메뉴 건너띄기
상단메뉴 바로가기 메인 왼쪽메뉴 바로가기 본문 바로가기 푸터 바로가기

알마즌닷컴

Mobile

화상회의실 표준구성안크기, 용도, 특성 등을 고려하여 고객님의 회의실에 가장 알맞은 화상회의시스템을 제공합니다.

Ries G, Gong J, Finlay C: From cell population models to

페이지 정보

profile_image
작성자 Audrea
댓글 0건 조회 140회 작성일 24-04-27 18:42

본문

Ries G, Gong J, Finlay C: From cell population models to tumor control probability: including cell cycle effects. Acta Oncol Stockh Swed 2010, 3 49:1315?323. 92. Munro TR, Gilbert CW: The relation between tumour lethal doses and the radiosensitivity of tumour cells. Br J Radiol 1961, 34:246?51. 93. Zaider M, Minerbo GN: Tumour control probability: a formulation applicable to any temporal protocol of n-Phenylpiperazine-1-carboxamide dose delivery. Phys Med Biol 2000, 45:279?93. 94. Zhu T, Lee H, Lei H, Jones C, Patel K, Johnson ME, Hevener KE: Fragment-based drug discovery using a multidomain, parallel MD-MM/PBSA screening protocol. J Chem Inf Model 2013, 53:560?72. 95. Fujihashi M, Ishida T, Kuroda S, Kotra LP, Pai EF, Miki K: Substrate distortion contributes to the catalysis of orotidine 5-monophosphate decarboxylase. J Am Chem Soc 2013, 135:17432?7443. 96. Tiwari G, Mohanty D: An in silico analysis of the binding modes and binding affinities of small molecule modulators of PDZ-peptide interactions. PLoS One 2013, 8:e71340. 97. Zahn D: Molecular dynamics simulation of ionic conductors: perspectives and limitations. J Mol PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/11834444 Model 2011, 17:1531?535. 98. Wood NT, Fadda E, Davis R, Grant OC, Martin JC, PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/8086425 Woods RJ, Travers SA: The influence of N-linked glycans on the molecular dynamics of the HIV-1 gp120 V3 loop. PLoS One 2013, 8:e80301. 99. Chaudhuri A, Sarkar I, Chakraborty S: Comparative analysis of binding sites of human meprins with hydroxamic acid derivative by molecular dynamics simulation study. J Biomol Struct Dyn 2013, 100. Leonis G, Steinbrecher T, Papadopoulos MG: A contribution to the drug resistance mechanism of darunavir, amprenavir, indinavir, and saquinavir complexes with HIV-1 protease due to flap mutation I50V: a systematic MM-PBSA and thermodynamic integration study. J Chem Inf Model 2013, 53:2141?153. 101. Yoda T, Sugita Y, Okamoto Y: Hydrophobic core formation and dehydration in protein folding studied by generalized-ensemble simulations. Biophys J 2010, 99:1637?644. 102. Yoda T, Sugita Y, Okamoto Y: Salt effects on hydrophobic-core formation in folding of a helical miniprotein studied by molecular dynamics simulations. Proteins 2014, 82:933?43. 103. Fukunishi Y, Nakamura H: Improved estimation of protein-ligand binding free energy by using the ligandentropy and mobility of water molecules. Pharm Basel Switz 2013, 6:604?22. 104. Cornell WD, Cieplak P, Bayly CI, Gould IR, Merz KM, Ferguson DM, Spellmeyer DC, Fox T, Caldwell JW, Kollman PA: A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J Am Chem Soc 1995, 117:5179?197. 105. Ponder JW, Case DA: Force fields for protein simulations. Adv Protein Chem 2003, 66:27?5.Tuszynski et al. Theoretical Biology and Medical Modelling 2014, 11:52 http://www.tbiomed.com/content/11/1/Page 37 of106. Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling 3-(2,4-Dichlorophenoxy)azetidine C: Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 2006, 65:712?25. 107. Wang J, Cieplak P, Kollman PA: How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J Comput Chem 2000, 21:1049?074. 108. Wickstrom L, Okur A, Simmerling C: Evaluating the performance of the ff99SB force field based on NMR scalar coupling data. Biophys J 2009, 97:853?56. 109. Cino EA, Choy W-Y, Karttunen M: Comparison of secondary structure formation using 10 different force fields in microse.

댓글목록

등록된 댓글이 없습니다.