Year |
Citation |
Score |
2022 |
Cruz A, Joseph S. Interaction of the Influenza A Virus NS1 Protein with the 5'-m7G-mRNA·eIF4E·eIF4G1 Complex. Biochemistry. PMID 35797022 DOI: 10.1021/acs.biochem.2c00019 |
0.306 |
|
2022 |
Edwards M, Huang M, Joseph S. The Fragile X Protein Disordered Regions Bind a Novel RNA Target. Biochemistry. 61: 1199-1212. PMID 35653700 DOI: 10.1021/acs.biochem.2c00228 |
0.344 |
|
2021 |
Edwards M, Joseph S. The Fragile X Proteins Differentially Regulate Translation of Reporter mRNAs with G-quadruplex Structures. Journal of Molecular Biology. 434: 167396. PMID 34896112 DOI: 10.1016/j.jmb.2021.167396 |
0.417 |
|
2020 |
de Rozières CM, Joseph S. Influenza A Virus NS1 Protein Binds as a Dimer to RNA-Free PABP1 but Not to the PABP1·Poly(A) RNA Complex. Biochemistry. PMID 33172261 DOI: 10.1021/acs.biochem.0c00666 |
0.376 |
|
2020 |
Athar YM, Joseph S. The Human Fragile X Mental Retardation Protein Inhibits the Elongation Step of Translation through its RGG and C-terminal domains. Biochemistry. PMID 32945655 DOI: 10.1021/Acs.Biochem.0C00534 |
0.751 |
|
2020 |
Athar YM, Joseph S. RNA-Binding Specificity of the Human Fragile X Mental Retardation Protein. Journal of Molecular Biology. PMID 32343993 DOI: 10.1016/J.Jmb.2020.04.021 |
0.758 |
|
2018 |
Hoernes TP, Faserl K, Juen MA, Kremser J, Gasser C, Fuchs E, Shi X, Siewert A, Lindner H, Kreutz C, Micura R, Joseph S, Höbartner C, Westhof E, Hüttenhofer A, et al. Translation of non-standard codon nucleotides reveals minimal requirements for codon-anticodon interactions. Nature Communications. 9: 4865. PMID 30451861 DOI: 10.1038/S41467-018-07321-8 |
0.487 |
|
2018 |
Arias-Mireles BH, de Rozieres CM, Ly K, Joseph S. RNA Modulates the Interaction Between Influenza A Virus NS1 and Human PABP1. Biochemistry. PMID 29782795 DOI: 10.1021/Acs.Biochem.8B00218 |
0.452 |
|
2018 |
Shi X, Wu T, M Cole C, K Devaraj N, Joseph S. Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system. Scientific Reports. 8: 3488. PMID 29472573 DOI: 10.1038/S41598-018-21739-6 |
0.617 |
|
2018 |
Hoernes TP, Clementi N, Juen MA, Shi X, Faserl K, Willi J, Gasser C, Kreutz C, Joseph S, Lindner H, Hüttenhofer A, Erlacher MD. Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release. Proceedings of the National Academy of Sciences of the United States of America. PMID 29298914 DOI: 10.1073/Pnas.1714554115 |
0.465 |
|
2016 |
Katz FE, Shi X, Owens CP, Joseph S, Tezcan FA. Determination of NTPase activities from measurement of true inorganic phosphate in the presence of labile phosphate compounds. Analytical Biochemistry. PMID 28017740 DOI: 10.1016/J.Ab.2016.12.012 |
0.308 |
|
2016 |
Shi X, Joseph S. Mechanism of Translation Termination: RF1 Dissociation follows RF3 Dissociation from the Ribosome. Biochemistry. PMID 27779391 DOI: 10.1021/Acs.Biochem.6B00921 |
0.376 |
|
2016 |
Shi X, Joseph S. Translocation: lights, camera, and action. Nature Structural & Molecular Biology. 23: 367-8. PMID 27142323 DOI: 10.1038/Nsmb.3219 |
0.416 |
|
2016 |
Trappl K, Joseph S. Ribosome Induces a Closed to Open Conformational Change in Release Factor 1. Journal of Molecular Biology. PMID 26827724 DOI: 10.1016/J.Jmb.2016.01.021 |
0.434 |
|
2015 |
Chen E, Joseph S. Fragile X mental retardation protein: A paradigm for translational control by RNA-binding proteins. Biochimie. 114: 147-54. PMID 25701550 DOI: 10.1016/J.Biochi.2015.02.005 |
0.441 |
|
2015 |
Joseph S. Modification interference analysis of the ribosome. Methods in Molecular Biology (Clifton, N.J.). 1240: 113-23. PMID 25352140 DOI: 10.1007/978-1-4939-1896-6_8 |
