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Plos One|March 30, 2011
Selective constraints on amino acids estimated by a mechanistic codon substitution model with multiple nucleotide changesSanzo MiyazawaPlos One|January 6, 2012
Advantages of a mechanistic codon substitution model for evolutionary analysis of protein-coding sequencesSanzo MiyazawaAdvances in Experimental Medicine and Biology|January 9, 2019
Prediction of Structures and Interactions from Genome InformationSanzo MiyazawaPlos One|January 24, 2013
Prediction of contact residue pairs based on co-substitution between sites in protein structuresSanzo MiyazawaBMC Evolutionary Biology|November 22, 2013
Superiority of a mechanistic codon substitution model even for protein sequences in phylogenetic analysisSanzo MiyazawaJournal of Theoretical Biology|August 29, 2017
Selection originating from protein stability/foldability: Relationships between protein folding free energy, sequence ensemble, and fitnessSanzo MiyazawaJournal of Theoretical Biology|December 19, 2015
Selection maintaining protein stability at equilibriumSanzo MiyazawaIEEE/ACM Transactions on Computational Biology and Bioinformatics|May 13, 2020
Boltzmann Machine Learning and Regularization Methods for Inferring Evolutionary Fields and Couplings From a Multiple Sequence AlignmentSanzo MiyazawaThe Journal of Chemical Physics|January 11, 2005
How effective for fold recognition is a potential of mean force that includes relative orientations between contacting residues in proteins?Sanzo Miyazawa, Robert L JerniganProteins|December 10, 2002
Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence spaceSanzo Miyazawa, Robert L JerniganPageof 2