Satish K. Nair

Affiliations: 
University of Illinois, Urbana-Champaign, Urbana-Champaign, IL 
Area:
Natural products biosynthesis, bacterial signalling, X-ray crystallography
Website:
https://mcb.illinois.edu/faculty/profile/snair/
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"Satish K. Nair"
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Cross-listing: Crystallography Tree

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Publications

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Vignale FA, Hernandez Garcia A, Modenutti CP, et al. (2025) Yerba mate () genome provides new insights into convergent evolution of caffeine biosynthesis. Elife. 14
Rodriguez Carrero RJ, Lloyd CT, Borkar J, et al. (2025) Genetic and biochemical characterization of a radical SAM enzyme required for post-translational glutamine methylation of methyl-coenzyme M reductase. Mbio. e0354624
Luo S, Li XR, Gong XT, et al. (2024) Trojan horse peptide conjugates remodel the activity spectrum of clinical antibiotics. Proceedings of the National Academy of Sciences of the United States of America. 122: e2319483121
Pei ZF, Vior NM, Zhu L, et al. (2024) Biosynthesis of peptide-nucleobase hybrids in ribosomal peptides. Nature Chemical Biology
Cossu M, Catlin D, Elliott SJ, et al. (2024) Structural organization of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina acetivorans. Structure (London, England : 1993)
Chaban A, Minakhin L, Goldobina E, et al. (2024) Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail. Nature Communications. 15: 317
Pei ZF, Zhu L, Nair SK. (2023) Core-dependent post-translational modifications guide the biosynthesis of a new class of hypermodified peptides. Nature Communications. 14: 7734
Hernandez Garcia A, Nair SK. (2023) Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase. Acs Central Science. 9: 1944-1956
Ongpipattanakul C, Liu S, Luo Y, et al. (2023) The mechanism of thia-Michael addition catalyzed by LanC enzymes. Proceedings of the National Academy of Sciences of the United States of America. 120: e2217523120
Park R, Ongpipattanakul C, Nair SK, et al. (2022) Designer installation of a substrate recruitment domain to tailor enzyme specificity. Nature Chemical Biology
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