| Year |
Citation |
Score |
| 2014 |
Jayasundar JJ, Xing J, Robinson JM, Cheung HC, Dong WJ. Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints. Plos One. 9: e87135. PMID 24558365 DOI: 10.1371/Journal.Pone.0087135 |
0.658 |
|
| 2011 |
Robinson JM, Moutsoglou ME, Lackey T, Dong W, Chinnaraj M, Cheung HC. Single Molecule FRET Measurements Reveal Incomplete Activation of the Cardiac Myofilament by Ca2+ Biophysical Journal. 100: 113a. DOI: 10.1016/J.Bpj.2010.12.826 |
0.598 |
|
| 2010 |
Chinnaraj M, Dong W, Cheung HC, Robinson J. Nanobiology of the Cardiac Myofilament Biophysical Journal. 98: 353a. DOI: 10.1016/J.Bpj.2009.12.1908 |
0.616 |
|
| 2010 |
Jayasundar JJ, Xing J, Robinson JM, Cheung HC, Dong W. Structure of Troponin Complex:FRET and Molecular Dynamic Simulations Biophysical Journal. 98: 6a. DOI: 10.1016/J.Bpj.2009.12.037 |
0.647 |
|
| 2009 |
Jayasundar JJ, Xing J, Robinson JM, Cheung HC, Dong W. Proximity mapping of troponin T and troponin I in cardiac troponin using molecular dynamics simulations Biophysical Journal. 96: 503a. DOI: 10.1016/J.Bpj.2008.12.2594 |
0.628 |
|
| 2008 |
Xing J, Chinnaraj M, Zhang Z, Cheung HC, Dong WJ. Structural studies of interactions between cardiac troponin I and actin in regulated thin filament using Förster resonance energy transfer. Biochemistry. 47: 13383-93. PMID 19053249 DOI: 10.1021/Bi801492X |
0.54 |
|
| 2008 |
Robinson JM, Cheung HC, Dong W. The cardiac Ca2+-sensitive regulatory switch, a system in dynamic equilibrium. Biophysical Journal. 95: 4772-89. PMID 18676638 DOI: 10.1529/Biophysj.108.131318 |
0.63 |
|
| 2008 |
Dong WJ, Xing J, Ouyang Y, An J, Cheung HC. Structural kinetics of cardiac troponin C mutants linked to familial hypertrophic and dilated cardiomyopathy in troponin complexes. The Journal of Biological Chemistry. 283: 3424-32. PMID 18063575 DOI: 10.1074/Jbc.M703822200 |
0.48 |
|
| 2007 |
Dong WJ, Jayasundar JJ, An J, Xing J, Cheung HC. Effects of PKA phosphorylation of cardiac troponin I and strong crossbridge on conformational transitions of the N-domain of cardiac troponin C in regulated thin filaments. Biochemistry. 46: 9752-61. PMID 17676764 DOI: 10.1021/Bi700574N |
0.54 |
|
| 2006 |
Dong WJ, An J, Xing J, Cheung HC. Structural transition of the inhibitory region of troponin I within the regulated cardiac thin filament. Archives of Biochemistry and Biophysics. 456: 135-42. PMID 16962989 DOI: 10.1016/J.Abb.2006.08.007 |
0.536 |
|
| 2006 |
Lamani E, Mewbourne RB, Fletcher DS, Maltsev SD, Danilov LL, Veselovsky VV, Lozanova AV, Grigorieva NY, Pinsker OA, Xing J, Forsee WT, Cheung HC, Schutzbach JS, Shibaev VN, Jedrzejas MJ. Structural studies and mechanism of Saccharomyces cerevisiae dolichyl-phosphate-mannose synthase: insights into the initial step of synthesis of dolichyl-phosphate-linked oligosaccharide chains in membranes of endoplasmic reticulum. Glycobiology. 16: 666-78. PMID 16549409 DOI: 10.1093/Glycob/Cwj104 |
0.333 |
|
| 2006 |
Maliga Z, Xing J, Cheung H, Juszczak LJ, Friedman JM, Rosenfeld SS. A pathway of structural changes produced by monastrol binding to Eg5. The Journal of Biological Chemistry. 281: 7977-82. PMID 16434397 DOI: 10.1074/Jbc.M511955200 |
