Alexei V. Korennykh, Ph.D. - Publications

2005 University of Chicago, Chicago, IL 
chemistry and biochemistryof nucleic acids

16 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.64
2014 van Anken E, Pincus D, Coyle S, Aragón T, Osman C, Lari F, Gómez Puerta S, Korennykh AV, Walter P. Specificity in endoplasmic reticulum-stress signaling in yeast entails a step-wise engagement of HAC1 mRNA to clusters of the stress sensor Ire1. Elife. 3: e05031. PMID 25549299 DOI: 10.7554/Elife.05031  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
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  0.64
2004 Shcherbakova TA, Korennykh AV, Langen LMV, Sheldon RA, Švedas VK. Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis Journal of Molecular Catalysis B: Enzymatic. 31: 63-65. DOI: 10.1016/j.molcatb.2004.07.006  0.64
2003 Khimiuk AY, Korennykh AV, Van Langen LM, Van Rantwijk F, Sheldon RA, Švedas VK. Penicillin acylase-catalyzed peptide synthesis in aqueous medium: A chemo-enzymatic route to stereoisomerically pure diketopiperazines Tetrahedron Asymmetry. 14: 3123-3128. DOI: 10.1016/j.tetasy.2003.08.011  0.64
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