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Volumn 15, Issue , 2017, Pages 138-145

Biobetters From an Integrated Computational/Experimental Approach

Author keywords

Docking; Free energy perturbation; Molecular dynamics; Potential of mean force; Rational drug design

Indexed keywords

COMPUTATIONAL CHEMISTRY; DISEASES; EPITOPES; FREE ENERGY; INVERSE PROBLEMS; MONOCLONAL ANTIBODIES; PEPTIDES;

EID: 85010460349     PISSN: None     EISSN: 20010370     Source Type: Journal    
DOI: 10.1016/j.csbj.2017.01.003     Document Type: Review
Times cited : (10)

References (73)
  • 1
    • 33747200808 scopus 로고    scopus 로고
    • Combining docking and molecular dynamic simulations in drug design
    • [1] Alonso, H., Bliznyuk, A.A., Gready, J.E., Combining docking and molecular dynamic simulations in drug design. Med Res Rev 26 (2006), 531–568.
    • (2006) Med Res Rev , vol.26 , pp. 531-568
    • Alonso, H.1    Bliznyuk, A.A.2    Gready, J.E.3
  • 2
    • 84873371685 scopus 로고    scopus 로고
    • Computational methods of studying the binding of toxins from venomous animals to biological ion channels
    • [2] Gordon, D., Chen, R., Chung, S.H., Computational methods of studying the binding of toxins from venomous animals to biological ion channels. Physiol Rev 93 (2013), 767–802.
    • (2013) Physiol Rev , vol.93 , pp. 767-802
    • Gordon, D.1    Chen, R.2    Chung, S.H.3
  • 3
    • 84911861938 scopus 로고    scopus 로고
    • Computational approaches for designing potent and selective analogues of peptide toxins as novel therapeutics
    • [3] Kuyucak, S., Norton, R.S., Computational approaches for designing potent and selective analogues of peptide toxins as novel therapeutics. Future Med Chem 6 (2014), 1645–1658.
    • (2014) Future Med Chem , vol.6 , pp. 1645-1658
    • Kuyucak, S.1    Norton, R.S.2
  • 4
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: an overview of search algorithms and a guide to scoring functions
    • [4] Halperin, I., Ma, B., Wolfson, H., Nussinov, R., Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins 47 (2002), 409–443.
    • (2002) Proteins , vol.47 , pp. 409-443
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 6
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • [6] Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., et al. Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J Comput Chem 19 (1998), 1639–1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6
  • 7
    • 70349932423 scopus 로고    scopus 로고
    • Autodock4 and AutoDockTools4: automated docking with selective receptor flexibility
    • [7] Morris, G.M., Huey, R., Lindstrom, W., Sanner, M.F., Belew, R.K., Goodsell, D.S., et al. Autodock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30 (2009), 2785–2791.
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5    Goodsell, D.S.6
  • 8
    • 35449008122 scopus 로고    scopus 로고
    • Integrating statistical pair potentials into protein complex prediction
    • [8] Mintseris, J., Pierce, B., Wiehe, K., Anderson, R., Chen, R., Weng, Z., Integrating statistical pair potentials into protein complex prediction. Proteins 69 (2007), 511–520.
    • (2007) Proteins , vol.69 , pp. 511-520
    • Mintseris, J.1    Pierce, B.2    Wiehe, K.3    Anderson, R.4    Chen, R.5    Weng, Z.6
  • 9
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: a protein-protein docking approach based on biochemical or biophysical information
    • [9] Dominguez, C., Boelens, R., Bonvin, A.M., HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc 125 (2003), 1731–1737.
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 10
    • 36748998784 scopus 로고    scopus 로고
    • HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets
    • [10] De Vries, S.J., van Dijk, A.D., Krzeminski, M., van Dijk, M., Thureau, A., Hsu, V., et al. HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets. Proteins 69 (2007), 726–733.