0.319 |
|
| 2005 |
Brouillette CG, Dong WJ, Yang ZW, Ray MJ, Protasevich II, Cheung HC, Engler JA. Förster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I. Biochemistry. 44: 16413-25. PMID 16342934 DOI: 10.1021/Bi051018V |
0.366 |
|
| 2004 |
Robinson JM, Dong WJ, Xing J, Cheung HC. Switching of troponin I: Ca(2+) and myosin-induced activation of heart muscle. Journal of Molecular Biology. 340: 295-305. PMID 15201053 DOI: 10.1016/J.Jmb.2004.04.046 |
0.635 |
|
| 2004 |
Kobayashi T, Dong WJ, Burkart EM, Cheung HC, Solaro RJ. Effects of protein kinase C dependent phosphorylation and a familial hypertrophic cardiomyopathy-related mutation of cardiac troponin I on structural transition of troponin C and myofilament activation. Biochemistry. 43: 5996-6004. PMID 15147183 DOI: 10.1021/Bi036073N |
0.403 |
|
| 2003 |
Dong WJ, Robinson JM, Xing J, Cheung HC. Kinetics of conformational transitions in cardiac troponin induced by Ca2+ dissociation determined by Förster resonance energy transfer. The Journal of Biological Chemistry. 278: 42394-402. PMID 12909617 DOI: 10.1074/Jbc.M304858200 |
0.646 |
|
| 2003 |
Heller WT, Finley NL, Dong WJ, Timmins P, Cheung HC, Rosevear PR, Trewhella J. Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation. Biochemistry. 42: 7790-800. PMID 12820888 DOI: 10.1021/Bi0341509 |
0.348 |
|
| 2003 |
Robinson JM, Dong WJ, Cheung HC. Can Förster resonance energy transfer measurements uniquely position troponin residues on the actin filament? A case study in multiple-acceptor FRET. Journal of Molecular Biology. 329: 371-80. PMID 12758083 DOI: 10.1016/S0022-2836(03)00424-8 |
0.583 |
|
| 2003 |
Burghardt TP, Park S, Dong WJ, Xing J, Cheung HC, Ajtai K. Energy transduction optical sensor in skeletal myosin. Biochemistry. 42: 5877-84. PMID 12741846 DOI: 10.1021/Bi026183E |
0.38 |
|
| 2003 |
Sheldahl C, Xing J, Dong WJ, Harvey SC, Cheung HC. The calcium-saturated cTnI/cTnC complex: structure of the inhibitory region of cTnI. Biophysical Journal. 84: 1057-64. PMID 12547787 DOI: 10.1016/S0006-3495(03)74922-4 |
0.683 |
|
| 2003 |
Dong WJ, Robinson JM, Stagg S, Xing J, Cheung HC. Ca2+-induced conformational transition in the inhibitory and regulatory regions of cardiac troponin I. The Journal of Biological Chemistry. 278: 8686-92. PMID 12511564 DOI: 10.1074/Jbc.M212886200 |
0.748 |
|
| 2002 |
Robinson JM, Wang Y, Kerrick WG, Kawai R, Cheung HC. Activation of striated muscle: nearest-neighbor regulatory-unit and cross-bridge influence on myofilament kinetics. Journal of Molecular Biology. 322: 1065-88. PMID 12367529 DOI: 10.1016/S0022-2836(02)00855-0 |
0.609 |
|
| 2001 |
Dong WJ, Xing J, Robinson JM, Cheung HC. Ca(2+) induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin. Journal of Molecular Biology. 314: 51-61. PMID 11724531 DOI: 10.1006/Jmbi.2001.5118 |
0.69 |
|
| 2001 |
Abbott MB, Dong WJ, Dvoretsky A, DaGue B, Caprioli RM, Cheung HC, Rosevear PR. Modulation of cardiac troponin C-cardiac troponin I regulatory interactions by the amino-terminus of cardiac troponin I. Biochemistry. 40: 5992-6001. PMID 11352734 DOI: 10.1021/Bi0100642 |
