Global fold determination from a small number of distance restraints.

By A. Aszódi, M. J. Gradwell, William R. Taylor. 1995

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1. Yang Zhang
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6. Allison N. Tegge
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Citations in the corpus

• Distance-based protein folding powered by deep learning (2018, methodology): “For example, Aszodi et al 22 predicted inter-residue distance from pairwise conserved hydrophobicity score and used it to reconstruct 3D models of a protein.”
• Toward an accurate prediction of inter-residue distances in proteins using 2D recursive neural networks (2014, background): “To our knowledge, only a few studies concerning inter-residue distances exist in the literature where a limited number of distance restraints have been predicted [31,32] or only an inter-residue distance distribution has been studied [33,34].”
• Deep learning extends de novo protein modelling coverage of genomes using iteratively predicted structural constraints (2018, unknown): “the DRAGON method of Taylor and Aszódi ​[8]​.”
• Prediction of contact maps by GIOHMMs and recurrent neural networks using lateral propagation from all four cardinal corners (2002, methodology): “, 2001a), distances (Aszodi et al., 1995; Lund et al., 1997; Gorodkin et al., 1999), and contact maps (Fariselli et al.”
• MONSSTER: a method for folding globular proteins with a small number of distance restraints. (1997, methodology): “By providing an initial guess of a structure for subsequent refinement, a successful method could be a very useful tool in NMR-based model building (Aszodi et al., 1995; Smith-Brown et al., 1993).”
• Machine Learning Methods for Protein Structure Prediction (2008, background): “D reconstruction algorithms that can tolerate the noise contained in predicted contact maps.”
• DESTINI: A deep-learning approach to contact-driven protein structure prediction (2019, background): “An early study estimates that, for single-domain proteins less than 200 amino acids (AAs), one can assemble a structural model within a 5 Å root-mean-square-deviation (RMSD) from the native structure if more than L /4 long-range protein contacts are known 8 , where L is the length of the protein.”
• Defining an Essence of Structure Determining Residue Contacts in Proteins (2009, background): “For several years, the distance constraints and other stereo chemical and biophysical restraints have been employed in computational restraint-based protein modelling [7–13].”