Year |
Citation |
Score |
2020 |
Zuo Y, De S, Feng Y, Steitz TA. Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation. Iscience. 23: 101445. PMID 32829286 DOI: 10.1016/J.Isci.2020.101445 |
0.332 |
|
2016 |
Liu B, Zuo Y, Steitz TA. Structures of E. coli σS-transcription initiation complexes provide new insights into polymerase mechanism. Proceedings of the National Academy of Sciences of the United States of America. PMID 27035955 DOI: 10.1073/Pnas.1520555113 |
0.344 |
|
2015 |
Zuo Y, Steitz TA. Crystal Structures of the E. coli Transcription Initiation Complexes with a Complete Bubble. Molecular Cell. 58: 534-40. PMID 25866247 DOI: 10.1016/J.Molcel.2015.03.010 |
0.345 |
|
2015 |
Liu B, Zuo Y, Steitz TA. Structural basis for transcription reactivation by RapA. Proceedings of the National Academy of Sciences of the United States of America. 112: 2006-10. PMID 25646438 DOI: 10.1073/Pnas.1417152112 |
0.358 |
|
2013 |
Zuo Y, Wang Y, Steitz TA. The mechanism of E. coli RNA polymerase regulation by ppGpp is suggested by the structure of their complex. Molecular Cell. 50: 430-6. PMID 23623685 DOI: 10.1016/J.Molcel.2013.03.020 |
0.316 |
|
2007 |
Lalonde MS, Zuo Y, Zhang J, Gong X, Wu S, Malhotra A, Li Z. Exoribonuclease R in Mycoplasma genitalium can carry out both RNA processing and degradative functions and is sensitive to RNA ribose methylation. Rna (New York, N.Y.). 13: 1957-68. PMID 17872508 DOI: 10.1261/Rna.706207 |
0.339 |
|
2007 |
Zuo Y, Zheng H, Wang Y, Chruszcz M, Cymborowski M, Skarina T, Savchenko A, Malhotra A, Minor W. Crystal structure of RNase T, an exoribonuclease involved in tRNA maturation and end turnover. Structure (London, England : 1993). 15: 417-28. PMID 17437714 DOI: 10.1016/J.Str.2007.02.004 |
0.476 |
|
2006 |
Zuo Y, Vincent HA, Zhang J, Wang Y, Deutscher MP, Malhotra A. Structural basis for processivity and single-strand specificity of RNase II. Molecular Cell. 24: 149-56. PMID 16996291 DOI: 10.1016/J.Molcel.2006.09.004 |
0.648 |
|
2006 |
Suzuki H, Zuo Y, Wang J, Zhang MQ, Malhotra A, Mayeda A. Characterization of RNase R-digested cellular RNA source that consists of lariat and circular RNAs from pre-mRNA splicing. Nucleic Acids Research. 34: e63. PMID 16682442 DOI: 10.1093/Nar/Gkl151 |
0.432 |
|
2005 |
Zuo Y, Wang Y, Malhotra A. Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing. Structure (London, England : 1993). 13: 973-84. PMID 16004870 DOI: 10.1016/J.Str.2005.04.015 |
0.389 |
|
2004 |
Fiedler TJ, Vincent HA, Zuo Y, Gavrialov O, Malhotra A. Purification and crystallization of Escherichia coli oligoribonuclease. Acta Crystallographica. Section D, Biological Crystallography. 60: 736-9. PMID 15039570 DOI: 10.1107/S0907444904002252 |
0.591 |
|
2002 |
Zuo Y, Deutscher MP. Structure and Mechanism of Rnase. Thescientificworldjournal. 2: 65-66. PMID 29973806 DOI: 10.1100/Tsw.2002.32 |
0.63 |
|
2002 |
Zuo Y, Deutscher MP. Mechanism of action of RNase T. I. Identification of residues required for catalysis, substrate binding, and dimerization. The Journal of Biological Chemistry. 277: 50155-9. PMID 12364334 DOI: 10.1074/Jbc.M207706200 |
0.605 |
|
2002 |
Zuo Y, Deutscher MP. Mechanism of action of RNase T. II. A structural and functional model of the enzyme. The Journal of Biological Chemistry. 277: 50160-4. PMID 12364333 DOI: 10.1074/Jbc.M207707200 |
0.596 |
|
2002 |
Zuo Y, Deutscher MP. The physiological role of RNase T can be explained by its unusual substrate specificity. The Journal of Biological Chemistry. 277: 29654-61. PMID 12050169 DOI: 10.1074/Jbc.M204252200 |
0.642 |
|
2001 |
Zuo Y, Deutscher MP. Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Research. 29: 1017-26. PMID 11222749 DOI: 10.1093/Nar/29.5.1017 |
0.569 |
|
1999 |
Zuo Y, Deutscher MP. The DNase activity of RNase T and its application to DNA cloning. Nucleic Acids Research. 27: 4077-82. PMID 10497273 DOI: 10.1093/Nar/27.20.4077 |
0.635 |
|
1998 |
Cheng ZF, Zuo Y, Li Z, Rudd KE, Deutscher MP. The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. The Journal of Biological Chemistry. 273: 14077-80. PMID 9603904 DOI: 10.1074/Jbc.273.23.14077 |
0.537 |
|
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