| Year |
Citation |
Score |
| 2023 |
Prangley E, Korennykh A. 2-5A-Mediated decay (2-5AMD): from antiviral defense to control of host RNA. Critical Reviews in Biochemistry and Molecular Biology. 1-15. PMID 36939319 DOI: 10.1080/10409238.2023.2181308 |
0.374 |
|
| 2021 |
Chitrakar A, Solorio-Kirpichyan K, Prangley E, Rath S, Du J, Korennykh A. Introns encode dsRNAs undetected by RIG-I/MDA5/interferons and sensed via RNase L. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34772806 DOI: 10.1073/pnas.2102134118 |
0.341 |
|
| 2019 |
Rath S, Prangley E, Donovan J, Demarest K, Wingreen NS, Meir Y, Korennykh A. Concerted 2-5A-Mediated mRNA Decay and Transcription Reprogram Protein Synthesis in the dsRNA Response. Molecular Cell. PMID 31494033 DOI: 10.1016/J.Molcel.2019.07.027 |
0.455 |
|
| 2019 |
Estrella MA, Du J, Chen L, Rath S, Prangley E, Chitrakar A, Aoki T, Schedl P, Rabinowitz J, Korennykh A. The metabolites NADP and NADPH are the targets of the circadian protein Nocturnin (Curled). Nature Communications. 10: 2367. PMID 31147539 DOI: 10.1038/S41467-019-10125-Z |
0.343 |
|
| 2019 |
Chitrakar A, Rath S, Donovan J, Demarest K, Li Y, Sridhar RR, Weiss SR, Kotenko SV, Wingreen NS, Korennykh A. Real-time 2-5A kinetics suggest that interferons β and λ evade global arrest of translation by RNase L. Proceedings of the National Academy of Sciences of the United States of America. PMID 30655338 DOI: 10.1073/Pnas.1818363116 |
0.401 |
|
| 2018 |
Estrella MA, Du J, Korennykh A. Crystal Structure of Human Nocturnin Catalytic Domain. Scientific Reports. 8: 16294. PMID 30389976 DOI: 10.1038/S41598-018-34615-0 |
0.426 |
|
| 2017 |
Oakes SR, Gallego-Ortega D, Stanford PM, Junankar S, Au WWY, Kikhtyak Z, von Korff A, Sergio CM, Law AMK, Castillo LE, Allerdice SL, Young AIJ, Piggin C, Whittle B, Bertram E, ... ... Korennykh A, et al. A mutation in the viral sensor 2'-5'-oligoadenylate synthetase 2 causes failure of lactation. Plos Genetics. 13: e1007072. PMID 29117179 DOI: 10.1371/Journal.Pgen.1007072 |
0.373 |
|
| 2017 |
Donovan J, Rath S, Kolet-Mandrikov D, Korennykh A. Rapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machinery. Rna (New York, N.Y.). 23: 1660-1671. PMID 28808124 DOI: 10.1261/Rna.062000.117 |
0.48 |
|
| 2017 |
Li Y, Banerjee S, Goldstein SA, Dong B, Gaughan C, Rath S, Donovan J, Korennykh AV, Silverman RH, Weiss SR. Ribonuclease L mediates the cell-lethal phenotype of the double-stranded RNA editing enzyme ADAR1 in a human cell line. Elife. 6. PMID 28362255 DOI: 10.7554/Elife.25687 |
0.4 |
|
| 2017 |
Li Y, Banerjee S, Goldstein SA, Dong B, Gaughan C, Rath S, Donovan J, Korennykh A, Silverman RH, Weiss SR. Author response: Ribonuclease L mediates the cell-lethal phenotype of double-stranded RNA editing enzyme ADAR1 deficiency in a human cell line Elife. DOI: 10.7554/Elife.25687.026 |
0.394 |
|
| 2015 |
Rath S, Donovan J, Whitney G, Chitrakar A, Wang W, Korennykh A. Human RNase L tunes gene expression by selectively destabilizing the microRNA-regulated transcriptome. Proceedings of the National Academy of Sciences of the United States of America. PMID 26668391 DOI: 10.1073/Pnas.1513034112 |
0.337 |
|
| 2015 |
Mendez AS, Alfaro J, Morales-Soto MA, Dar AC, McCullagh E, Gotthardt K, Li H, Acosta-Alvear D, Sidrauski C, Korennykh AV, Bernales S, Shokat KM, Walter P. Endoplasmic reticulum stress-independent activation of unfolded protein response kinases by a small molecule ATP-mimic. Elife. 4. PMID 25986605 DOI: 10.7554/Elife.05434 |
0.376 |
|
| 2015 |
Donovan J, Whitney G, Rath S, Korennykh A. Structural mechanism of sensing long dsRNA via a noncatalytic domain in human oligoadenylate synthetase 3. Proceedings of the National Academy of Sciences of the United States of America. 112: 3949-54. PMID 25775560 DOI: 10.1073/Pnas.1419409112 |
0.451 |
|
| 2015 |
