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View all- Xie YCao PQin YWu XHuang BLiu KLiu Y(2022)Catalytic activity in vitro of the human protein kinase ASK1 mutantsComputational Biology and Chemistry10.1016/j.compbiolchem.2022.10771299:COnline publication date: 1-Aug-2022
Molecular insight into the T798M gatekeeper mutation-caused acquired resistance to tyrosine kinase inhibitors in ErbB2-positive breast cancer
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Ji Lu, Kun Zhou, Xiaoxing Yin, Han Xu, Baojin MaAuthors Info & Claims
Ji Lu, Kun Zhou, Xiaoxing Yin, Han Xu, Baojin MaAuthors Info & ClaimsPages 290 - 296
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[1]
X. Ai, Y. Sun, H. Wang, S. Lu, A systematic profile of clinical inhibitors responsive to EGFR somatic amino acid mutations in lung cancer: implication for the molecular mechanism of drug resistance and sensitivity, Amino Acids 46 (2014) 1635–1648.
[2]
Z. Bai, S. Hou, S. Zhang, Z. Li, P. Zhou, Targeting self-binding peptides as a novel strategy to regulate protein activity and function: a case study on the proto-oncogene tyrosine protein kinase c-Src, J. Chem. Inf. Model. 57 (2017) 835–845.
[3]
H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne, The protein data bank, Nucleic Acids Res. 28 (2000) 235–242.
[4]
A. Bondi, Van der waals volumes and radii, J. Phys. Chem. 68 (1964) 441–451.
[5]
S.F. Boys, F. Bernardi, The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors, Mol. Phys. 19 (1970) 553–566.
[6]
Y.H. Cui, J. Chen, T. Xu, H.L. Tian, Structure-based grafting and identification of kinase-inhibitors to target mTOR signaling pathway as potential therapeutics for glioblastoma, Comput. Biol. Chem. 54 (2015) 57–65.
[7]
M.I. Davis, J.P. Hunt, S. Herrgard, P. Ciceri, L.M. Wodicka, G. Pallares, M. Hocker, D.K. Treiber, P.P. Zarrinkar, Comprehensive analysis of kinase inhibitor selectivity, Nat. Biotechnol. 29 (2011) 1046–1051.
[8]
M.J. Eck, C.H. Yun, Structural and mechanistic underpinnings of the differential drug sensitivity of EGFR mutations in non-small cell lung cancer, Biochim. Biophys. Acta 1804 (2010) 559–566.
[9]
R. Friedman, The molecular mechanism behind resistance of the kinase FLT3 to the inhibitor quizartinib, Proteins 85 (2017) 2143–2152.
[10]
C.E. Geyer, J. Forster, D. Lindquist, S. Chan, C.G. Romieu, T. Pienkowski, A. Jagiello-Gruszfeld, J. Crown, A. Chan, B. Kaufman, D. Skarlos, M. Campone, N. Davidson, M. Berger, C. Oliva, S.D. Rubin, S. Stein, D. Cameron, Lapatinib plus capecitabine for HER2-positive advanced breast cancer, New Engl. J. Med. 355 (2006) 2733–2743.
[11]
E. Gniazdowska, P. Koźmiński, K. Bańkowski, W. Łuniewski, L. Królicki, Synthesis, physicochemical and biological evaluation of technetium-99m labeled lapatinib as a novel potential tumor imaging agent of Her-2 positive breast cancer, Eur. J. Med. Chem. 87 (2014) 493–499.
[12]
D. Hauchecorne, A. Moiana, B.J. van der Veken, W.A. Herrebout, Halogen bonding to a divalent sulfur atom: an experimental study of the interactions of CF3X (X = Cl, Br, I) with dimethyl sulfide, Phys. Chem. Chem. Phys. 13 (2011) 10204–10213.
[13]
C.A. Hudis, Trastuzumab –– mechanism of action and use in clinical practice, New Engl. J. Med. 357 (2007) 39–51.
[14]
P.A. Jänne, Challenges of detecting EGFR T790M in gefitinib/erlotinib-resistant tumours, Lung Cancer 60 (2008) S3–S9.
[15]
R.K. Kancha, N. von Bubnoff, N. Bartosch, C. Peschel, R.A. Engh, J. Duyster, Differential sensitivity of ERBB2 kinase domain mutations towards lapatinib, PLoS One 6 (2011).
