參考文獻 |
1. Fanali G, Rampoldi V, Masi Ad, Bolli A, Lopiano L, Ascenzi P, Fasano M: Binding of anti-Parkinson′s disease drugs to human serum albumin is allosterically modulated. IUBMB Life 2010, 62(5):371-376.
2. Bourassa P, Dubeau S, Maharvi GM, Fauq AH, Thomas TJ, Tajmir-Riahi HA: Binding of antitumor tamoxifen and its metabolites 4-hydroxytamoxifen and endoxifen to human serum albumin. Biochimie 2011, 93(7):1089-1101.
3. Dömötör O, Hartinger C, Bytzek A, Kiss T, Keppler B, Enyedy E: Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies. J Biol Inorg Chem 2013, 18(1):9-17.
4. Taguchi K, Giam Chuang VT, Maruyama T, Otagiri M: Pharmaceutical aspects of the recombinant human serum albumin dimer: Structural characteristics, biological properties, and medical applications. Journal of Pharmaceutical Sciences 2012, 101(9):3033-3046.
5. Curry S, Brick P, Franks NP: Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1999, 1441(2–3):131-140.
6. Fanali G, di Masi A, Trezza V, Marino M, Fasano M, Ascenzi P: Human serum albumin: From bench to bedside. Molecular Aspects of Medicine 2012, 33(3):209-290.
7. Varshney A, Sen P, Ahmad E, Rehan M, Subbarao N, Khan RH: Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 2010, 22(1):77-87.
8. U. Kragh-Hansen VTGC, M. Otagiri: Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol Pharm Bull 2002, 25:695-704.
9. Yamasaki K, Chuang VTG, Maruyama T, Otagiri M: Albumin–drug interaction and its clinical implication. Biochimica et Biophysica Acta (BBA) - General Subjects 2013, 1830(12):5435-5443.
10. Beljaars LM, G.; Schuppan, D.; Geerts, A.; De Bleser, P. J.; Weert, B.; Meijer, D. K. F.; Poelstra, K. : Successful Targeting to Rat Hepatic Stellate Cells Using Albumin Modified with Cyclic Peptides That Recognize the Collagen Type VI Receptor. J Biol Chem 2000, 275:12743-12751.
11. Sheffield WP: Modification of Clearance of Therapeutic and Potentially Therapeutic Proteins. Current Drug Targets -Cardiovascular & Haematological Disorders 2001, 1(1):1-22.
12. Carter D, He X, Munson S, Twigg P, Gernert K, Broom M, Miller T: Three-dimensional structure of human serum albumin. Science 1989, 244(4909):1195-1198.
13. Stephen Curry HM, Peter Brick & Nick Franks: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural & Molecular Biology 1998, 5:827-835.
14. Carter XMHDC: Atomic structure and chemistry of human serum albumin. Nature 1992, 358(6383):209-215.
15. Bhattacharya AA, Grüne T, Curry S: Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. Journal of Molecular Biology 2000, 303(5):721-732.
16. Zunszain P, Ghuman J, Komatsu T, Tsuchida E, Curry S: Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Structural Biology 2003, 3(1):6.
17. V.Jeney JB, A.Yachie, Z, Varga, G.M. Vercellotti, J.W. Eaton, and G.Balla: Pro-oxidant and cytotoxic effects of circulating heme. Blood 2002, 100:879-889.
18. J.BALLA GMV, V.JENEY,A.YACHIE,Z.VARGA,H.S. JACOB, J. W.EATON, and G.BALLA: Heme, Heme Oxygenase, and Ferritin: How the Vascular Endothelium Survives (and Dies) in an Iron-Rich Environment. Antioxidants & Redox Signaling 2007, 9:2119-2137.
19. Balla J, Vercellotti GM, Jeney V, Yachie A, Varga Z, Eaton JW, Balla G: Heme, heme oxygenase and ferritin in vascular endothelial cell injury. Molecular Nutrition & Food Research 2005, 49(11):1030-1043.
20. Vinchi F, Gastaldi S, Silengo L, Altruda F, Tolosano E: Hemopexin Prevents Endothelial Damage and Liver Congestion in a Mouse Model of Heme Overload. The American Journal of Pathology 2008, 173(1):289-299.
21. Altruda ETaF: Hemopexin: Structure, Function, and Regulation. DNA and Cell Biology 2002, 21:297.
22. Berman PAAaC: Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin. Biochem J 1980, 191:95.
23. Monzani E, Bonafè B, Fallarini A, Redaelli C, Casella L, Minchiotti L, Galliano M: Enzymatic properties of human hemalbumin. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 2001, 1547(2):302-312.