0.418 |
|
| 2000 |
Dong WJ, Xing J, Chandra M, Solaro J, Cheung HC. Structural mapping of single cysteine mutants of cardiac troponin I. Proteins. 41: 438-47. PMID 11056032 DOI: 10.1002/1097-0134(20001201)41:4<438::Aid-Prot20>3.0.Co;2-E |
0.517 |
|
| 2000 |
Xing J, Wriggers W, Jefferson GM, Stein R, Cheung HC, Rosenfeld SS. Kinesin has three nucleotide-dependent conformations. Implications for strain-dependent release. The Journal of Biological Chemistry. 275: 35413-23. PMID 10852922 DOI: 10.1074/Jbc.M004232200 |
0.4 |
|
| 2000 |
Rosenfeld SS, Xing J, Whitaker M, Cheung HC, Brown F, Wells A, Milligan RA, Sweeney HL. Kinetic and spectroscopic evidence for three actomyosin:ADP states in smooth muscle. The Journal of Biological Chemistry. 275: 25418-26. PMID 10827085 DOI: 10.1074/Jbc.M002685200 |
0.403 |
|
| 2000 |
Dong WJ, Robinson JM, Xing J, Umeda PK, Cheung HC. An interdomain distance in cardiac troponin C determined by fluorescence spectroscopy. Protein Science : a Publication of the Protein Society. 9: 280-9. PMID 10716180 DOI: 10.1110/Ps.9.2.280 |
0.647 |
|
| 2000 |
Shibaev VN, Veselovsky VV, Lozanova AV, Maltsev SD, Danilov LL, Forsee WT, Xing J, Cheung HC, Jedrzejas MJ. Synthesis of dolichyl phosphate derivatives with fluorescent label at the omega-end of the chain, new tools to study protein glycosylation. Bioorganic & Medicinal Chemistry Letters. 10: 189-92. PMID 10673108 DOI: 10.1016/S0960-894X(99)00662-9 |
0.304 |
|
| 1999 |
Dong WJ, Xing J, Villain M, Hellinger M, Robinson JM, Chandra M, Solaro RJ, Umeda PK, Cheung HC. Conformation of the regulatory domain of cardiac muscle troponin C in its complex with cardiac troponin I. The Journal of Biological Chemistry. 274: 31382-90. PMID 10531339 DOI: 10.1074/Jbc.274.44.31382 |
0.682 |
|
| 1999 |
Finley N, Abbott MB, Abusamhadneh E, Gaponenko V, Dong W, Gasmi-Seabrook G, Howarth JW, Rance M, Solaro RJ, Cheung HC, Rosevear PR. NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation. Febs Letters. 453: 107-12. PMID 10403385 DOI: 10.1016/S0014-5793(99)00693-6 |
0.407 |
|
| 1998 |
Rosenfeld SS, Xing J, Cheung HC, Brown F, Kar S, Sweeney HL. Structural and kinetic studies of phosphorylation-dependent regulation in smooth muscle myosin. The Journal of Biological Chemistry. 273: 28682-90. PMID 9786863 DOI: 10.1074/Jbc.273.44.28682 |
0.378 |
|
| 1998 |
She M, Xing J, Dong WJ, Umeda PK, Cheung HC. Calcium binding to the regulatory domain of skeletal muscle troponin C induces a highly constrained open conformation. Journal of Molecular Biology. 281: 445-52. PMID 9698560 DOI: 10.1006/Jmbi.1998.1933 |
0.45 |
|
| 1998 |
She M, Dong WJ, Umeda PK, Cheung HC. Tryptophan mutants of troponin C from skeletal muscle--an optical probe of the regulatory domain. European Journal of Biochemistry / Febs. 252: 600-7. PMID 9546679 DOI: 10.1046/J.1432-1327.1998.2520600.X |
0.479 |
|
| 1997 |
Chandra M, Dong WJ, Pan BS, Cheung HC, Solaro RJ. Effects of protein kinase A phosphorylation on signaling between cardiac troponin I and the N-terminal domain of cardiac troponin C. Biochemistry. 36: 13305-11. PMID 9341222 DOI: 10.1021/Bi9710129 |
0.493 |
|
