| Year |
Citation |
Score |
| 2019 |
Luisi BF, Malhotra A. Decision letter: A dedicated diribonucleotidase resolves a key bottleneck for the terminal step of RNA degradation Elife. DOI: 10.7554/Elife.46313.052 |
0.417 |
|
| 2018 |
Aguero T, Jin Z, Owens D, Malhotra A, Newman K, Yang J, King ML. Combined functions of two RRMs in Dead-end1 mimic helicase activity to promote nanos1 translation in the germline. Molecular Reproduction and Development. PMID 30230100 DOI: 10.1002/Mrd.23062 |
0.35 |
|
| 2017 |
Schmier BJ, Nelersa CM, Malhotra A. Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Scientific Reports. 7: 11085. PMID 28894100 DOI: 10.1038/S41598-017-09403-X |
0.781 |
|
| 2016 |
Hossain ST, Malhotra A, Deutscher MP. How RNase R Degrades Structured RNA: Role of the Helicase Activity and the S1 Domain. The Journal of Biological Chemistry. PMID 26872969 DOI: 10.1074/Jbc.M116.717991 |
0.487 |
|
| 2016 |
Song L, Wang G, Malhotra A, Deutscher MP, Liang W. Reversible acetylation on Lys501 regulates the activity of RNase II. Nucleic Acids Research. PMID 26847092 DOI: 10.1093/Nar/Gkw053 |
0.385 |
|
| 2015 |
Hossain ST, Malhotra A, Deutscher MP. The Helicase Activity of Ribonuclease R Is Essential for Efficient Nuclease Activity. The Journal of Biological Chemistry. 290: 15697-706. PMID 25931119 DOI: 10.1074/Jbc.M115.650176 |
0.43 |
|
| 2015 |
Yuan F, Dutta T, Wang L, Song L, Gu L, Qian L, Benitez A, Ning S, Malhotra A, Deutscher MP, Zhang Y. Human DNA Exonuclease TREX1 Is Also an Exoribonuclease That Acts on Single-stranded RNA. The Journal of Biological Chemistry. 290: 13344-53. PMID 25855793 DOI: 10.1074/Jbc.M115.653915 |
0.507 |
|
| 2014 |
Schmier B, Nelersa C, Malhotra A. Structural Basis for the Novel Bidirectional Activity of the nanoRNase NrnA Acta Crystallographica Section a Foundations and Advances. 70: C212-C212. DOI: 10.1107/S2053273314097873 |
0.781 |
|
| 2013 |
Dutta T, Malhotra A, Deutscher MP. How a CCA sequence protects mature tRNAs and tRNA precursors from action of the processing enzyme RNase BN/RNase Z. The Journal of Biological Chemistry. 288: 30636-44. PMID 24022488 DOI: 10.1074/Jbc.M113.514570 |
0.441 |
|
| 2013 |
Lee SH, Ripke S, Neale BM, Faraone SV, Purcell SM, Perlis RH, Mowry BJ, Thapar A, Goddard ME, Witte JS, Absher D, Agartz I, Akil H, Amin F, ... ... Malhotra AK, et al. Genetic relationship between five psychiatric disorders estimated from genome-wide SNPs. Nature Genetics. 45: 984-94. PMID 23933821 DOI: 10.1038/Ng.2711 |
0.306 |
|
| 2012 |
Dutta T, Malhotra A, Deutscher MP. Exoribonuclease and endoribonuclease activities of RNase BN/RNase Z both function in vivo. The Journal of Biological Chemistry. 287: 35747-55. PMID 22893707 DOI: 10.1074/Jbc.M112.407403 |
0.474 |
|
| 2012 |
McDonald CB, Buffa L, Bar-Mag T, Salah Z, Bhat V, Mikles DC, Deegan BJ, Seldeen KL, Malhotra A, Sudol M, Aqeilan RI, Nawaz Z, Farooq A. Biophysical basis of the binding of WWOX tumor suppressor to WBP1 and WBP2 adaptors. Journal of Molecular Biology. 422: 58-74. PMID 22634283 DOI: 10.1016/J.Jmb.2012.05.015 |
0.346 |
|
| 2012 |
Schmier BJ, Seetharaman J, Deutscher MP, Hunt JF, Malhotra A. The structure and enzymatic properties of a novel RNase II family enzyme from Deinococcus radiodurans. Journal of Molecular Biology. 415: 547-59. PMID 22133431 DOI: 10.1016/J.Jmb.2011.11.031 |
0.772 |
|
| 2011 |