0.43 |
|
2014 |
Chen E, Sharma MR, Shi X, Agrawal RK, Joseph S. Fragile X mental retardation protein regulates translation by binding directly to the ribosome. Molecular Cell. 54: 407-17. PMID 24746697 DOI: 10.1016/J.Molcel.2014.03.023 |
0.472 |
|
2014 |
Trappl K, Mathew MA, Joseph S. Thermodynamic and kinetic insights into stop codon recognition by release factor 1. Plos One. 9: e94058. PMID 24699820 DOI: 10.1371/Journal.Pone.0094058 |
0.41 |
|
2014 |
Alverdi V, Hetrick B, Joseph S, Komives EA. Direct observation of a transient ternary complex during IκBα-mediated dissociation of NF-κB from DNA. Proceedings of the National Academy of Sciences of the United States of America. 111: 225-30. PMID 24367071 DOI: 10.1073/Pnas.1318115111 |
0.684 |
|
2013 |
Sahu B, Khade PK, Joseph S. Highly conserved base A55 of 16S ribosomal RNA is important for the elongation cycle of protein synthesis. Biochemistry. 52: 6695-701. PMID 24025161 DOI: 10.1021/Bi4008879 |
0.469 |
|
2013 |
Khade PK, Shi X, Joseph S. Steric complementarity in the decoding center is important for tRNA selection by the ribosome. Journal of Molecular Biology. 425: 3778-89. PMID 23542008 DOI: 10.1016/J.Jmb.2013.02.038 |
0.42 |
|
2012 |
Sahu B, Khade PK, Joseph S. Functional replacement of two highly conserved tetraloops in the bacterial ribosome. Biochemistry. 51: 7618-26. PMID 22938718 DOI: 10.1021/Bi300930R |
0.487 |
|
2012 |
Shi X, Khade PK, Sanbonmatsu KY, Joseph S. Functional role of the sarcin-ricin loop of the 23S rRNA in the elongation cycle of protein synthesis. Journal of Molecular Biology. 419: 125-38. PMID 22459262 DOI: 10.1016/J.Jmb.2012.03.016 |
0.469 |
|
2011 |
Khade PK, Joseph S. Messenger RNA interactions in the decoding center control the rate of translocation. Nature Structural & Molecular Biology. 18: 1300-2. PMID 22020300 DOI: 10.1038/Nsmb.2140 |
0.479 |
|
2010 |
Field A, Hetrick B, Mathew M, Joseph S. Histidine 197 in release factor 1 is essential for a site binding and peptide release. Biochemistry. 49: 9385-90. PMID 20873815 DOI: 10.1021/Bi1012047 |
0.764 |
|
2010 |
Hetrick B, Khade PK, Lee K, Stephen J, Thomas A, Joseph S. Polyamines accelerate codon recognition by transfer RNAs on the ribosome. Biochemistry. 49: 7179-89. PMID 20666453 DOI: 10.1021/Bi1009776 |
0.776 |
|
2010 |
García-Ortega L, Alvarez-García E, Gavilanes JG, Martínez-del-Pozo A, Joseph S. Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding. Nucleic Acids Research. 38: 4108-19. PMID 20215430 DOI: 10.1093/Nar/Gkq151 |
0.507 |
|
2010 |
Khade P, Joseph S. Functional interactions by transfer RNAs in the ribosome. Febs Letters. 584: 420-6. PMID 19914248 DOI: 10.1016/J.Febslet.2009.11.034 |
0.367 |
|
2009 |
Hetrick B, Lee K, Joseph S. Kinetics of stop codon recognition by release factor 1. Biochemistry. 48: 11178-84. PMID 19874047 DOI: 10.1021/Bi901577D |
0.734 |
|
2009 |
Shi X, Chiu K, Ghosh S, Joseph S. Bases in 16S rRNA important for subunit association, tRNA binding, and translocation. Biochemistry. 48: 6772-82. PMID 19545171 DOI: 10.1021/Bi900472A |
0.459 |
|
2008 |
Garcia-Ortega L, Stephen J, Joseph S. Precise alignment of peptidyl tRNA by the decoding center is essential for EF-G-dependent translocation. Molecular Cell. 32: 292-9. PMID 18951096 DOI: 10.1016/J.Molcel.2008.09.012 |
0.451 |
|
2007 |
Studer SM, Joseph S. Binding of mRNA to the bacterial translation initiation complex. Methods in Enzymology. 430: 31-44. PMID 17913633 DOI: 10.1016/S0076-6879(07)30002-5 |
0.712 |
|
2007 |