    • (2007) Proteins , vol.69 , pp. 726-733
    • De Vries, S.J.1    van Dijk, A.D.2    Krzeminski, M.3    van Dijk, M.4    Thureau, A.5    Hsu, V.6
  • 12
    • 35148851120 scopus 로고    scopus 로고
    • Binding of organic cations to gramicidin: a channel studied with autodock and molecular dynamics simulations
    • [12] Patra, S.M., Bastug, T., Kuyucak, S., Binding of organic cations to gramicidin: a channel studied with autodock and molecular dynamics simulations. J Phys Chem B 111 (2007), 11303–11311.
    • (2007) J Phys Chem B , vol.111 , pp. 11303-11311
    • Patra, S.M.1    Bastug, T.2    Kuyucak, S.3
  • 13
    • 38549144657 scopus 로고    scopus 로고
    • Ligand binding to the voltage-gated Kv1.5 potassium channel in the open state–docking and computer simulations of a homology model
    • [13] Ander, M., Luzhkov, V.B., Aqvist, J., Ligand binding to the voltage-gated Kv1.5 potassium channel in the open state–docking and computer simulations of a homology model. Biophys J 9 (2007), 820–831.
    • (2007) Biophys J , vol.9 , pp. 820-831
    • Ander, M.1    Luzhkov, V.B.2    Aqvist, J.3
  • 14
    • 38549168519 scopus 로고    scopus 로고
    • Molecular basis of inhibitory peptide maurotoxin recognizing Kv1.2 channel explored by ZDOCK and molecular dynamic simulations
    • [14] Yi, H., Qiu, S., Cao, Z.J., Wu, Y.L., Li, W.X., Molecular basis of inhibitory peptide maurotoxin recognizing Kv1.2 channel explored by ZDOCK and molecular dynamic simulations. Proteins 70 (2008), 844–854.
    • (2008) Proteins , vol.70 , pp. 844-854
    • Yi, H.1    Qiu, S.2    Cao, Z.J.3    Wu, Y.L.4    Li, W.X.5
  • 15
    • 67649386435 scopus 로고    scopus 로고
    • Mechanism and energetics of charybdotoxin unbinding from a potassium channel from molecular dynamics simulations
    • [15] Chen, P.C., Kuyucak, S., Mechanism and energetics of charybdotoxin unbinding from a potassium channel from molecular dynamics simulations. Biophys J 96 (2009), 2577–2588.
    • (2009) Biophys J , vol.96 , pp. 2577-2588
    • Chen, P.C.1    Kuyucak, S.2
  • 16
    • 84863393842 scopus 로고    scopus 로고
    • Developing a comparative docking protocol for the prediction of peptide selectivity profiles: investigation of potassium channel toxins
    • [16] Chen, P.C., Kuyucak, S., Developing a comparative docking protocol for the prediction of peptide selectivity profiles: investigation of potassium channel toxins. Toxins 4 (2012), 110–138.
    • (2012) Toxins , vol.4 , pp. 110-138
    • Chen, P.C.1    Kuyucak, S.2
  • 18
    • 0029878720 scopus 로고    scopus 로고
    • VMD–visual molecular dynamics
    • [18] Humphrey, W., Dalke, A., Schulten, K., VMD–visual molecular dynamics. J Mol Graph 14 (1996), 33–38.
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 19
  • 20
    • 84870726202 scopus 로고    scopus 로고
    • Understanding molecular simulation: from algorithms to applications
    • Academic Press San Diego
    • [20] Frenkel, D., Smit, B., Understanding molecular simulation: from algorithms to applications. 1996, Academic Press, San Diego.
    • (1996)
    • Frenkel, D.1    Smit, B.2
  • 21
    • 84985974923 scopus 로고    scopus 로고
    • Molecular Modelling, principles, applications
    • Prentice Hall New York
    • [21] Leach, A.R., Molecular Modelling, principles, applications. 2001, Prentice Hall, New York.