Nelersa CM, Schmier BJ, Malhotra A. Purification and crystallization of Bacillus subtilis NrnA, a novel enzyme involved in nanoRNA degradation. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 1235-8. PMID 22102036 DOI: 10.1107/S1744309111026509 |
0.758 |
|
| 2011 |
Liang W, Malhotra A, Deutscher MP. Acetylation regulates the stability of a bacterial protein: growth stage-dependent modification of RNase R. Molecular Cell. 44: 160-6. PMID 21981926 DOI: 10.1016/J.Molcel.2011.06.037 |
0.348 |
|
| 2010 |
Steen KA, Malhotra A, Weeks KM. Selective 2'-hydroxyl acylation analyzed by protection from exoribonuclease. Journal of the American Chemical Society. 132: 9940-3. PMID 20597503 DOI: 10.1021/Ja103781U |
0.39 |
|
| 2008 |
Larrea AA, Pedroso IM, Malhotra A, Myers RS. Identification of two conserved aspartic acid residues required for DNA digestion by a novel thermophilic Exonuclease VII in Thermotoga maritima. Nucleic Acids Research. 36: 5992-6003. PMID 18812402 DOI: 10.1093/Nar/Gkn588 |
0.722 |
|
| 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 |
0.47 |
|
| 2007 |
Vaidyanathan PP, Deutscher MP, Malhotra A. RluD, a highly conserved pseudouridine synthase, modifies 50S subunits more specifically and efficiently than free 23S rRNA. Rna (New York, N.Y.). 13: 1868-76. PMID 17872507 DOI: 10.1261/Rna.711207 |
0.6 |
|
| 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 |
0.478 |
|
| 2007 |
Abaffy T, Malhotra A, Luetje CW. The molecular basis for ligand specificity in a mouse olfactory receptor: a network of functionally important residues. The Journal of Biological Chemistry. 282: 1216-24. PMID 17114180 DOI: 10.1074/Jbc.M609355200 |
0.322 |
|
| 2007 |
Tolun AA, Dickerson IM, Malhotra A. Overexpression and purification of human calcitonin gene-related peptide-receptor component protein in Escherichia coli. Protein Expression and Purification. 52: 167-74. PMID 17067815 DOI: 10.1016/J.Pep.2006.09.008 |
0.664 |
|
| 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 |
0.52 |
|
| 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 |
0.46 |
|
| 2006 |
Hsiao B, Mihalak KB, Repicky SE, Everhart D, Mederos AH, Malhotra A, Luetje CW. Determinants of zinc potentiation on the alpha4 subunit of neuronal nicotinic receptors. Molecular Pharmacology. 69: 27-36. PMID 16189299 DOI: 10.1124/Mol.105.015164 |
0.302 |
|
| 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 |
0.458 |
|
| 2004 |
Blits-Huizinga CT, Nelersa CM, Malhotra A, Liebl DJ. Ephrins and their receptors: binding versus biology. Iubmb Life. 56: 257-265. PMID 15370889 DOI: 10.1080/15216540412331270076 |
0.311 |
|
| 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 |
0.319 |
|
| 2004 |
Everhart D, Cartier GE, Malhotra A, Gomes AV, McIntosh JM, Luetje CW. Determinants of potency on alpha-conotoxin MII, a peptide antagonist of neuronal nicotinic receptors. Biochemistry. 43: 2732-7. PMID 15005608 DOI: 10.1021/Bi036180H |
0.306 |
|
| 2004 |
Kaya Y, Del Campo M, Ofengand J, Malhotra A. Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold. The Journal of Biological Chemistry. 279: 18107-10. PMID 14999002 DOI: 10.1074/Jbc.C400072200 |
0.627 |
|
| 2004 |
Del Campo M, Ofengand J, Malhotra A. Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli. Rna (New York, N.Y.). 10: 231-9. PMID 14730022 DOI: 10.1261/Rna.5187404 |
0.526 |
|
| 2003 |
Del Campo M, Ofengand J, Malhotra A. Purification and crystallization of Escherichia coli pseudouridine synthase RluD. Acta Crystallographica. Section D, Biological Crystallography. 59: 1871-3. PMID 14501142 DOI: 10.1107/S0907444903018468 |