Dunham CM, Selmer M, Phelps SS, Kelley AC, Suzuki T, Joseph S, Ramakrishnan V. Structures of tRNAs with an expanded anticodon loop in the decoding center of the 30S ribosomal subunit. Rna (New York, N.Y.). 13: 817-23. PMID 17416634 DOI: 10.1261/Rna.367307 |
0.501 |
|
2006 |
Feinberg JS, Joseph S. A conserved base-pair between tRNA and 23 S rRNA in the peptidyl transferase center is important for peptide release. Journal of Molecular Biology. 364: 1010-20. PMID 17045291 DOI: 10.1016/J.Jmb.2006.09.040 |
0.778 |
|
2006 |
Ali IK, Lancaster L, Feinberg J, Joseph S, Noller HF. Deletion of a Conserved, Central Ribosomal Intersubunit RNA Bridge Molecular Cell. 23: 865-874. PMID 16973438 DOI: 10.1016/J.Molcel.2006.08.011 |
0.806 |
|
2006 |
Komoda T, Sato NS, Phelps SS, Namba N, Joseph S, Suzuki T. The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. The Journal of Biological Chemistry. 281: 32303-9. PMID 16950778 DOI: 10.1074/Jbc.M607058200 |
0.45 |
|
2006 |
Phelps SS, Gaudin C, Yoshizawa S, Benitez C, Fourmy D, Joseph S. Translocation of a tRNA with an extended anticodon through the ribosome. Journal of Molecular Biology. 360: 610-22. PMID 16787653 DOI: 10.1016/J.Jmb.2006.05.016 |
0.529 |
|
2006 |
Studer SM, Joseph S. Unfolding of mRNA secondary structure by the bacterial translation initiation complex. Molecular Cell. 22: 105-15. PMID 16600874 DOI: 10.1016/J.Molcel.2006.02.014 |
0.71 |
|
2006 |
Feinberg JS, Joseph S. Ribose 2'-hydroxyl groups in the 5' strand of the acceptor arm of P-site tRNA are not essential for EF-G catalyzed translocation. Rna (New York, N.Y.). 12: 580-8. PMID 16489185 DOI: 10.1261/Rna.2290706 |
0.801 |
|
2005 |
Sanbonmatsu KY, Joseph S, Tung CS. Simulating movement of tRNA into the ribosome during decoding. Proceedings of the National Academy of Sciences of the United States of America. 102: 15854-9. PMID 16249344 DOI: 10.1073/Pnas.0503456102 |
0.457 |
|
2005 |
Phelps SS, Joseph S, Draper DE. Non-bridging phosphate oxygen atoms within the tRNA anticodon stem-loop are essential for ribosomal a site binding and translocation Journal of Molecular Biology. 349: 288-301. PMID 15890196 DOI: 10.1016/J.Jmb.2005.03.079 |
0.483 |
|
2005 |
Ghosh S, Joseph S. Nonbridging phosphate oxygens in 16S rRNA important for 30S subunit assembly and association with the 50S ribosomal subunit. Rna (New York, N.Y.). 11: 657-67. PMID 15811917 DOI: 10.1261/Rna.7224305 |
0.417 |
|
2004 |
Phelps SS, Malkiewicz A, Agris PF, Joseph S. Modified nucleotides in tRNA(Lys) and tRNA(Val) are important for translocation. Journal of Molecular Biology. 338: 439-44. PMID 15081802 DOI: 10.1016/J.Jmb.2004.02.070 |
0.537 |
|
2003 |
Sanbonmatsu KY, Joseph S. Understanding discrimination by the ribosome: stability testing and groove measurement of codon-anticodon pairs. Journal of Molecular Biology. 328: 33-47. PMID 12683995 DOI: 10.1016/S0022-2836(03)00236-5 |
0.439 |
|
2003 |
Studer SM, Feinberg JS, Joseph S. Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome. Journal of Molecular Biology. 327: 369-81. PMID 12628244 DOI: 10.1016/S0022-2836(03)00146-3 |
0.784 |
|
2003 |
Joseph S. After the ribosome structure: how does translocation work? Rna (New York, N.Y.). 9: 160-4. PMID 12554856 DOI: 10.1261/Rna.2163103 |
0.319 |
|
2002 |
Phelps SS, Jerinic O, Joseph S. Universally conserved interactions between the ribosome and the anticodon stem-loop of A site tRNA important for translocation. Molecular Cell. 10: 799-807. PMID 12419224 DOI: 10.1016/S1097-2765(02)00686-X |
0.499 |
|
2002 |
