Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation S Miyazawa, RL Jernigan Macromolecules 18 (3), 534-552, 1985 | 1984 | 1985 |
Residue–residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading S Miyazawa, RL Jernigan Journal of molecular biology 256 (3), 623-644, 1996 | 1467 | 1996 |
Two types of amino acid substitutions in protein evolution T Miyata, S Miyazawa, T Yasunaga Journal of molecular evolution 12, 219-236, 1979 | 530 | 1979 |
Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the β-chain of major … T Miyauchi, T Kanekura, A Yamaoka, M Ozawa, S Miyazawa, ... The Journal of Biochemistry 107 (2), 316-323, 1990 | 234 | 1990 |
Self‐consistent estimation of inter‐residue protein contact energies based on an equilibrium mixture approximation of residues S Miyazawa, RL Jernigan Proteins: Structure, Function, and Bioinformatics 34 (1), 49-68, 1999 | 225 | 1999 |
Only DFL16, DSP2, and DQ52 gene families exist in mouse immunoglobulin heavy chain diversity gene loci, of which DFL16 and DSP2 originate from the same primordial DH gene Y Ichihara, H Hayashida, S Miyazawa, Y Kurosawa European journal of immunology 19 (10), 1849-1854, 1989 | 152 | 1989 |
An empirical energy potential with a reference state for protein fold and sequence recognition S Miyazawa, RL Jernigan Proteins: Structure, Function, and Bioinformatics 36 (3), 357-369, 1999 | 130 | 1999 |
A reliable sequence alignment method based on probabilities of residue correspondences S Miyazawa Protein Engineering, Design and Selection 8 (10), 999-1009, 1995 | 123 | 1995 |
A new substitution matrix for protein sequence searches based on contact frequencies in protein structures S Miyazawa, RL Jernigan Protein Engineering, Design and Selection 6 (3), 267-278, 1993 | 100 | 1993 |
Relationship between mutability, polarity and exteriority of amino acid residues in protein evolution M GO, S MIYAZAWA International journal of peptide and protein research 15 (3), 211-224, 1980 | 95 | 1980 |
How effective for fold recognition is a potential of mean force that includes relative orientations between contacting residues in proteins? S Miyazawa, RL Jernigan The Journal of chemical physics 122 (2), 2005 | 79 | 2005 |
Protein stability for single substitution mutants and the extent of local compactness in the denatured state S Miyazawa, RL Jernigan Protein Engineering, Design and Selection 7 (10), 1209-1220, 1994 | 75 | 1994 |
Evaluation of short‐range interactions as secondary structure energies for protein fold and sequence recognition S Miyazawa, RL Jernigan Proteins: Structure, Function, and Bioinformatics 36 (3), 347-356, 1999 | 50 | 1999 |
Equilibrium folding and unfolding pathways for a model protein S Miyazawa, RL Jernigan Biopolymers: Original Research on Biomolecules 21 (7), 1333-1363, 1982 | 37 | 1982 |
Identifying sequence–structure pairs undetected by sequence alignments S Miyazawa, RL Jernigan Protein Engineering 13 (7), 459-475, 2000 | 34 | 2000 |
Long‐and short‐range interactions in native protein structures are consistent/minimally frustrated in sequence space S Miyazawa, RL Jernigan Proteins: Structure, Function, and Bioinformatics 50 (1), 35-43, 2003 | 32 | 2003 |
Advantages of a mechanistic codon substitution model for evolutionary analysis of protein-coding sequences S Miyazawa PloS one 6 (12), e28892, 2011 | 21 | 2011 |
DNA Data Bank of Japan: Present Status and Future Plans S Miyazawa Computers and DNA: the proceedings of the Interface between Computation …, 1990 | 21* | 1990 |
Prediction of contact residue pairs based on co-substitution between sites in protein structures S Miyazawa PloS one 8 (1), e54252, 2013 | 18 | 2013 |
Selective constraints on amino acids estimated by a mechanistic codon substitution model with multiple nucleotide changes S Miyazawa PLoS One 6 (3), e17244, 2011 | 17 | 2011 |