Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Dongxian Yue"'
Autor:
Dongxian Yue
The clFects of nucleoside modifications on E. coii tllNA^^' structure have be(Mi probed by imino Hi NMR. The NMR data shows that the structure of in oilro transcribed (unmodified) and native (modified) tRNA^^' are very similar in 15 iiiM Mg-^". Tempe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e58d7e0850e62afb0970d8ef6bb6a74a
https://doi.org/10.31274/rtd-180813-11557
https://doi.org/10.31274/rtd-180813-11557
Autor:
Ying Zhou, Yukun Ren, Haruichi Asahara, David A. Weitz, Ye Tao, Lloyd W. Ung, Shaorong Chong, John A. Heyman, Dongxian Yue, Alireza Abbaspourrad, Stephan A. Koehler, Roy Ziblat, Naiwen Cui, Huidan Zhang
Publikováno v:
Scientific Reports
Quantitative protein analysis of single cells is rarely achieved due to technical difficulties of detecting minute amounts of proteins present in one cell. We develop a mix-and-read assay for drop-based label-free protein analysis of single cells. Th
Autor:
Archibald S. Perkins, Dongxian Yue, Andrew J. Read, Sharon Lin, Kristin E. Yates, Pei Hui, Amanda C. Poholek, Bogdan Yatsula
Publikováno v:
Journal of Biological Chemistry. 280:30712-30722
The leukemia-associated protein EVI1 possesses seven zinc fingers within an N-terminal domain (amino acids 1-250) that binds to GACAAGATA. Single amino acid missense mutants of EVI1 were developed that failed to bind DNA either in vitro, as assessed
Publikováno v:
Biochemistry. 33:8905-8911
The structures of in vitro transcribed Escherichia coli tRNA(Val), which lacks base modifications, and the native tRNA, which contains them, are very similar in the presence of excess Mg2+ (Kintanar, Yue, and Horowitz, unpublished results). To furthe
Autor:
Dongxian Yue, Nicole M. Nichols
Publikováno v:
Current protocols in molecular biology.
Ribonucleases (RNases) with different sequence or structural specificities are used for a variety of analytical purposes, including RNA sequencing, mapping, and quantitation. The development of RNase protection assays, structural determination assays
Publikováno v:
Current Protocols in Molecular Biology
Terminal deoxynucleotidyl transferase (TdT), is a template-independent DNA polymerase that catalyzes the incorporation of deoxynucleotides at the 3'-hydroxyl terminus of DNA, accompanied by the release of inorganic phosphate. TdT does not require a t
Publikováno v:
The Biological bulletin. 196(3)
The CCA-adding enzyme [ATP(CTP):tRNA nucleotidyl transferase] catalyzes the addition and regeneration of the 3’ terminal CCA sequence of tRNAs. The enzyme adds the sequence CCA one nucleotide at a time to the 3’-terminus of tRNA, using CTP and AT
Publikováno v:
Biochemistry. 38(24)
We have studied the interactions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic footprinting with nuclease S1 and ribonuclease V1, and by analysis of the aminoacylation kinetics of mutant tRNAVal transcripts. Valyl-tR
Autor:
Pei Hui, Anna R Bjoring, Jeong H. Kim, Archibald S. Perkins, Dongxian Yue, Cynthia L. Leclerc, Joyce Aycock
Publikováno v:
Oncogene. 17(12)
We have sought to identify and isolate target genes for the zinc finger protein, EVI-1, which has been implicated in the genesis of myelogenous leukemia both in mouse and human. We have approached this with a two-step selection: we first selected for
Publikováno v:
The Journal of biological chemistry. 273(45)
The CCA-adding enzyme (tRNA nucleotidyltransferase) synthesizes and repairs the 3'-terminal CCA sequence of tRNA. The eubacterial, eukaryotic, and archaeal CCA-adding enzymes all share a single active-site signature motif, which identifies these enzy