    • (2001)
    • Leach, A.R.1
  • 22
    • 80855156716 scopus 로고    scopus 로고
    • Molecular simulation approaches to membrane proteins
    • [22] Stansfeld, P.J., Sansom, M.S.P., Molecular simulation approaches to membrane proteins. Structure 19 (2011), 1562–1572.
    • (2011) Structure , vol.19 , pp. 1562-1572
    • Stansfeld, P.J.1    Sansom, M.S.P.2
  • 23
    • 84861367246 scopus 로고    scopus 로고
    • Biomolecular simulations: a computational microscope for molecular biology
    • [23] Dror, R.O., Dirks, R.M., Grossman, J.P., Xu, H., Shaw, D.E., Biomolecular simulations: a computational microscope for molecular biology. Annu Rev Biophys 41 (2012), 429–452.
    • (2012) Annu Rev Biophys , vol.41 , pp. 429-452
    • Dror, R.O.1    Dirks, R.M.2    Grossman, J.P.3    Xu, H.4    Shaw, D.E.5
  • 24
    • 84873129310 scopus 로고    scopus 로고
    • Molecular dynamics simulations of membrane proteins
    • [24] Bastug, T., Kuyucak, S., Molecular dynamics simulations of membrane proteins. Biophys Rev 4 (2012), 271–282.
    • (2012) Biophys Rev , vol.4 , pp. 271-282
    • Bastug, T.1    Kuyucak, S.2
  • 25
    • 68049122041 scopus 로고    scopus 로고
    • Importance of the peptide backbone description in modeling the selectivity filter in potassium channels
    • [25] Bastug, T., Kuyucak, S., Importance of the peptide backbone description in modeling the selectivity filter in potassium channels. Biophys J 96 (2009), 4006–4012.
    • (2009) Biophys J , vol.96 , pp. 4006-4012
    • Bastug, T.1    Kuyucak, S.2
  • 26
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: combining molecular mechanic and continuum models
    • [26] Kollman, P.A., Massova, I., Reyes, C., Kuhn, B., Huo, S., Chong, L., et al. Calculating structures and free energies of complex molecules: combining molecular mechanic and continuum models. Acc Chem Res 33 (2000), 889–897.
    • (2000) Acc Chem Res , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5    Chong, L.6
  • 27
    • 70349100806 scopus 로고    scopus 로고
    • Theory of free energy and entropy in noncovalent binding
    • [27] Zhou, H.X., Gilson, M.K., Theory of free energy and entropy in noncovalent binding. Chem Rev 109 (2009), 4092–4107.
    • (2009) Chem Rev , vol.109 , pp. 4092-4107
    • Zhou, H.X.1    Gilson, M.K.2
  • 28
    • 65249124122 scopus 로고    scopus 로고
    • Computations of standard binding free energies with molecular dynamics simulations
    • [28] Deng, Y., Roux, B., Computations of standard binding free energies with molecular dynamics simulations. J Phys Chem B 113 (2009), 2234–2246.
    • (2009) J Phys Chem B , vol.113 , pp. 2234-2246
    • Deng, Y.1    Roux, B.2
  • 29
    • 77952390528 scopus 로고    scopus 로고
    • Basic ingredients of free energy calculations
    • [29] Christ, C.D., Mark, A.E., van Gunsteren, W.F., Basic ingredients of free energy calculations. J Comput Chem 31 (2010), 1569–1582.
    • (2010) J Comput Chem , vol.31 , pp. 1569-1582
    • Christ, C.D.1    Mark, A.E.2    van Gunsteren, W.F.3
  • 30
    • 77950650980 scopus 로고    scopus 로고
    • Towards accurate free energy calculations in ligand-protein binding studies
    • [30] Steinbrecher, T., Labahn, A., Towards accurate free energy calculations in ligand-protein binding studies. Curr Med Chem 17 (2010), 767–785.
    • (2010) Curr Med Chem , vol.17 , pp. 767-785
    • Steinbrecher, T.1    Labahn, A.2
  • 31
    • 41349090342 scopus 로고    scopus 로고
    • Can we use docking and scoring for hit-to-lead optimization?