0.421 |
|
| 2002 |
Fiedler TJ, Malhotra A. Crystallographic Studies of Bacterial Exoribonucleases. Thescientificworldjournal. 2: 53-54. PMID 29973801 DOI: 10.1100/Tsw.2002.27 |
0.526 |
|
| 2001 |
Ofengand J, Malhotra A, Remme J, Gutgsell NS, Del Campo M, Jean-Charles S, Peil L, Kaya Y. Pseudouridines and pseudouridine synthases of the ribosome. Cold Spring Harbor Symposia On Quantitative Biology. 66: 147-59. PMID 12762017 DOI: 10.1101/Sqb.2001.66.147 |
0.645 |
|
| 2000 |
Korzheva N, Mustaev A, Kozlov M, Malhotra A, Nikiforov V, Goldfarb A, Darst SA. A structural model of transcription elongation. Science (New York, N.Y.). 289: 619-25. PMID 10915625 DOI: 10.1126/Science.289.5479.619 |
0.427 |
|
| 1998 |
Polyakov A, Richter C, Malhotra A, Koulich D, Borukhov S, Darst SA. Visualization of the binding site for the transcript cleavage factor GreB on Escherichia coli RNA polymerase. Journal of Molecular Biology. 281: 465-73. PMID 9698562 DOI: 10.1006/Jmbi.1998.1958 |
0.508 |
|
| 1998 |
Malhotra A, Penczek P, Agrawal RK, Gabashvili IS, Grassucci RA, Jünemann R, Burkhardt N, Nierhaus KH, Frank J. Escherichia coli 70 S ribosome at 15 A resolution by cryo-electron microscopy: localization of fMet-tRNAfMet and fitting of L1 protein. Journal of Molecular Biology. 280: 103-16. PMID 9653034 DOI: 10.1006/Jmbi.1998.1859 |
0.505 |
|
| 1997 |
Koulich D, Orlova M, Malhotra A, Sali A, Darst SA, Borukhov S. Domain organization of Escherichia coli transcript cleavage factors GreA and GreB. The Journal of Biological Chemistry. 272: 7201-10. PMID 9054416 DOI: 10.1074/Jbc.272.11.7201 |
0.46 |
|
| 1996 |
Malhotra A, Severinova E, Darst SA. Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase. Cell. 87: 127-36. PMID 8858155 DOI: 10.1016/S0092-8674(00)81329-X |
0.515 |
|
| 1995 |
Leontis NB, Piotto ME, Hills MT, Malhotra A, Ouporov IV, Nussbaum JM, Gorenstein DG. Structural studies of DNA three-way junctions. Methods in Enzymology. 261: 183-207. PMID 8569495 DOI: 10.1016/S0076-6879(95)61010-3 |
0.361 |
|
| 1994 |
Easterwood TR, Major F, Malhotra A, Harvey SC. Orientations of transfer RNA in the ribosomal A and P sites. Nucleic Acids Research. 22: 3779-86. PMID 7937092 DOI: 10.1093/Nar/22.18.3779 |
0.339 |
|
| 1994 |
Harris ME, Nolan JM, Malhotra A, Brown JW, Harvey SC, Pace NR. Use of photoaffinity crosslinking and molecular modeling to analyze the global architecture of ribonuclease P RNA. The Embo Journal. 13: 3953-63. PMID 7521297 DOI: 10.1002/J.1460-2075.1994.Tb06711.X |
0.472 |
|
| 1994 |
Malhotra A, Tan RK, Harvey SC. Modeling large RNAs and ribonucleoprotein particles using molecular mechanics techniques. Biophysical Journal. 66: 1777-95. PMID 7521223 DOI: 10.1016/S0006-3495(94)80972-5 |
0.43 |
|
| 1994 |
Malhotra A, Harvey SC. A quantitative model of the Escherichia coli 16 S RNA in the 30 S ribosomal subunit. Journal of Molecular Biology. 240: 308-40. PMID 7518524 DOI: 10.1006/Jmbi.1994.1448 |
0.475 |
|
| 1993 |
Malhotra A, Gabb HA, Harvey SC. Modeling large nucleic acids Current Opinion in Structural Biology. 3: 241-246. DOI: 10.1016/S0959-440X(05)80159-9 |
0.335 |
|
| 1990 |
Malhotra A, Tan RK, Harvey SC. Prediction of the three-dimensional structure of Escherichia coli 30S ribosomal subunit: a molecular mechanics approach. Proceedings of the National Academy of Sciences of the United States of America. 87: 1950-4. PMID 2408047 DOI: 10.1073/Pnas.87.5.1950 |
0.48 |
|
| Show low-probability matches. |