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Hidden Markov models in computational biology: Applications to protein modeling
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Krogh A, Brown B, Mian IS, Sjolander K, Haussler D: Hidden Markov models in computational biology: applications to protein modeling. J Mol Biol 1994, 235:1501-1531. This is the paper that introduced the use of HMM methods for protein and DNA sequence profiles.
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Krogh, A.1
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Saldi P, Chauvin Y, Hunkapiller T, McClure MA: Hidden Markov models of biological primary sequence information. Proc Natl Acad Sci USA 1994, 91:1059-1063.
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Saldi, P.1
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Maximum discrimination hidden Markov models of sequence consensus
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Eddy SR, Mitchison G, Durbin R: Maximum discrimination hidden Markov models of sequence consensus. J Comput Biol 1995, 2:9-23. This paper constitutes a principled HMM-style contribution to the ever-increasing number of sequence-weighting methods. It introduces an alternative to maximum likelihood parameter estimation that compensates for biased sequence representation.
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J Comput Biol
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Eddy, S.R.1
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Churchill GA: Stochastic models for heterogeneous DNA sequences. Bull Math Biol 1989, 51:79-94.
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Stultz CM, White JV, Smith TF: Structural analysis based on state-space modeling. Protein Sci 1993, 2:305-314.
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White, J.V.2
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White JV, Stultz CM, Smith TF: Protein classification by stochastic modeling and optimal filtering of amino-acid sequences. Math Biosci 1994, 119:35-75.
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Rabiner LR: A tutorial on hidden Markov models and selected applications in speech recognition. Proc IEEE 1989, 77:257-286.
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Godzik A, Kolinski A, Skolnick J: Topology fingerprint approach to the inverse protein folding problem. J Mol Biol 1992, 227:227-238.
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Tree-based maximal likelihood likelihood substitution matrices and hidden Markov models
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Mitchison GJ, Durbin RM: Tree-based maximal likelihood likelihood substitution matrices and hidden Markov models. J Mol Evol 1995, 41:1139-1151.
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Baldi P, Chauvin Y: Smooth on-line learning algorithms for hidden Markov models. Neural Computation 1994, 6:305-316.
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Edited by Rawlings C, Clark D, Altman R, Hunter L, Lengauer T, Wodak S. Menlo Park: AAAI Press
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Eddy, S.R.1
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The posterior probability distribution of alignments and its application to parameter estimation of evolutionary trees and to optimization of multiple alignments
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Allison L, Wallace CS: The posterior probability distribution of alignments and its application to parameter estimation of evolutionary trees and to optimization of multiple alignments. J Mol Evol 1994, 39:418-430. The authors' work is HMM-ish in character, but written in the language of information theory (minimum message length) rather than probabilistic modeling (maximum likelihood). The contrast is instructive.
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J Mol Evol
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Allison, L.1
Wallace, C.S.2
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Protein fold recognition
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Shortle D: Protein fold recognition. Nat Struct Biol 1995, 2:91-93. This is a short review of the Asilomar conference, at which current methods for protein structure prediction were rigorously compared. Be aware, though, that Shortle confuses threading methods, which deal with pairwise residue correlations in protein structure, with HMMs, which don't.
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Nat Struct Biol
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Shortle, D.1
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Using Dirichlet mixture priors to derive hidden Markov models for protein families
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Edited by Hunter L, Searls D, Shavlik J. Menlo Park: AAAI Press
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Brown M, Hughey R, Krogh A, Mian IS, Sjolander K, Haussler D: Using Dirichlet mixture priors to derive hidden Markov models for protein families. Proceedings of the First International Conference on Intelligent Systems for Molecular Biology. Edited by Hunter L, Searls D, Shavlik J. Menlo Park: AAAI Press; 1993:47-55.
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Brown, M.1
Hughey, R.2
Krogh, A.3
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Sjolander, K.5
Haussler, D.6
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Evaluating regularizes for estimating distributions of amino acids
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Edited by Rawlings C, Clark D, Altman R, Hunter L, Lengauer T, Wodak S. Menlo Park: AAAI Press
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Karplus K: Evaluating regularizes for estimating distributions of amino acids. Proceedings of the Third International Conference on Intelligent Systems in Molecular Biology. Edited by Rawlings C, Clark D, Altman R, Hunter L, Lengauer T, Wodak S. Menlo Park: AAAI Press; 1995:188-196.
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Substitution matrices and hidden Markov models
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Baldi P: Substitution matrices and hidden Markov models. J Comput Biol 1995, 2:487-491.
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SCOP: A structural classification of proteins database for the investigation of sequences and structures
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Murzin A, Brenner SE, Hubbard T, Chothia C: SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995, 247:536-540.
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A hidden Markov model that finds genes in E. coli DNA
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Krogh A, Mian IS, Haussler D: A hidden Markov model that finds genes in E. coli DNA. Nucleic Acids Res 1994, 22:4768-4778. This is a nice illustration of the power of HMM methods to integrate various kinds of information into a single probabilistic model. Krogh's gene model includes a statistical description of ribosome binding sites, start and stop codons, codon usage, and intergenic repetitive elements.
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Nucleic Acids Res
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Prediction of protein secondary structure by the hidden Markov model
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Asai K, Hayamizu S, Handa KI: Prediction of protein secondary structure by the hidden Markov model. Comput Appl Biosci 1993, 9:141-146.
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Statistical methods for polyploid radiation hybrid mapping
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Lange K, Boehnke M, Cox DR, Lunetta KI: Statistical methods for polyploid radiation hybrid mapping. Genome Res 1995, 5:136-150.
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RNA sequence analysis using covariance models
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Eddy SR, Durbin R: RNA sequence analysis using covariance models. Nucleic Acids Res 1994, 22:2079-2088.
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Nucleic Acids Res
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Stochastic context-free grammars for tRNA modeling
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Haussler D, Sakakibara Y, Brown M: Stochastic context-free grammars for tRNA modeling. Nucleic Acids Res 1994, 22:5112-5120.
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Nucleic Acids Res
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Predicting coiled coils by use of pairwise residue correlations
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Berger B, Wilson DB, Wolf E, Tonchev T, Milla M, Kim PS: Predicting coiled coils by use of pairwise residue correlations. Proc Natl Acad Sci USA 1995, 92:8259-8263. The importance of taking pairwise residue correlations into account in protein sequence-structure analysis is controversial. If pairwise correlation is relatively unimportant, HMMs can be as good as the more complicated 'threading' methods for protein inverse folding for a fraction of the computational cost. To date, this paper is one of the few arguments for the importance of modeling pairwise residue correlations that I find convincing. The approach of Berger et al. is a simple Markov random field, although they don't explicitly call it such in the paper.
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Proc Natl Acad Sci USA
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Berger, B.1
Wilson, D.B.2
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Modeling protein cores with Markov random fields
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White JV, Muchnik I, Smith TF: Modeling protein cores with Markov random fields. Math Biosci 1994, 124:149-179.
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Math Biosci
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Tatusov RL, Altschul SF, Koonin EV: Detection of conserved segments in proteins: Iterative scanning of sequence databases with alignment blocks. Proc Natl Acad Sci USA 1994, 91:12091-12095.
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Tatusov, R.L.1
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