    • [31] Enyedy, I.J., Egan, W.J., Can we use docking and scoring for hit-to-lead optimization?. J Comput Aided Mol Des 22 (2008), 161–168.
    • (2008) J Comput Aided Mol Des , vol.22 , pp. 161-168
    • Enyedy, I.J.1    Egan, W.J.2
  • 32
    • 77950503976 scopus 로고    scopus 로고
    • Virtual screening: an endless staircase?
    • [32] Schneider, G., Virtual screening: an endless staircase?. Nat Rev Drug Discov 9 (2010), 273–276.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 273-276
    • Schneider, G.1
  • 33
    • 66249097011 scopus 로고    scopus 로고
    • Large scale application of high-throughput molecular mechanics with Poisson-Boltzmann surface area for routine physics-based scoring of protein-ligand complexes
    • [33] Brown, S.P., Muchmore, S.W., Large scale application of high-throughput molecular mechanics with Poisson-Boltzmann surface area for routine physics-based scoring of protein-ligand complexes. J Med Chem 52 (2009), 3159–3165.
    • (2009) J Med Chem , vol.52 , pp. 3159-3165
    • Brown, S.P.1    Muchmore, S.W.2
  • 34
    • 77951210462 scopus 로고    scopus 로고
    • Absolute binding free energy calculations: on the accuracy of computational scoring of protein-ligand interactions
    • [34] Singh, N., Warshel, A., Absolute binding free energy calculations: on the accuracy of computational scoring of protein-ligand interactions. Proteins 78 (2010), 1705–17123.
    • (2010) Proteins , vol.78 , pp. 1705-17123
    • Singh, N.1    Warshel, A.2
  • 35
    • 77955663115 scopus 로고    scopus 로고
    • Prediction of protein-ligand affinity by free energy simulations: assumptions, pitfalls and expectations
    • [35] Michel, J., Essex, J.W., Prediction of protein-ligand affinity by free energy simulations: assumptions, pitfalls and expectations. J Comput Aided Mol Des 24 (2011), 639–658.
    • (2011) J Comput Aided Mol Des , vol.24 , pp. 639-658
    • Michel, J.1    Essex, J.W.2
  • 37
    • 84871960256 scopus 로고    scopus 로고
    • Perspective: alchemical free energy calculations in drug discovery
    • [37] Mobley, D.L., Klimov, P.V., Perspective: alchemical free energy calculations in drug discovery. J Chem Phys, 137, 2012, 230901.
    • (2012) J Chem Phys , vol.137 , pp. 230901
    • Mobley, D.L.1    Klimov, P.V.2
  • 38
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules
    • [38] Kumar, S., Bouzida, S.D., Swensen, R.H., Kollman, P.A., Rosenberg, J.M., The weighted histogram analysis method for free-energy calculations on biomolecules. J Comput Chem 13 (1992), 1011–1021.
    • (1992) J Comput Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, S.D.2    Swensen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 39
    • 79959663208 scopus 로고    scopus 로고
    • Accurate determination of the binding free energy for KcsA-charybdotoxin complex from the potential of mean force calculations
    • [39] Chen, P.C., Kuyucak, S., Accurate determination of the binding free energy for KcsA-charybdotoxin complex from the potential of mean force calculations. Biophys J 100 (2011), 2466–2474.
    • (2011) Biophys J , vol.100 , pp. 2466-2474
    • Chen, P.C.1    Kuyucak, S.2
  • 40
    • 84875769555 scopus 로고    scopus 로고
    • Computational studies of marine toxins targeting ion channels
    • [40] Rashid, M.H., Mahdavi, S., Kuyucak, S., Computational studies of marine toxins targeting ion channels. Mar Drugs 11 (2013), 848–869.
    • (2013) Mar Drugs , vol.11 , pp. 848-869
    • Rashid, M.H.1    Mahdavi, S.2    Kuyucak, S.3
  • 41
    • 4143087050 scopus 로고    scopus 로고
    • Calculating potentials of mean force from steered molecular dynamics simulations
    • [41] Park, S., Schulten, K., Calculating potentials of mean force from steered molecular dynamics simulations. J Chem Phys 120 (2004), 5946–5961.
