Yudao Shen, Jing Liu, Cheng-Kui Qu, Xiaosi Han, Christopher A. Klug, Ravi Bhatia, Yabing Chen, Stephen D. Nimer, Y. George Zheng, Camelia Iancu-Rubin, Jian Jin, Haiteng Deng, Diane S. Krause, Jenny Xiang, Amit Verma, Minkui Luo, Xinyang Zhao
Publikováno v:
Cell Reports, Vol 36, Iss 4, Pp 109421- (2021)
Summary: Mitogen-activated protein kinases (MAPKs) are inactivated by dual-specificity phosphatases (DUSPs), the activities of which are tightly regulated during cell differentiation. Using knockdown screening and single-cell transcriptional analysis
Externí odkaz:
https://doaj.org/article/c390eca951f14661aa1b8d2ec69d2ff2
Autor:
Lulu Hu, Shun Liu, Yong Peng, Ruiqi Ge, Rui Su, Chamara Senevirathne, Bryan T. Harada, Qing Dai, Jiangbo Wei, Lisheng Zhang, Ziyang Hao, Liangzhi Luo, Huanyu Wang, Yuru Wang, Minkui Luo, Mengjie Chen, Jianjun Chen, Chuan He
Publikováno v:
Nature Biotechnology. 40:1210-1219
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0032b5e4be60815f1ecac05964a5689f
https://doi.org/10.1038/s41587-022-01243-z
https://doi.org/10.1038/s41587-022-01243-z
Autor:
Lulu Hu, Shun Liu, Yong Peng, Ruiqi Ge, Rui Su, Chamara Senevirathne, Bryan T. Harada, Qing Dai, Jiangbo Wei, Lisheng Zhang, Ziyang Hao, Liangzhi Luo, Huanyu Wang, Yuru Wang, Minkui Luo, Mengjie Chen, Jianjun Chen, Chuan He
Publikováno v:
Nature Biotechnology. 41:150-150
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::965b87f4a9fdbe674423017ec5343a21
https://doi.org/10.1038/s41587-022-01616-4
https://doi.org/10.1038/s41587-022-01616-4
Autor:
Lulu, Hu, Shun, Liu, Yong, Peng, Ruiqi, Ge, Rui, Su, Chamara, Senevirathne, Bryan T, Harada, Qing, Dai, Jiangbo, Wei, Lisheng, Zhang, Ziyang, Hao, Liangzhi, Luo, Huanyu, Wang, Yuru, Wang, Minkui, Luo, Mengjie, Chen, Jianjun, Chen, Chuan, He
Publikováno v:
Nature biotechnology. 40(8)
Functional studies of the RNA N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::063f653c011204ccc7bca988bc2c1619
https://pubmed.ncbi.nlm.nih.gov/36450851
https://pubmed.ncbi.nlm.nih.gov/36450851
Autor:
Xiaosi Han, Jian Jin, Chiao-Wang Sun, Jenny Xiang, Juliana Xavier-Ferrucio, Camelia Iancu-Rubin, Y. George Zheng, Xinyang Zhao, Amit Verma, Lou Ann Cable, Qing Zhao, Yabing Chen, Yuling Chen, Srinivas Aluri, Hairui Su, Tuo Zhang, Han Guo, Ming Jiang, Chamara Senevirathne, Haiteng Deng, Stephen D. Nimer, Christopher A. Klug, Shuiling Jin, Ngoc Tung Tran, Yudao Shen, Ravi Bhatia, Jing Liu, Yongxia Zhu, Szu Mam Liu, Diane S. Krause, Minkui Luo, Cheng-Kui Qu
Publikováno v:
Cell Reports, Vol 36, Iss 4, Pp 109421-(2021)
Summary: Mitogen-activated protein kinases (MAPKs) are inactivated by dual-specificity phosphatases (DUSPs), the activities of which are tightly regulated during cell differentiation. Using knockdown screening and single-cell transcriptional analysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de79f2e88ab95121da72d12b4cc03c98
https://doi.org/10.1016/j.celrep.2021.109421
https://doi.org/10.1016/j.celrep.2021.109421
Autor:
Junyi Wang, Joshua A. Linscott, Minkui Luo, Kanishk Kapilashrami, Zhen Wang, Shi Chen, Chamara Senevirathne
Publikováno v:
J Am Chem Soc
Transition state stabilization is essential for rate acceleration of enzymatic reactions. Despite extensive studies on various transition state structures of enzymes, an intriguing puzzle is whether an enzyme can accommodate multiple transition state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed615a3d80e29d113582ddb928f200cb
https://pubmed.ncbi.nlm.nih.gov/31034218
https://pubmed.ncbi.nlm.nih.gov/31034218
Autor:
Ahmed E. Fouda, D. Maheeka Embogama, Chamara Senevirathne, Mary Kay H. Pflum, Thilani A. Anthony
Publikováno v:
Bioorganic & Medicinal Chemistry. 24:12-19
Kinase-catalyzed protein phosphorylation is involved in a wide variety of cellular events. Development of methods to monitor phosphoproteins in normal and diseased states is critical to fully characterize cell signalling. Towards phosphoprotein analy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90ec3f85fb5ada6aedb57d7e9e9f5cce
https://doi.org/10.1016/j.bmc.2015.11.029
https://doi.org/10.1016/j.bmc.2015.11.029
Autor:
Chamara Senevirathne, Joshua A. Linscott, Gil Blum, Zhen Wang, Kanishk Kapilashrami, Ian R. Bothwell, Minkui Luo
Protein lysine methyltransferases (PKMTs) catalyze the methylation of protein substrates, and their dysregulation has been linked to many diseases, including cancer. Accumulated evidence suggests that the reaction path of PKMT-catalyzed methylation c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::267f9f52cf482922a79ff5fd0384285c
https://europepmc.org/articles/PMC5206543/
https://europepmc.org/articles/PMC5206543/
Publikováno v:
ChemBioChem. 14:381-387
Kinase-catalyzed protein phosphorylation is involved in a wide variety of cellular events. Development of methods to monitor phosphorylation is critical to understand cell biology. Our lab recently discovered kinase-catalyzed biotinylation, where ATP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0235dfe7954bc55886a9f492c74c8f9
https://doi.org/10.1002/cbic.201200626
https://doi.org/10.1002/cbic.201200626
Publikováno v:
Bioconjugate Chemistry. 23:2386-2391
Kinase-catalyzed protein phosphorylation is an important biochemical process involved in cellular functions. We recently discovered that kinases promiscuously accept γ-modified ATP analogues as cosubstrates and used several ATP analogues as tools fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b36e2b3821c5ca79cdc615c10b5ba204
https://doi.org/10.1021/bc300404s
https://doi.org/10.1021/bc300404s