| 1997 |
She M, Dong WJ, Umeda PK, Cheung HC. Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C. Biophysical Journal. 73: 1042-55. PMID 9251821 DOI: 10.1016/S0006-3495(97)78137-2 |
0.447 |
|
| 1997 |
Dong WJ, Wang CK, Gordon AM, Rosenfeld SS, Cheung HC. A kinetic model for the binding of Ca2+ to the regulatory site of troponin from cardiac muscle. The Journal of Biological Chemistry. 272: 19229-35. PMID 9235915 DOI: 10.1074/Jbc.272.31.19229 |
0.494 |
|
| 1997 |
Dong WJ, Chandra M, Xing J, She M, Solaro RJ, Cheung HC. Phosphorylation-induced distance change in a cardiac muscle troponin I mutant. Biochemistry. 36: 6754-61. PMID 9184157 DOI: 10.1021/bi9622276 |
0.368 |
|
| 1997 |
Dong WJ, Chandra M, Xing J, Solaro RJ, Cheung HC. Conformation of the N-terminal segment of a monocysteine mutant of troponin I from cardiac muscle. Biochemistry. 36: 6745-53. PMID 9184156 DOI: 10.1021/bi962226d |
0.324 |
|
| 1997 |
Dong WJ, Wang CK, Gordon AM, Cheung HC. Disparate fluorescence properties of 2-[4'-(iodoacetamido)anilino]-naphthalene-6-sulfonic acid attached to Cys-84 and Cys-35 of troponin C in cardiac muscle troponin. Biophysical Journal. 72: 850-7. PMID 9017210 DOI: 10.1016/S0006-3495(97)78719-8 |
0.487 |
|
| 1996 |
Rosenfeld SS, Correia JJ, Xing J, Rener B, Cheung HC. Structural studies of kinesin-nucleotide intermediates. The Journal of Biological Chemistry. 271: 30212-21. PMID 8939973 DOI: 10.1074/Jbc.271.47.30212 |
0.374 |
|
| 1996 |
Dong WJ, Cheung HC. Calcium-induced conformational change in cardiac troponin C studied by fluorescence probes attached to Cys-84. Biochimica Et Biophysica Acta. 1295: 139-46. PMID 8695639 DOI: 10.1016/0167-4838(96)00028-3 |
0.49 |
|
| 1996 |
Rosenfeld SS, Rener B, Correia JJ, Mayo MS, Cheung HC. Equilibrium studies of kinesin-nucleotide intermediates. The Journal of Biological Chemistry. 271: 9473-82. PMID 8621618 DOI: 10.1074/Jbc.271.16.9473 |
0.368 |
|
| 1996 |
Dong W, Rosenfeld SS, Wang CK, Gordon AM, Cheung HC. Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle. The Journal of Biological Chemistry. 271: 688-94. PMID 8557674 DOI: 10.1074/Jbc.271.2.688 |
0.481 |
|
| 1995 |
Xing J, Cheung HC. Internal movement in myosin subfragment 1 detected by fluorescence resonance energy transfer. Biochemistry. 34: 6475-87. PMID 7756279 DOI: 10.1021/Bi00019A029 |
0.435 |
|
| 1994 |
Xing J, Cheung HC. Vanadate-induced changes in myosin subfragment-1 from cardiac muscle. Archives of Biochemistry and Biophysics. 313: 229-34. PMID 8080266 DOI: 10.1006/abbi.1994.1381 |
0.305 |
|
| 1994 |
Censullo R, Cheung HC. Tropomyosin length and two-stranded F-actin flexibility in the thin filament. Journal of Molecular Biology. 243: 520-9. PMID 7966277 DOI: 10.1006/Jmbi.1994.1677 |
0.367 |
|
| 1994 |
Liao R, Wang CK, Cheung HC. Coupling of calcium to the interaction of troponin I with troponin C from cardiac muscle. Biochemistry. 33: 12729-34. PMID 7918499 DOI: 10.1021/Bi00208A026 |
0.488 |
|
| 1993 |
Lin SH, Harzelrig JB, Cheung HC. Transient kinetics of the interaction of actin with myosin subfragment-1 in the absence of nucleotide. Biophysical Journal. 65: 1433-44. PMID 8274637 DOI: 10.1016/S0006-3495(93)81209-8 |
