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Sergey Ovchinnikov

Showing results (1-10 of 83) with videos related to

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BMC Evolutionary Biology|March 14, 2012
Pseudoscorpion mitochondria show rearranged genes and genome-wide reductions of RNA gene sizes and inferred structures, yet typical nucleotide composition biasSergey Ovchinnikov, Susan E Masta
Current Opinion in Chemical Biology|September 21, 2021
Structure-based protein design with deep learningSergey Ovchinnikov, Po-Ssu Huang
Physical Review Letters|December 23, 2022
State-of-the-Art Estimation of Protein Model Accuracy Using AlphaFoldJames P Roney, Sergey Ovchinnikov
Proceedings of the National Academy of Sciences of the United States of America|September 7, 2013
Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich eraHetunandan Kamisetty, Sergey Ovchinnikov, David Baker
Elife|May 21, 2014
Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary informationSergey Ovchinnikov, Hetunandan Kamisetty, David Baker
Protein Science : a Publication of the Protein Society|December 14, 2024
Predicting absolute protein folding stability using generative modelsMatteo Cagiada, Sergey Ovchinnikov, Kresten Lindorff-Larsen
Bioinformatics (Oxford, England)|March 13, 2025
actifpTM: a refined confidence metric of AlphaFold2 predictions involving flexible regionsJulia K Varga, Sergey Ovchinnikov, Ora Schueler-Furman
Proceedings of the National Academy of Sciences of the United States of America|August 9, 2017
Origins of coevolution between residues distant in protein 3D structuresIvan Anishchenko, Sergey Ovchinnikov, Hetunandan Kamisetty, et al.
Biorxiv : the Preprint Server for Biology|December 3, 2025
CIRPIN: Learning Circular Permutation-Invariant Representations to Uncover Putative Protein HomologsAiden R Kolodziej, S Mazdak Abulnaga, Sergey Ovchinnikov
Science (New York, N.Y.)|July 13, 2019
Protein interaction networks revealed by proteome coevolutionQian Cong, Ivan Anishchenko, Sergey Ovchinnikov, et al.
Pageof 9

Showing results (1-10 of 83) with videos related to

Sort By:
Pageof 9
BMC Evolutionary Biology|March 14, 2012
Pseudoscorpion mitochondria show rearranged genes and genome-wide reductions of RNA gene sizes and inferred structures, yet typical nucleotide composition biasSergey Ovchinnikov, Susan E Masta
Current Opinion in Chemical Biology|September 21, 2021
Structure-based protein design with deep learningSergey Ovchinnikov, Po-Ssu Huang
Physical Review Letters|December 23, 2022
State-of-the-Art Estimation of Protein Model Accuracy Using AlphaFoldJames P Roney, Sergey Ovchinnikov
Proceedings of the National Academy of Sciences of the United States of America|September 7, 2013
Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich eraHetunandan Kamisetty, Sergey Ovchinnikov, David Baker
Elife|May 21, 2014
Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary informationSergey Ovchinnikov, Hetunandan Kamisetty, David Baker
Protein Science : a Publication of the Protein Society|December 14, 2024
Predicting absolute protein folding stability using generative modelsMatteo Cagiada, Sergey Ovchinnikov, Kresten Lindorff-Larsen
Bioinformatics (Oxford, England)|March 13, 2025
actifpTM: a refined confidence metric of AlphaFold2 predictions involving flexible regionsJulia K Varga, Sergey Ovchinnikov, Ora Schueler-Furman
Proceedings of the National Academy of Sciences of the United States of America|August 9, 2017
Origins of coevolution between residues distant in protein 3D structuresIvan Anishchenko, Sergey Ovchinnikov, Hetunandan Kamisetty, et al.
Biorxiv : the Preprint Server for Biology|December 3, 2025
CIRPIN: Learning Circular Permutation-Invariant Representations to Uncover Putative Protein HomologsAiden R Kolodziej, S Mazdak Abulnaga, Sergey Ovchinnikov
Science (New York, N.Y.)|July 13, 2019
Protein interaction networks revealed by proteome coevolutionQian Cong, Ivan Anishchenko, Sergey Ovchinnikov, et al.
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