[16]
G. Keller, P. Schafhausen, T.H. Brümmendorf, Bosutinib. Recent Results Cancer Res. 184 (2010) 119–127.
[17]
G.G. Krivov, M.V. Shapovalov, R.L. Dunbrack, Improved prediction of protein side-chain conformations with SCWRL4, Proteins 77 (2009) 778–795.
[18]
W.T. Kuo, W.C. Lin, K.C. Chang, J.Y. Huang, K.C. Yen, I.C. Young, Y.J. Sun, F.H. Lin, Quantitative analysis of ligand-EGFR interactions: a platform for screening targeting molecules, PLoS One 10 (2015).
[19]
N.M. Levinson, S.G. Boxer, Structural and spectroscopic analysis of the kinase inhibitor bosutinib and an isomer of bosutinib binding to the Abl tyrosine kinase domain, PLoS One 7 (2012).
[20]
H. Luo, T. Du, P. Zhou, L. Yang, H. Mei, H. Ng, W. Zhang, M. Shu, W. Tong, L. Shi, D.L. Mendrick, H. Hong, Molecular docking to identify associations between drugs and class I human leukocyte antigens for predicting idiosyncratic drug reactions, Comb. Chem. High Throughput Screen. 18 (2015) 296–304.
[21]
X. Meng, Y. Li, H. Tang, W. Mao, H. Yang, X. Wang, X. Ding, S. Xie, Drug response to HER2 gatekeeper T798M mutation in HER2-positive breast cancer, Amino Acids 48 (2016) 487–497.
[22]
Z. Mitri, T. Constantine, R. O’Regan, The HER2 receptor in breast cancer: pathophysiology, clinical use, and new advances in therapy, Chemother. Res. Pract. 2012 (2012).
[23]
M.A. Olayioye, Update on HER-2 as a target for cancer therapy: intracellular signaling pathways of ErbB2/HER-2 and family members, Breast Cancer Res. 3 (2001) 385–389.
[24]
S. Ravichandran, B.T. Luke, J.R. Collins, Can structural features of kinase receptors provide clues on selectivity and inhibition? A molecular modeling study, J. Mol. Graph. Model. 57 (2015) 36–48.
[25]
Y. Ren, X. Chen, M. Feng, Q. Wang, P. Zhou, Gaussian process: a promising approach for the modeling and prediction of Peptide binding affinity to MHC proteins, Protein Pept. Lett. 18 (2011) 670–678.
[26]
B.N. Rexer, C.L. Arteaga, Intrinsic and acquired resistance to HER2-targeted therapies in HER2 gene-amplified breast cancer: mechanisms and clinical implications, Crit. Rev. Oncog. 17 (2012) 1–16.
[27]
B.N. Rexer, R. Ghosh, A. Narasanna, M.V. Estrada, A. Chakrabarty, Y. Song, J.A. Engelman, C.L. Arteaga, Human breast cancer cells harboring a gatekeeper T798M mutation in HER2 overexpress EGFR ligands and are sensitive to dual inhibition of EGFR and HER2, Clin. Cancer Res. 19 (2013) 5390–5401.
[28]
R. Roskoski, Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes, Pharmacol. Res. 103 (2016) 26–48.
[29]
H.M. Senn, W. Thiel, QM/MM methods for biomolecular systems, Angew. Chem. Int. Ed. Engl. 48 (2009) 1198–1229.
[30]
H. Sun, Y. Li, D. Li, T. Hou, Insight into crizotinib resistance mechanisms caused by three mutations in ALK tyrosine kinase using free energy calculation approaches, J. Chem. Inf. Model. 53 (2013) 2376–2389.
[31]
Z. Sun, Y. Shi, Y. Shen, L. Cao, W. Zhang, X. Guan, Analysis of different HER-2 mutations in breast cancer progression and drug resistance, J. Cell. Mol. Med. 19 (2015) 2691–2701.
[32]
Z. Tao, A. Shi, C. Lu, T. Song, Z. Zhang, J. Zhao, Breast cancer: epidemiology and etiology, Cell Biochem. Biophys. 72 (2015) 333–338.
[33]
F. Tian, Y. Lv, P. Zhou, L. Yang, Characterization of PDZ domain–peptide interactions using an integrated protocol of QM/MM, PB/SA, and CFEA analyses, J. Comput. Aided Mol. Des. 25 (2011) 947–958.
