"MD-based free-energy methods (26, 31), molecular mechanics calculations (32), and molecular modeling studies (33) have provided new insights into mutation-induced drug resistance mechanisms and the conformational transitions connecting active and inactive states (34-36)." (References 31 and 32 are our publications). In "Altered conformational landscape and dimerization dependency underpins the activation of EGFR by Alpha C - Beta 4 loop insertion mutations" published in PNAS by Zheng Ruan and Natarajan Kannan, Institute of Bioinformatics, University of Georgia, USA.
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"Recently, computational structural modeling and molecular dynamics (MD) simulations have helped us clarify the activation mechanism of EGFR at the atomic level (25-27). In addition, predictions of sensitivity of EGFR mutants to EGFR tyrosine kinase inhibitors were performed for several EGFR mutations using binding free energy calculated with MD simulation (28, 29) and fitness scores calculated by molecular docking simulation (30)." (References 28 and 29 are our publications). In "Molecular dynamics simulation-guided drug sensitivity prediction for lung cancer with rare EGFR mutations" published in PNAS by Shinnosuke Ikemura et al, Division of Pulmonary Medicine, Department of Medicine, Keio University, School of Medicine, Shinjuku-ku, 160-8582 Tokyo, Japan.
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"... a more recent study by Ma et al. [31] elegantly postulated a different response driven by the free binding energy of specific EGFR mutants with different TKIs." (Reference 31 is our publication). In "Different EGFR gene mutations in Exon 18, 19 and 21 as prognostic and predictive markers in NSCLC: A single institution analysis" published in Molecular Diagnosis & Therapy by Sabrina Rossi et al, Department of Medical Oncology, Catholic University of Sacred Heart, Largo A. Gemelli, 8, 00168 Rome, Italy.
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"Preclinical prediction of intrinsic resistance mechanisms of drug resistance has been reported. For kinase-directed therapies that would be expected to elicit intrinsic acquired resistance, structural analysis during drug design can identify mutations that would interfere with drug binding. Co-crystal structures and molecular modeling studies can identify amino acid residues essential to drug binding (79-81)." (Reference 81 is our publication). In "Durability of kinase-directed therapies - A network perspective on response and resistance" published in Molecular Cancer Therapeutics by Brion W. Murray and Nichol Miller, Oncology Research Unit, Pfizer Worldwide Research and Development, San Diego, California, USA.
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"Recently, Wang et al. reported the prediction of EGFR mutation-induced drugresistance in lung cancer, which is a major problem to be resolvedin cancer treatment [8]." (Reference 8 is our publication). In "Different EGFR gene mutations in Exon 18, 19 and 21 as prognostic and predictive markers in NSCLC: A single institution analysis" published in Mutation Research by P. Anoosha, Liang-Tsung Huang, R. Sakthivel, D. Karunagaran, M. Michael Gromiha, Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600 036, Tamil Nadu, India, and Department of Medical Informatics, Tzu Chi University, Hualien 970, Taiwan.
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"The development of tyrosine kinase inhibitors (TKIs) targeting the epidermal growth factor receptor (EGFR) provide an important insight on oncogenic therapy.[1–4]" and "Lichun et al. (should be "Ma et al.", the first author is Lichun Ma) created EGFR mutant structural database by collecting information of 942 NSCLC patients toward 112 mutation types which includes: insertion, deletion, duplication, modification, and substitution. Clinical data showed that the large number of patients have L858R mutation followed by Exon 19 and Exon 21 mutations, respectively.[9]" "(References 1 and 9 are our publications). In "Epidermal growth factor receptor (EGFR) structure-based bioactive pharmacophore models for identifying next-generation inhibitors against clinically relevant EGFR mutations" published in Chemical Biology & Drug Design by Pooja S. Panicker et al, Centre for Nanosciences and Molecular Medicine, Amrita Institute of Medical Sciences and Research Centre, Amrita University, Kochi, Kerala, India.
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