24. Watanabe K, Ishikawa N, Komatsu T: Human Serum Albumin-Based Peroxidase Having an Iron Protoporphyrin IX in Artificial Heme Pocket. Chemistry – An Asian Journal 2012, 7(11):2534-2537.
25. Ryunosuke Kato YK, Motofusa Akiyamaa and Teruyuki Komatsu: Human serum albumin mutants complexed Mn(III) protoporphyrin IX as superoxide dismutase mimics Dalton Trans 2013.
26. Komatsu T, Ohmichi N, Nakagawa A, Zunszain PA, Curry S, Tsuchida E: O2 and CO Binding Properties of Artificial Hemoproteins Formed by Complexing Iron Protoporphyrin IX with Human Serum Albumin Mutants. Journal of the American Chemical Society 2005, 127(45):15933-15942.
27. Komatsu T, Nakagawa A, Zunszain PA, Curry S, Tsuchida E: Genetic Engineering of the Heme Pocket in Human Serum Albumin: Modulation of O2 Binding of Iron Protoporphyrin IX by Variation of Distal Amino Acids. Journal of the American Chemical Society 2007, 129(36):11286-11295.
28. Teruyuki Komatsu AN, Stephen Curry, Eishun Tsuchida,a Kenichi Murata,d Nobuhumi Nakamurad and Hiroyuki Ohnod The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O2 and CO binding to iron protoporphyrin IX. Org Biomol Chem 2009, 7:3836-3841.
29. Akito Nakagawa TK, Stephen Curry, Eishun Tsuchida: O2 Binding Properties of Human Serum Albumin Quadruple Mutant Complexed Iron Protoporphyrin IX with Axial His-186 Coordination. The Chemical Society of Japan ,Chemistry Letters 2009, 8:776-777.
30. Komatsu T, Ohmichi N, Zunszain PA, Curry S, Tsuchida E: Dioxygenation of Human Serum Albumin Having a Prosthetic Heme Group in a Tailor-Made Heme Pocket. Journal of the American Chemical Society 2004, 126(44):14304-14305.
31. Elber R, Gibson QH: Toward Quantitative Simulations of Carbon Monoxide Escape Pathways in Myoglobin†. The Journal of Physical Chemistry B 2008, 112(19):6147-6154.
32. Maragliano L, Cottone G, Ciccotti G, Vanden-Eijnden E: Mapping the Network of Pathways of CO Diffusion in Myoglobin. Journal of the American Chemical Society 2009, 132(3):1010-1017.
33. Tomita A, Sato T, Ichiyanagi K, Nozawa S, Ichikawa H, Chollet M, Kawai F, Park S-Y, Tsuduki T, Yamato T et al: Visualizing breathing motion of internal cavities in concert with ligand migration in myoglobin. Proceedings of the National Academy of Sciences 2009, 106(8):2612-2616.
34. Lutz S, Nienhaus K, Nienhaus GU, Meuwly M: Ligand Migration between Internal Docking Sites in Photodissociated Carbonmonoxy Neuroglobin. The Journal of Physical Chemistry B 2009, 113(46):15334-15343.
35. Zhang B, Xu J, Li Y, Du W, Fang W: Molecular dynamics simulation of carboxy and deoxy human cytoglobin in solution. Journal of inorganic biochemistry 2011, 105(7):949-956.
36. Orlowski S, Nowak W: Locally enhanced sampling molecular dynamics study of the dioxygen transport in human cytoglobin. J Mol Model 2007, 13(6-7):715-723.
37. Takayanagi M, Kurisaki I, Nagaoka M: Oxygen Entry through Multiple Pathways in T-State Human Hemoglobin. The Journal of Physical Chemistry B 2013, 117(20):6082-6091.
38. Lepeshkevich SV, Biziuk SA, Lemeza AM, Dzhagarov BM: The kinetics of molecular oxygen migration in the isolated α chains of human hemoglobin as revealed by molecular dynamics simulations and laser kinetic spectroscopy. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2011, 1814(10):1279-1288.
39. Ciacchi LC, Payne MC: The entry pathway of O2 into human ferritin. Chemical Physics Letters 2004, 390(4–6):491-495.
40. Pesce A, Nardini M, Dewilde S, Capece L, Martí MA, Congia S, Salter MD, Blouin GC, Estrin DA, Ascenzi P et al: Ligand Migration in the Apolar Tunnel of Cerebratulus lacteus Mini-Hemoglobin. Journal of Biological Chemistry 2011, 286(7):5347-5358.
41. Daigle R, Guertin M, Lagüe P: Structural characterization of the tunnels of Mycobacterium tuberculosis truncated hemoglobin N from molecular dynamics simulations. Proteins: Structure, Function, and Bioinformatics 2009, 75(3):735-747.
