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Wang, W. and Hecht, M.H. (2002) Rationally designed mutations convert de novo amyloid-like fibrils into monomerric β-sheet proteins. Proceedings of the National Academy of Sciences of the United States of America, 99, 2760-2765.
http://dx.doi.org/10.1073/pnas.052706199

has been cited by the following article:

• TITLE: Geometrical criteria for left-handed twists within protein beta-strands

  AUTHORS: Bernard Caudron, Jean-Luc Jestin

  KEYWORDS: Beta-Sheet; Protein Data Bank; Protein Backbone; Protein Structure; Model Quality Assessment; CASP

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.5 No.1, February 25, 2014

  ABSTRACT: Using a statistical analysis on beta-sheet structures from the Protein Data Bank, characteristic angles within beta-strands were correlated to the nature of the side chains. The twists were computed from the atomic coordinates of five consecutive amino acids’ alpha carbons from single beta-strand sequences. Conditions on the angles for twists to be mainly left-handed are given together with the frequency of occurrence for these non-standard geometrical properties within protein beta-strands. Applications in protein structure prediction and CASP challenges in particular are envisioned by making use of the probabilities of occurrence in protein structures of angle value ranges for given amino acids.