    • (2004) J Chem Phys , vol.120 , pp. 5946-5961
    • Park, S.1    Schulten, K.2
  • 42
    • 42449129769 scopus 로고    scopus 로고
    • Potential of mean force calculations of ligand binding to ion channels from Jarzynski's equality and umbrella sampling
    • [42] Bastug, T., Chen, P.C., Patra, S.M., Kuyucak, S., Potential of mean force calculations of ligand binding to ion channels from Jarzynski's equality and umbrella sampling. J Chem Phys 128 (2008), 104–112.
    • (2008) J Chem Phys , vol.128 , pp. 104-112
    • Bastug, T.1    Chen, P.C.2    Patra, S.M.3    Kuyucak, S.4
  • 43
    • 84892388463 scopus 로고    scopus 로고
    • A potent and selective peptide blocker of the Kv1.3 channel: prediction from free-energy simulations and experimental confirmation
    • [43] Rashid, M.H., Heinzelmann, G., Huq, R., Tajhya, R.B., Chang, S.C., Chhabra, S., et al. A potent and selective peptide blocker of the Kv1.3 channel: prediction from free-energy simulations and experimental confirmation. PLoS One, 8, 2013, e78712.
    • (2013) PLoS One , vol.8
    • Rashid, M.H.1    Heinzelmann, G.2    Huq, R.3    Tajhya, R.B.4    Chang, S.C.5    Chhabra, S.6
  • 44
    • 0142123347 scopus 로고    scopus 로고
    • Determination of antibody affinity by ELISA
    • [44] Bobrovnik, S.A., Determination of antibody affinity by ELISA. Theory J Biochem Biophys Methods 57 (2003), 213–236.
    • (2003) Theory J Biochem Biophys Methods , vol.57 , pp. 213-236
    • Bobrovnik, S.A.1
  • 45
  • 46
    • 23444440845 scopus 로고    scopus 로고
    • Affinity ranking of antibodies using flow cytometry: application in antibody phage display-based target discovery
    • [46] Geuijen, C.A.W., Clijsters-van der Horst, M., Cox, F., Throsby, P.M.L. Rood, Jongeneelen, M.A., et al. Affinity ranking of antibodies using flow cytometry: application in antibody phage display-based target discovery. J Immunol Methods 302 (2005), 68–77.
    • (2005) J Immunol Methods , vol.302 , pp. 68-77
    • Geuijen, C.A.W.1    Clijsters-van der Horst, M.2    Cox, F.3    Throsby, P.M.L.R.4    Jongeneelen, M.A.5
  • 47
    • 77955466435 scopus 로고    scopus 로고
    • Identification and impact of aggregation-prone regions in proteins and therapeutic monoclonal antibodies, in aggregation of therapeutic proteins
    • John Wiley & Sons
    • [47] Kumar, S., Wang, X., Singh, S.K., Identification and impact of aggregation-prone regions in proteins and therapeutic monoclonal antibodies, in aggregation of therapeutic proteins. 2010, John Wiley & Sons, 103–118.
    • (2010) , pp. 103-118
    • Kumar, S.1    Wang, X.2    Singh, S.K.3
  • 48
    • 79955638418 scopus 로고    scopus 로고
    • Strategies for the assessment of protein aggregates in pharmaceutical biotech product development
    • [48] den Engelsman, J., Garidel, P., Smulders, R., Koll, H., Smith, B., Bassarab, S., et al. Strategies for the assessment of protein aggregates in pharmaceutical biotech product development. Pharm Res 28 (2011), 920–933.
