Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Thomas Zengeya"'
Autor:
Sarah E. Bergholtz, Anthony Omole, Yihang Jing, Thomas Zengeya, Jordan L. Meier, Euna Yoo, Rhushi A. Kulkarni
Publikováno v:
Chembiochem
Lysine malonylation is a recently characterized posttranslational modification involved in the regulation of energy metabolism and gene expression. One unique feature of this posttranslational modification is its potential susceptibility to decarboxy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdf31f42b3af0ed5589e9a696280dc3f
https://europepmc.org/articles/PMC10262540/
https://europepmc.org/articles/PMC10262540/
Lysine malonylation is a recently characterized posttranslational modification involved in the regulation of energy metabolism and gene expression. Two unique features of this posttranslational modification are its negative charge and potential susce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f51ee5571fe3e4b234a92dbbbd3b5e0
https://doi.org/10.1101/2020.08.23.263285
https://doi.org/10.1101/2020.08.23.263285
Autor:
Thomas Zengeya, Jordan L. Meier, Stephen D. Fox, David C. Montgomery, Daniel Arango, Wilson R. Sinclair, Justin M. Thomas, Jonathan H. Shrimp, Shalini Oberdoerffer, Thorkell Andresson
Publikováno v:
ACS Chem Biol
The human acetyltransferase NAT10 has recently been shown to catalyze formation of N4-acetylcytidine (ac4C), a minor nucleobase known to alter RNA structure and function. In order to better understand the role of RNA acetyltransferases in biology and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf6d734f73cd4f0d35f8d37db9f43a47
https://pubmed.ncbi.nlm.nih.gov/29039931
https://pubmed.ncbi.nlm.nih.gov/29039931
Autor:
Wilson R. Sinclair, Ian A. Blair, Jonathan H. Shrimp, Thomas Zengeya, Andrew J. Worth, Jordan L. Meier, Julie M. Garlick, Rhushikesh A. Kulkarni, Nathaniel W. Snyder, Hans Luecke
Publikováno v:
Chemical Science
A systematically designed panel of biorthogonal pro-metabolites was synthesized and evaluated as agents for tracing cellular short chain fatty acylation.
Short chain fatty acids (SCFAs) play a central role in health and disease. One function of
Short chain fatty acids (SCFAs) play a central role in health and disease. One function of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03e9fe93824b9b6554562ed55693505e
https://pubmed.ncbi.nlm.nih.gov/29675169
https://pubmed.ncbi.nlm.nih.gov/29675169
Autor:
Jeff Coller, Najwa Alhusaini, Thomas Zengeya, Jordan L. Meier, Wilson R. Sinclair, Thorkell Andresson, Stephen D. Fox, Mariana D. Mandler, Allissa Dillman, Masaki Hosogane, Thomas J. Sweet, David Sturgill, Daniel Arango, Kyster K. Nanan, Shalini Oberdoerffer, Gavin Hanson
Publikováno v:
Cell. 175:1872-1886.e24
Summary Generation of the "epitranscriptome" through post-transcriptional ribonucleoside modification embeds a layer of regulatory complexity into RNA structure and function. Here, we describe N4-acetylcytidine (ac4C) as an mRNA modification that is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16a28a90dd05c84b4da105e930d8b09c
https://doi.org/10.1016/j.cell.2018.10.030
https://doi.org/10.1016/j.cell.2018.10.030
Autor:
Sudipto Das, W. Marston Linehan, Ming Zhou, Rhushikesh A. Kulkarni, David C. Montgomery, Clementina Mesaros, Benjamin K. Gibbs, King C. Chan, Thorkell Andresson, Thomas Zengeya, Julie M. Garlick, Jordan L. Meier, Andrew J. Worth, Allison M. Roberts, Yien Che Tsai, Nathaniel W. Snyder, Ian A. Blair, Jonathan H. Shrimp, Carole Sourbier, Allan M. Weissman
Publikováno v:
Cell chemical biology. 24(2)
Non-enzymatic protein modification driven by thioester reactivity is thought to play a major role in the establishment of cellular lysine acylation. However, the specific protein targets of this process are largely unknown. Here we report an experime
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b3f209bc60dafd56f58b5ee7bfa3f9b
https://pubmed.ncbi.nlm.nih.gov/28212757
https://pubmed.ncbi.nlm.nih.gov/28212757
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 21:2121-2124
Peptide nucleic acid (PNA1) containing a 5-methylisocytidine (iC) nucleobase has been synthesized. Triple helix formation between PNA1 and RNA hairpins having variable base pairs interacting with iC was studied using isothermal titration calorimetry.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c95e9dae3fbefa711570a2d9565fe734
https://doi.org/10.1016/j.bmcl.2011.01.130
https://doi.org/10.1016/j.bmcl.2011.01.130
Publikováno v:
Phytochemistry. 69:396-402
The leaf cuticular waxes of six Salix clones (one Salix miyabeana, one Salix dasyclados, one Salix eriocephala, two Salix purpurea, and one interspecific hybrid of Salix eriocephala x interior) with different biomass productivities were characterized
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1369886f5488731b589fa2c5f131bd6b
https://doi.org/10.1016/j.phytochem.2007.08.015
https://doi.org/10.1016/j.phytochem.2007.08.015
Publikováno v:
Organic letters. 17(10)
Cell-permeating esters of 2-ketoglutarate (2-KG) have been synthesized through a convergent sequence from two modules in two and three steps, respectively. This route provides access to a full series of mono- and disubstituted 2-KG esters, enabling u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e74521ffa01207f1f50572abb50754c2
https://pubmed.ncbi.nlm.nih.gov/25915096
https://pubmed.ncbi.nlm.nih.gov/25915096
Publikováno v:
Analytical biochemistry. 470
We describe a new method for protein affinity purification that capitalizes on the high affinity of streptavidin for biotin but does not require dissociation of the biotin-streptavidin complex for protein retrieval. Conventional reagents place both t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3de3b52f62dbecff3d9ed27f72718341
https://pubmed.ncbi.nlm.nih.gov/25447466
https://pubmed.ncbi.nlm.nih.gov/25447466