42. Pietra F: On the Pathways of Biologically Relevant Diatomic Gases through Proteins. Dioxygen and Heme Oxygenase from the Perspective of Molecular Dynamics. Chemistry & Biodiversity 2013, 10(4):556-568.
43. Baron R, Riley C, Chenprakhon P, Thotsaporn K, Winter RT, Alfieri A, Forneris F, van Berkel WJH, Chaiyen P, Fraaije MW et al: Multiple pathways guide oxygen diffusion into flavoenzyme active sites. Proceedings of the National Academy of Sciences 2009, 106(26):10603-10608.
44. Teixeira VH, Baptista AM, Soares CM: Pathways of H2 toward the Active Site of [NiFe]-Hydrogenase. Biophysical Journal 2006, 91(6):2035-2045.
45. Elber R, Karplus M: Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin. Journal of the American Chemical Society 1990, 112(25):9161-9175.
46. Cohen J, Kim K, King P, Seibert M, Schulten K: Finding Gas Diffusion Pathways in Proteins: Application to O2 and H2 Transport in CpI [FeFe]-Hydrogenase and the Role of Packing Defects. Structure 2005, 13(9):1321-1329.
47. Shadrina MS, English AM, Peslherbe GH: Effective Simulations of Gas Diffusion Through Kinetically Accessible Tunnels in Multisubunit Proteins: O2 Pathways and Escape Routes in T-state Deoxyhemoglobin. Journal of the American Chemical Society 2012, 134(27):11177-11184.
48. Topin J, Diharce J, Fiorucci S, Antonczak S, Golebiowski J: O2 Migration Rates in [NiFe] Hydrogenases. A Joint Approach Combining Free-Energy Calculations and Kinetic Modeling. The Journal of Physical Chemistry B 2013, 118(3):676-681.
49. Das B, Helms V, Lounnas V, Wade RC: Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam. Journal of inorganic biochemistry 2000, 81(3):121-131.
50. Xu L, Liu X, Zhao W, Wang X: Locally Enhanced Sampling Study of Dioxygen Diffusion Pathways in Homoprotocatechuate 2,3-Dioxygenase. The Journal of Physical Chemistry B 2009, 113(41):13596-13603.
51. Kale L, Skeel R, Bhandarkar M, Brunner R, Gursoy A, Krawetz N, Phillips J, Shinozaki A, Varadarajan K, Schulten K: NAMD2: Greater scalability for parallel molecular dynamics. J Comp Phys 1999, 151(1):283-312.
52. Klauda JB, Venable RM, Freites JA, O′Connor JW, Tobias DJ, Mondragon-Ramirez C, Vorobyov I, MacKerell AD, Pastor RW: Update of the CHARMM All-Atom Additive Force Field for Lipids: Validation on Six Lipid Types. J Phys Chem B 2010, 114(23):7830-7843.
53. Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML: Comparison of Simple Potential Functions for Simulating Liquid Water. J Chem Phys 1983, 79(2):926-935.
54. Ryckaert J-P, Ciccotti G, Berendsen HJC: Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. J Comp Phys 1977, 23(3):327-341.
55. Feller SE, Zhang YH, Pastor RW, Brooks BR: Constant-Pressure Molecular-Dynamics Simulation - the Langevin Piston Method. J Chem Phys 1995, 103(11):4613-4621.
56. Steinbach PJ, Brooks BR: New Spherical-Cutoff Methods for Long-Range Forces in Macromolecular Simulation. J Comput Chem 1994, 15(7):667-683.
57. Guex N, Peitsch MC: SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling. ELECTROPHORESIS 1997, 18(15):2714-2723.
58. Cohen J, Arkhipov A, Braun R, Schulten K: Imaging the Migration Pathways for O2, CO, NO, and Xe Inside Myoglobin. Biophysical Journal 2006, 91(5):1844-1857.
59. Olson JS, Phillips Jr GN: Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand. J Biol Inorg Chem 1997, 2(4):544-552.
60. Springer BA, Sligar SG, Olson JS, Phillips GN, Jr.: Mechanisms of Ligand Recognition in Myoglobin. Chemical Reviews 1994, 94(3):699-714.
61. Liong EC, Dou Y, Scott EE, Olson JS, Phillips GN: Waterproofing the Heme Pocket: ROLE OF PROXIMAL AMINO ACID SIDE CHAINS IN PREVENTING HEMIN LOSS FROM MYOGLOBIN. Journal of Biological Chemistry 2001, 276(12):9093-9100.
62. Salomonsson L, Lee A, Gennis RB, Brzezinski P: A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter. Proceedings of the National Academy of Sciences of the United States of America 2004, 101(32):11617-11621.
63. de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M: Mapping protein matrix cavities in human cytoglobin through Xe atom binding. Biochemical and Biophysical Research Communications 2004, 316(4):1217-1221.
|