    • (2011) Pharm Res , vol.28 , pp. 920-933
    • den Engelsman, J.1    Garidel, P.2    Smulders, R.3    Koll, H.4    Smith, B.5    Bassarab, S.6
  • 49
    • 84947466271 scopus 로고    scopus 로고
    • Biophysical techniques for characterizing the higher order structure and interactions of monoclonal antibodies, in state-of-the-art and emerging technologies for therapeutic monoclonal antibody characterization
    • American Chemical Society
    • [49] Gokarn, Y., Agarwal, S., Arthur, K., Bepperling, A., Day, E.S., Filoti, D., et al. Biophysical techniques for characterizing the higher order structure and interactions of monoclonal antibodies, in state-of-the-art and emerging technologies for therapeutic monoclonal antibody characterization. American Chemical Society, (eds.) Volume 2. Biopharmaceutical characterization The NISTmAb case study, vol. 1201, 2015, 285–327.
    • (2015) Volume 2. Biopharmaceutical characterization, The NISTmAb case study , vol.1201 , pp. 285-327
    • Gokarn, Y.1    Agarwal, S.2    Arthur, K.3    Bepperling, A.4    Day, E.S.5    Filoti, D.6
  • 50
    • 77953865084 scopus 로고    scopus 로고
    • Principles of fluorescence spectroscopy
    • 3rd ed. Springer Maryland, USA
    • [50] Lakowicz, J.R., Principles of fluorescence spectroscopy. 3rd ed., 2006, Springer, Maryland, USA.
    • (2006)
    • Lakowicz, J.R.1
  • 51
    • 79951512916 scopus 로고    scopus 로고
    • Tryptophan-tryptophan energy transfer and classification of tryptophan residues in proteins: therapeutic monoclonal antibody as a model
    • [51] Kayser, V., Chennamsetty, N., Voynov, V., Helk, B., Trout, B.L., Tryptophan-tryptophan energy transfer and classification of tryptophan residues in proteins: therapeutic monoclonal antibody as a model. J Fluoresc 21 (2010), 275–288.
    • (2010) J Fluoresc , vol.21 , pp. 275-288
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Trout, B.L.5
  • 52
    • 0033801573 scopus 로고    scopus 로고
    • The identification of tryptophan residues responsible for ATP-induced increase in intrinsic fluorescence of myosin subfragment 1
    • [52] Reshetnyak, Y.K., Andreev, O.A., Borejdo, J., Toptygin, D.D., Brand, L., Burstein, E.A., The identification of tryptophan residues responsible for ATP-induced increase in intrinsic fluorescence of myosin subfragment 1. J Biomol Struct Dyn 18 (2000), 113–125.
    • (2000) J Biomol Struct Dyn , vol.18 , pp. 113-125
    • Reshetnyak, Y.K.1    Andreev, O.A.2    Borejdo, J.3    Toptygin, D.D.4    Brand, L.5    Burstein, E.A.6
  • 53
    • 84855575327 scopus 로고    scopus 로고
    • A screening tool for therapeutic monoclonal antibodies: identifying the most stable protein and its best formulation based on thioflavin T binding
    • [53] Kayser, V., Chennamsetty, N., Voynov, V., Helk, B., Forrer, K., Trout, B.L., A screening tool for therapeutic monoclonal antibodies: identifying the most stable protein and its best formulation based on thioflavin T binding. Biotechnol J 7 (2012), 127–132.
    • (2012) Biotechnol J , vol.7 , pp. 127-132
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Forrer, K.5    Trout, B.L.6
  • 54
    • 11844292073 scopus 로고    scopus 로고
    • New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins
    • [54] Attri, A.K., Minton, A.P., New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. Anal Biochem 337 (2005), 103–110.
    • (2005) Anal Biochem , vol.337 , pp. 103-110
    • Attri, A.K.1    Minton, A.P.2
  • 55
    • 0036558370 scopus 로고    scopus 로고
    • Kinetics of thermal aggregation of tobacco mosaic virus coat protein
    • [55] Kurganov, E.R.R.B.I., Dobrov, E.N., Kinetics of thermal aggregation of tobacco mosaic virus coat protein. Biochemistry (Mosc) 67 (2002), 525–533.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 525-533
    • Kurganov, E.R.R.B.I.1    Dobrov, E.N.2
  • 56
    • 79955591497 scopus 로고    scopus 로고
    • Evaluation of a non-Arrhenius model for therapeutic monoclonal antibody aggregation
    • [56] Kayser, V., Chennamsetty, N., Voynov, V., Helk, B., Forrer, K., Trout, B.L., Evaluation of a non-Arrhenius model for therapeutic monoclonal antibody aggregation. J Pharm Sci 100 (2011), 2526–2542.
