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Zhou, H.X. (2004) Improving the understanding of human genetic diseases through predictions of protein structures and protein-protein interaction sites. Current Medicinal Chemistry, 11, 539-549.

has been cited by the following article:

• TITLE: Mutation pattern in human adrenoleukodystrophy protein in terms of amino-acid pair predictability

  AUTHORS: Shao-Min Yan, Guang Wu

  KEYWORDS: Adrenoleukodystrophy; Amino-Acid Pair Predictability; Mutation Pattern

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.3 No.3, April 8, 2010

  ABSTRACT: The mutation pattern in protein is a very important feature and is studied through various approaches including the study on mutation pattern in domains where amino acids are converted into numbers from letters. In this study, we converted the amino acids in human adrenoleukodystrophy protein with its 128 missense mutations into random domain using the amino-acid pair predictability, and then we studied their mutation patterns. The results show 1) the mutations are more likely to target the amino-acid pairs whose actual frequency is larger than their predicted one, 2) the mutations are more likely to form the amino-acid pairs whose actual frequency is smaller than their predicted frequency, 3) mutations are more likely to occur at unpredictable amino-acid pairs, and 4) mutations have the trend to narrow the difference between predicted and actual frequencies of amino-acid pairs.