Tung CS, Joseph S, Sanbonmatsu KY. All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nature Structural Biology. 9: 750-5. PMID 12244297 DOI: 10.1038/Nsb841 |
0.362 |
|
2002 |
Ma C, Baker NA, Joseph S, McCammon JA. Binding of aminoglycoside antibiotics to the small ribosomal subunit: a continuum electrostatics investigation. Journal of the American Chemical Society. 124: 1438-42. PMID 11841313 DOI: 10.1021/Ja016830+ |
0.395 |
|
2001 |
Feinberg JS, Joseph S. Identification of molecular interactions between P-site tRNA and the ribosome essential for translocation. Proceedings of the National Academy of Sciences of the United States of America. 98: 11120-5. PMID 11562497 DOI: 10.1073/Pnas.211184098 |
0.8 |
|
2000 |
Jerinic O, Joseph S. Conformational changes in the ribosome induced by translational miscoding agents. Journal of Molecular Biology. 304: 707-713. PMID 11124020 DOI: 10.1006/Jmbi.2000.4269 |
0.362 |
|
2000 |
Joseph S, Noller HF. [13] Directed hydroxyl radical probing using iron(II) tethered to RNA Methods in Enzymology. 318: 175-190. PMID 10889988 DOI: 10.1016/S0076-6879(00)18052-8 |
0.545 |
|
2000 |
Joseph S, Whirl ML, Kondo D, Noller HF, Altman RB. Calculation of the relative geometry of tRNAs in the ribosome from directed hydroxyl-radical probing data Rna. 6: 220-232. PMID 10688361 DOI: 10.1017/S1355838200992112 |
0.675 |
|
1999 |
Samaha RR, Joseph S, O'Brien B, O'Brien TW, Noller HF. Site-directed hydroxyl radical probing of 30S ribosomal subunits by using Fe(II) tethered to an interruption in the 16S rRNA chain Proceedings of the National Academy of Sciences of the United States of America. 96: 366-370. PMID 9892639 DOI: 10.1073/Pnas.96.2.366 |
0.654 |
|
1998 |
Joseph S, Noller HF. EF-G-catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome Embo Journal. 17: 3478-3483. PMID 9628883 DOI: 10.1093/Emboj/17.12.3478 |
0.673 |
|
1997 |
Joseph S, Weiser B, Noller HF. Mapping the inside of the ribosome with an RNA helical ruler Science. 278: 1093-1098. PMID 9353184 DOI: 10.1126/Science.278.5340.1093 |
0.64 |
|
1996 |
Joseph S, Noller HF. Mapping the rRNA neighborhood of the acceptor end of tRNA in the ribosome. The Embo Journal. 15: 910-6. PMID 8631311 DOI: 10.1002/J.1460-2075.1996.Tb00425.X |
0.635 |
|
1996 |
Noller HF, Green R, Heilek G, Hoffarth V, Hüttenhofer A, Joseph S, Lee I, Lieberman K, Mankin A, Merryman C, Powers T, Puglisi EV, Samaha RR, Weiser B. Erratum: Structure and function of ribosomal RNA Biochemistry and Cell Biology. 74: 417-417. DOI: 10.1139/O96-045 |
0.702 |
|
1995 |
Noller HF, Green R, Heilek G, Hoffarth V, Hüttenhofer A, Joseph S, Lee I, Lieberman K, Mankin A, Merryman C. Structure and function of ribosomal RNA. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 73: 997-1009. PMID 8722015 DOI: 10.1139/O95-107 |
0.782 |
|
1993 |
Berzal-Herranz A, Joseph S, Chowrira BM, Butcher SE, Burke JM. Essential nucleotide sequences and secondary structure elements of the hairpin ribozyme. The Embo Journal. 12: 2567-73. PMID 8508779 DOI: 10.1002/J.1460-2075.1993.Tb05912.X |
0.723 |
|
1993 |
Joseph S, Berzal-Herranz A, Chowrira BM, Butcher SE, Burke JM. Substrate selection rules for the hairpin ribozyme determined by in vitro selection, mutation, and analysis of mismatched substrates. Genes & Development. 7: 130-8. PMID 7678568 DOI: 10.1101/Gad.7.1.130 |
0.692 |
|
1992 |
Berzal-Herranz A, Joseph S, Burke JM. In vitro selection of active hairpin ribozymes by sequential RNA-catalyzed cleavage and ligation reactions Genes and Development. 6: 129-134. PMID 1730406 DOI: 10.1101/Gad.6.1.129 |
0.576 |
|
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