[34]
F. Tian, R. Tan, T. Guo, P. Zhou, L. Yang, Fast and reliable prediction of domain-peptide binding affinity using coarse-grained structure models, Biosystems 113 (2013) 40–49.
[35]
F. Tian, C. Yang, C. Wang, T. Guo, P. Zhou, Mutatomics analysis of the systematic thermostability profile of Bacillus subtilis lipase A, J. Mol. Model. 20 (2014) 2257.
[36]
S. Vrbic, I. Pejcic, S. Filipovic, B. Kocic, M. Vrbic, Current and future anti-HER2 therapy in breast cancer, J. BUON 18 (2013) 4–16.
[37]
Y.W. Wang, H.Y. Zhang, J.S. Li, X.W. Wang, Integrated exploitation of the structural diversity space of chemotherapy drugs to selectively inhibit HER2 T798M mutant in lung cancer, Chem. Biodivers. 14 (2017).
[38]
C. Yang, C. Wang, S. Zhang, J. Huang, P. Zhou, Structural and energetic insights into the intermolecular interaction among human leukocyte antigens, clinical hypersensitive drugs and antigenic peptides, Mol. Simul. 41 (2015) 741–751.
[39]
C. Yang, S. Zhang, P. He, C. Wang, J. Huang, P. Zhou, Self-binding peptides: folding or binding, J. Chem. Inf. Model. 55 (2015) 329–342.
[40]
C. Yang, S. Zhang, Z. Bai, S. Hou, D. Wu, J. Huang, P. Zhou, A two-step binding mechanism for the self-binding peptide recognition of target domains, Mol. Biosyst. 12 (2016) 1201–1213.
[41]
H. Yu, P. Zhou, M. Deng, Z. Shang, Indirect readout in protein–peptide recognition: a different story from classical biomolecular recognition, J. Chem. Inf. Model. 54 (2014) 2022–2032.
[42]
X. Yu, T. Wang, Y. Lou, Y. Li, Combination of in silico analysis and in vitro assay to investigate drug response to human epidermal growth factor receptor 2 mutations in lung cancer, Mol. Inform. 35 (2016) 25–35.
[43]
C.H. Yun, K.E. Mengwasser, A.V. Toms, M.S. Woo, H. Greulich, K.K. Wong, M. Meyerson, M.J. Eck, The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP, Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 2070–2075.
[44]
Y. Zhao, Y. Jiao, F. Sun, X. Liu, Revisiting the molecular mechanism of acquired resistance to reversible tyrosine kinase inhibitors caused by EGFR gatekeeper T790M mutation in non-small-cell lung cancer, Med. Chem. Res. 27 (2018) 2160–2170.
[45]
P. Zhou, C. Yang, Y. Ren, C. Wang, F. Tian, What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach, Food Chem. 141 (2013) 2967–2973.
[46]
P. Zhou, C. Wang, F. Tian, Y. Ren, C. Yang, J. Huang, Biomacromolecular quantitative structure-activity relationship (BioQSAR): a proof-of-concept study on the modeling, prediction and interpretation of protein–protein binding affinity, J. Comput. Aided Mol. Des. 27 (2013) 67–78.
[47]
P. Zhou, S. Zhang, Y. Wang, C. Yang, J. Huang, Structural modeling of HLA-B:1502 peptide carbamazepine T-cell receptor complex architecture: implication for the molecular mechanism of carbamazepine-induced Stevens-Johnson syndrome toxic epidermal necrolysis, J. Biomol. Struct. Dyn. 34 (2016) 1806–1817.
[48]
P. Zhou, S. Hou, Z. Bai, Z. Li, H. Wang, Z. Chen, Y. Meng, Disrupting the intramolecular interaction between proto-oncogene c-Src SH3 domain and its self-binding peptide PPII with rationally designed peptide ligands, Artif. Cells Nanomed. Biotechnol. 46 (2018) 1122–1131.
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Published: 01 February 2019
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View all- Xie YCao PQin YWu XHuang BLiu KLiu Y(2022)Catalytic activity in vitro of the human protein kinase ASK1 mutantsComputational Biology and Chemistry10.1016/j.compbiolchem.2022.10771299:COnline publication date: 1-Aug-2022