Mendez AS, Alfaro J, Morales-Soto MA, Dar AC, McCullagh E, Gotthardt K, Li H, Acosta-Alvear D, Sidrauski C, Korennykh AV, Bernales S, Shokat KM, Walter P. Author response: Endoplasmic reticulum stress-independent activation of unfolded protein response kinases by a small molecule ATP-mimic Elife. DOI: 10.7554/Elife.05434.022 |
0.328 |
|
| 2014 |
Han Y, Donovan J, Rath S, Whitney G, Chitrakar A, Korennykh A. Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response. Science (New York, N.Y.). 343: 1244-8. PMID 24578532 DOI: 10.1126/Science.1249845 |
0.476 |
|
| 2013 |
Donovan J, Dufner M, Korennykh A. Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1. Proceedings of the National Academy of Sciences of the United States of America. 110: 1652-7. PMID 23319625 DOI: 10.1073/Pnas.1218528110 |
0.503 |
|
| 2012 |
Han Y, Whitney G, Donovan J, Korennykh A. Innate immune messenger 2-5A tethers human RNase L into active high-order complexes. Cell Reports. 2: 902-13. PMID 23084743 DOI: 10.1016/J.Celrep.2012.09.004 |
0.364 |
|
| 2012 |
Korennykh A, Walter P. Structural basis of the unfolded protein response. Annual Review of Cell and Developmental Biology. 28: 251-77. PMID 23057742 DOI: 10.1146/Annurev-Cellbio-101011-155826 |
0.351 |
|
| 2011 |
Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Stroud RM, Zhang C, Shokat KM, Walter P. Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. Bmc Biology. 9: 48. PMID 21729334 DOI: 10.1186/1741-7007-9-48 |
0.387 |
|
| 2011 |
Korennykh AV, Korostelev AA, Egea PF, Finer-Moore J, Stroud RM, Zhang C, Shokat KM, Walter P. Structural and functional basis for RNA cleavage by Ire1. Bmc Biology. 9: 47. PMID 21729333 DOI: 10.1186/1741-7007-9-47 |
0.504 |
|
| 2011 |
Rubio C, Pincus D, Korennykh A, Schuck S, El-Samad H, Walter P. Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity. The Journal of Cell Biology. 193: 171-84. PMID 21444684 DOI: 10.1083/Jcb.201007077 |
0.413 |
|
| 2011 |
Plantinga MJ, Korennykh AV, Piccirilli JA, Correll CC. The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues. Biochemistry. 50: 3004-13. PMID 21417210 DOI: 10.1021/Bi1018336 |
0.638 |
|
| 2010 |
Li H, Korennykh AV, Behrman SL, Walter P. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proceedings of the National Academy of Sciences of the United States of America. 107: 16113-8. PMID 20798350 DOI: 10.1073/Pnas.1010580107 |
0.376 |
|
| 2009 |
Aragón T, van Anken E, Pincus D, Serafimova IM, Korennykh AV, Rubio CA, Walter P. Messenger RNA targeting to endoplasmic reticulum stress signalling sites. Nature. 457: 736-40. PMID 19079237 DOI: 10.1038/Nature07641 |
0.437 |
|
| 2009 |
Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Zhang C, Shokat KM, Stroud RM, Walter P. The unfolded protein response signals through high-order assembly of Ire1. Nature. 457: 687-93. PMID 19079236 DOI: 10.1038/Nature07661 |
0.47 |
|
| 2008 |
Plantinga MJ, Korennykh AV, Piccirilli JA, Correll CC. Electrostatic interactions guide the active site face of a structure-specific ribonuclease to its RNA substrate. Biochemistry. 47: 8912-8. PMID 18672906 DOI: 10.1021/Bi800592G |
0.621 |
|
| 2007 |
Korennykh AV, Plantinga MJ, Correll CC, Piccirilli JA. Linkage between substrate recognition and catalysis during cleavage of sarcin/ricin loop RNA by restrictocin. Biochemistry. 46: 12744-56. PMID 17929942 DOI: 10.1021/Bi700931Y |
0.611 |
|
| 2007 |
Korennykh AV, Correll CC, Piccirilli JA. Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. Rna (New York, N.Y.). 13: 1391-6. PMID 17626843 DOI: 10.1261/Rna.619707 |
0.565 |
|
| 2006 |
Korennykh AV, Piccirilli JA, Correll CC. The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins. Nature Structural & Molecular Biology. 13: 436-43. PMID 16604082 DOI: 10.1038/Nsmb1082 |
0.607 |
|
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