Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Anup K. Upadhyay"'
Autor:
Eric R. Goedken, Maria A. Argiriadi, Justin D. Dietrich, Andrew M. Petros, Navasona Krishnan, Sanjay C. Panchal, Wei Qiu, Haihong Wu, Haizhong Zhu, Ashley M. Adams, Pierre M. Bodelle, Lucas Goguen, Paul L. Richardson, Peter F. Slivka, Myron Srikumaran, Anup K. Upadhyay, Bainan Wu, Russell A. Judge, Anil Vasudevan, Sujatha M. Gopalakrishnan, Philip B. Cox, Vincent S. Stoll, Chaohong Sun
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-12 (2022)
Abstract Anti-IL17A therapies have proven effective for numerous inflammatory diseases including psoriasis, axial spondylitis and psoriatic arthritis. Modulating and/or antagonizing protein–protein interactions of IL17A cytokine binding to its cell
Externí odkaz:
https://doaj.org/article/73a129f16e244becaaa09ce714e81a66
Autor:
Anup K. Upadhyay, Andrew M. Petros, Chaohong Sun, Andrew T. Namanja, Steven R. Van Doren, Jia Xu, Qi Sun, Haihong Wu
Publikováno v:
Journal of Biomolecular NMR. 73:675-685
Protein-based NMR spectroscopy has proven to be a very robust method for finding fragment leads to protein targets. However, one limitation of protein-based NMR is that the data acquisition and analysis can be time consuming. In order to streamline t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ce3b37c313294ed47064f866eb097f0
https://doi.org/10.1007/s10858-019-00279-9
https://doi.org/10.1007/s10858-019-00279-9
Autor:
Anup K. Upadhyay, Ron Pithawalla, Rodger F. Henry, Russell A. Judge, Chaohong Sun, Justin A. Simanis, Leiming Li, Violeta L. Marin, Andrew M. Petros, Pierre M. Bodelle
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 28:1708-1713
The tandem TUDOR domains present in the non-catalytic C-terminal half of the KDM4A, 4B and 4C enzymes play important roles in regulating their chromatin localizations and substrate specificities. They achieve this regulatory role by binding to differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eb7dcb63ded0bdffc7ddcc0ad4e291a
https://doi.org/10.1016/j.bmcl.2018.04.050
https://doi.org/10.1016/j.bmcl.2018.04.050
Autor:
Anup K. Upadhyay, Dale J. Kempf, Rakesh Tripathi, Kenton L. Longenecker, Chaohong Sun, Matthew Cyr
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
The recent epidemic of Zika virus (ZIKV) has created a major global health concern. Here, the crystal structure of the full-length ZIKV NS5 protein at 3.05 Å resolution is presented to facilitate the structure-based design of antiviral agents agains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80f7465455e72258ba3c4c575ed16650
https://doi.org/10.1107/s2053230x17001601
https://doi.org/10.1107/s2053230x17001601
Autor:
Gary G. Chiang, Masoud Vedadi, Alberto Martin, Dalia Barsyte-Lovejoy, William N. Pappano, Cheryl H. Arrowsmith, Alexander Nuber, Vijayaratnam Santhakumar, Kenneth M. Comess, Judd C. Rice, Maricel Torrent, Gunnar Schotta, Peter Brown, Conglei Li, Anup K. Upadhyay, Fengling Li, Alex R Shoemaker, Ramzi F. Sweis, Mikkel Algire, Yujia Dai, Loren M. Lasko, Taylor R H Mitchell, Creighton T. Tuzon, Kenneth D. Bromberg, Mohammad S. Eram, Michael R. Michaelides, Niru B. Soni, Clarissa G. Jakob, Chaohong Sun, Manisha A Jhala, Vlasios Manaves
Publikováno v:
Nature Chemical Biology. 13:317-324
Protein lysine methyltransferases (PKMTs) regulate diverse physiological processes including transcription and the maintenance of genomic integrity. Genetic studies suggest that the PKMTs SUV420H1 and SUV420H2 facilitate proficient nonhomologous end-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa83d9f95eebf4a7288c158fbe1c7aaf
https://doi.org/10.1038/nchembio.2282
https://doi.org/10.1038/nchembio.2282
Autor:
Li-Jung Juan, Yi Zhang, Ting Huei Du, Anup K. Upadhyay, Xiaodong Cheng, Yu Ting Yan, Chung Fan Lee, Chen Cheng Lee, Ming Lun Kang, Shih Huan Peng, Li Shen, Guoliang Xu
Genomic imprinting is an allelic gene expression phenomenon primarily controlled by allele-specific DNA methylation at the imprinting control region (ICR), but the underlying mechanism remains largely unclear. N-α-acetyltransferase 10 protein (Naa10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20a4617ff73da58b690bfed0d19b9ff5
https://europepmc.org/articles/PMC6322414/
https://europepmc.org/articles/PMC6322414/
Autor:
Xiaodong Cheng, Hideharu Hashimoto, Anup K. Upadhyay, Paula M. Vertino, Xing Zhang, Shelley B. Howerton, Yiwei Liu, Yanqi Chang
Publikováno v:
Nucleic Acids Research
Cytosine residues in mammalian DNA occur in at least three forms, cytosine (C), 5-methylcytosine (M; 5mC) and 5-hydroxymethylcytosine (H; 5hmC). During semi-conservative DNA replication, hemi-methylated (M/C) and hemi-hydroxymethylated (H/C) CpG dinu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b54a5ed1809d4289ed02a3fe56202f00
https://doi.org/10.1093/nar/gks155
https://doi.org/10.1093/nar/gks155
Autor:
Xing Zhang, Xiaodong Cheng, Ruogu Hu, Antonello Mai, Ji Woong Han, Donatella Labella, Yanqi Chang, Young Sup Yoon, Anup K. Upadhyay, Dante Rotili
Publikováno v:
Journal of Molecular Biology; Vol 416
BIX-01294 and its analogs were originally identified and subsequently designed as potent inhibitors against histone H3 lysine 9 (H3K9) methyltransferases G9a and G9a-like protein. Here, we show that BIX-01294 and its analog E67 can also inhibit H3K9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d61bb130809ed3bdf84f2aec5c229699
https://doi.org/10.1016/j.jmb.2011.12.036
https://doi.org/10.1016/j.jmb.2011.12.036
Publikováno v:
Current Opinion in Structural Biology. 21:750-760
Both components of chromatin (DNA and histones) are subjected to dynamic postsynthetic covalent modifications. Dynamic histone lysine methylation involves the activities of modifying enzymes (writers), enzymes removing modifications (erasers), and re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f88eee7d39e2717d93bfdf24be66a552
https://doi.org/10.1016/j.sbi.2011.08.003
https://doi.org/10.1016/j.sbi.2011.08.003
Autor:
Xiaodong Cheng, Pierre Olivier Estève, Anup K. Upadhyay, George R. Feehery, John R. Horton, Sriharsa Pradhan, Mala Samaranayake, Yanqi Chang
Publikováno v:
Nature Structural & Molecular Biology. 18:42-48
The protein lysine methyltransferase SET7 regulates DNA methyltransferase-1 (DNMT1) activity in mammalian cells by promoting degradation of DNMT1 and thus allows epigenetic changes via DNA demethylation. Here we reveal an interplay between monomethyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8797e3d2e8aa80ded4143a10369a38ee
https://doi.org/10.1038/nsmb.1939
https://doi.org/10.1038/nsmb.1939