    • (2011) J Pharm Sci , vol.100 , pp. 2526-2542
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Forrer, K.5    Trout, B.L.6
  • 57
    • 44849093511 scopus 로고    scopus 로고
    • + channel modulators for the treatment of neurological disorders and autoimmune diseases
    • + channel modulators for the treatment of neurological disorders and autoimmune diseases. Chem Rev 108 (2008), 1744–1773.
    • (2008) Chem Rev , vol.108 , pp. 1744-1773
    • Wulff, H.1    Zhorov, B.S.2
  • 59
    • 84857039386 scopus 로고    scopus 로고
    • Development of a sea anemone toxin as an immunomodulator for therapy of autoimmune diseases
    • [59] Chi, V., Pennington, M.W., Norton, R.S., Tarcha, E.J., Londono, L.M., Sims-Fahey, B., et al. Development of a sea anemone toxin as an immunomodulator for therapy of autoimmune diseases. Toxicon 59 (2012), 529–546.
    • (2012) Toxicon , vol.59 , pp. 529-546
    • Chi, V.1    Pennington, M.W.2    Norton, R.S.3    Tarcha, E.J.4    Londono, L.M.5    Sims-Fahey, B.6
  • 60
    • 84860307772 scopus 로고    scopus 로고
    • Affinity and selectivity of ShK toxin for the Kv1 potassium channels from free energy simulations
    • [60] Rashid, M.H., Kuyucak, S., Affinity and selectivity of ShK toxin for the Kv1 potassium channels from free energy simulations. J Phys Chem B 116 (2012), 4812–4822.
    • (2012) J Phys Chem B , vol.116 , pp. 4812-4822
    • Rashid, M.H.1    Kuyucak, S.2
  • 61
    • 11244306404 scopus 로고    scopus 로고
    • Evidence for domain specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins
    • [61] Regaya, L., Beeton, C., Ferrat, G., Andreotti, N., Darbon, H., Waard, M. De, et al. Evidence for domain specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins. J Biol Chem 279 (2004), 55690–55696.
    • (2004) J Biol Chem , vol.279 , pp. 55690-55696
    • Regaya, L.1    Beeton, C.2    Ferrat, G.3    Andreotti, N.4    Darbon, H.5    Waard, M.D.6
  • 62
    • 84893120991 scopus 로고    scopus 로고
    • Free energy simulations of binding of HsTx1 toxin to Kv1 potassium channels: the basis of Kv1.3/Kv1.1 selectivity
    • [62] Rashid, M.H., Kuyucak, S., Free energy simulations of binding of HsTx1 toxin to Kv1 potassium channels: the basis of Kv1.3/Kv1.1 selectivity. J Phys Chem B 118 (2014), 707–716.
    • (2014) J Phys Chem B , vol.118 , pp. 707-716
    • Rashid, M.H.1    Kuyucak, S.2
  • 63
    • 84897147621 scopus 로고    scopus 로고
    • A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases
    • [63] Rashid, M.H., Huq, R., Tanner, M., Chhabra, S., Khoo, K.K., Estrada, R., et al. A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases. Sci Rep, 4, 2014, 4509.
    • (2014) Sci Rep , vol.4 , pp. 4509
    • Rashid, M.H.1    Huq, R.2    Tanner, M.3    Chhabra, S.4    Khoo, K.K.5    Estrada, R.6
  • 64
    • 84975865350 scopus 로고    scopus 로고
    • Enabling noninvasive systemic delivery of the Kv1.3-blocking peptide HsTX1[R14A] via the buccal mucosa
    • [64] Jin, L., Boyd, B.J., Larson, I.C., Pennington, M.W., Norton, R.S., Nicolazzo, J.A., Enabling noninvasive systemic delivery of the Kv1.3-blocking peptide HsTX1[R14A] via the buccal mucosa. J Pharm Sci 105 (2016), 2173–2179.
    • (2016) J Pharm Sci , vol.105 , pp. 2173-2179
    • Jin, L.1    Boyd, B.J.2    Larson, I.C.3    Pennington, M.W.4    Norton, R.S.5    Nicolazzo, J.A.6
  • 65
    • 84857048280 scopus 로고    scopus 로고
    • Cyclization of conotoxins to improve their biopharmaceutical properties
    • [65] Clark, R.J., Akcan, M., Kaas, Q., Daly, N.L., Craik, D.J., Cyclization of conotoxins to improve their biopharmaceutical properties. Toxicon 59 (2012), 446–455.
    • (2012) Toxicon , vol.59 , pp. 446-455
    • Clark, R.J.1    Akcan, M.2    Kaas, Q.3    Daly, N.L.4    Craik, D.J.5
  • 66
    • 80053469174 scopus 로고    scopus 로고
    • α-Conotoxin ImI incorporating stable cystathionine bridges maintains full potency and identical three-dimensional structure
    • [66] Dekan, Z., Vetter, I., Dally, N., Craik, D.J., Lewis, R.J., Alewood, P.F., α-Conotoxin ImI incorporating stable cystathionine bridges maintains full potency and identical three-dimensional structure. JACS 133 (2011), 15866–15869.
    • (2011) JACS , vol.133 , pp. 15866-15869
    • Dekan, Z.1    Vetter, I.2    Dally, N.3    Craik, D.J.4    Lewis, R.J.5    Alewood, P.F.6
  • 67
    • 80455144785 scopus 로고    scopus 로고
    • Lactam-stabilized helical analogues of the analgesic μ-conotoxin KIIIA
    • [67] Khoo, K.K., Wilson, M.J., Smith, B.J., Zhang, M.M., Gulyas, J., Yoshikami, D., et al. Lactam-stabilized helical analogues of the analgesic μ-conotoxin KIIIA. J Med Chem 54 (2011), 7558–7566.
    • (2011) J Med Chem , vol.54 , pp. 7558-7566
    • Khoo, K.K.1    Wilson, M.J.2    Smith, B.J.3    Zhang, M.M.4    Gulyas, J.5    Yoshikami, D.6
  • 68
    • 84962069666 scopus 로고    scopus 로고
    • Peptidomimetic star polymers for targeting biological ion channels
    • [68] Chen, R., Lu, D.R., Xie, Z.L., Feng, J., Jia, Z., Ho, J., et al. Peptidomimetic star polymers for targeting biological ion channels. PLoS One, 11, 2016, e0152169.
    • (2016) PLoS One , vol.11
    • Chen, R.1    Lu, D.R.2    Xie, Z.L.3    Feng, J.4    Jia, Z.5    Ho, J.6
  • 69
    • 84921352030 scopus 로고    scopus 로고
    • The therapeutic monoclonal antibody market
    • [69] Ecker, D.M., Jones, S.D., Levine, H.L., The therapeutic monoclonal antibody market. MAbs 7 (2015), 9–14.
    • (2015) MAbs , vol.7 , pp. 9-14
    • Ecker, D.M.1    Jones, S.D.2    Levine, H.L.3
  • 73
    • 84859910826 scopus 로고    scopus 로고
    • Understanding protein unfolding from molecular simulations
    • [73] Toofanny, R.D., Daggett, V., Understanding protein unfolding from molecular simulations. WIREs Comput Mol Sci 2 (2012), 405–423.
    • (2012) WIREs Comput Mol Sci , vol.2 , pp. 405-423
    • Toofanny, R.D.1    Daggett, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.