0.351 |
|
| 1992 |
Censullo R, Martin JC, Cheung HC. The use of the isotropic orientation factor in fluorescence resonance energy transfer (FRET) studies of the actin filament. Journal of Fluorescence. 2: 141-55. PMID 24241625 DOI: 10.1007/Bf00866929 |
0.321 |
|
| 1992 |
Lin SH, Cheung HC. The kinetics of a two-state transition of myosin subfragment 1. A temperature-jump relaxation study. Febs Letters. 304: 184-6. PMID 1618320 DOI: 10.1016/0014-5793(92)80614-M |
0.32 |
|
| 1992 |
Wang CK, Liao R, Cheung HC. Nanosecond study of fluorescently labeled troponin C. Biochimica Et Biophysica Acta. 1121: 16-22. PMID 1599937 DOI: 10.1016/0167-4838(92)90331-7 |
0.418 |
|
| 1992 |
Wang CK, Mani RS, Kay CM, Cheung HC. Conformation and dynamics of bovine brain S-100a protein determined by fluorescence spectroscopy. Biochemistry. 31: 4289-95. PMID 1567874 DOI: 10.1021/Bi00132A020 |
0.395 |
|
| 1992 |
Liao R, Wang CK, Cheung HC. Time-resolved tryptophan emission study of cardiac troponin I. Biophysical Journal. 63: 986-95. PMID 1420937 DOI: 10.1016/S0006-3495(92)81685-5 |
0.417 |
|
| 1991 |
Cheung HC, Wang CK, Gryczynski I, Wiczk W, Laczko G, Johnson ML, Lakowicz JR. Distance distributions and anisotropy decays of troponin C and its complex with troponin I. Biochemistry. 30: 5238-47. PMID 2036391 DOI: 10.1021/Bi00235A018 |
0.445 |
|
| 1991 |
Lin SH, Cheung HC. Two-state equilibria of myosin subfragment 1 and its complexes with ADP and actin. Biochemistry. 30: 4317-22. PMID 2021623 DOI: 10.1021/Bi00231A030 |
0.343 |
|
| 1991 |
Cheung HC, Gryczynski I, Malak H, Wiczk W, Johnson ML, Lakowicz JR. Conformational flexibility of the Cys 697-Cys 707 segment of myosin subfragment-1. Distance distributions by frequency-domain fluorometry. Biophysical Chemistry. 40: 1-17. PMID 1873469 DOI: 10.1016/0301-4622(91)85025-L |
0.404 |
|
| 1989 |
Aguirre R, Lin SH, Gonsoulin F, Wang CK, Cheung HC. Characterization of the ethenoadenosine diphosphate binding site of myosin subfragment 1. Energetics of the equilibrium between two states of nucleotide.S1 and vanadate-induced global conformation changes detected by energy transfer. Biochemistry. 28: 799-807. PMID 2713346 DOI: 10.1021/Bi00428A058 |
0.38 |
|
| 1989 |
Lopez-Lacomba JL, Guzman M, Cortijo M, Mateo PL, Aguirre R, Harvey SC, Cheung HC. Differential scanning calorimetric study of the thermal unfolding of myosin rod, light meromyosin, and subfragment 2. Biopolymers. 28: 2143-59. PMID 2690963 DOI: 10.1002/Bip.360281208 |
0.527 |
|
| 1989 |
Wang CK, Lebowitz J, Cheung HC. Acid-induced dimerization of skeletal troponin C. Proteins. 6: 424-30. PMID 2622912 DOI: 10.1002/Prot.340060409 |
0.345 |
|
| 1988 |
Lakowicz JR, Gryczynski I, Cheung HC, Wang CK, Johnson ML. Distance distributions in native and random-coil troponin I from frequency-domain measurements of fluorescence energy transfer. Biopolymers. 27: 821-30. PMID 3382720 DOI: 10.1002/Bip.360270509 |
0.333 |
|
| 1988 |
Lakowicz JR, Gryczynski I, Cheung HC, Wang CK, Johnson ML, Joshi N. Distance distributions in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C. Biochemistry. 27: 9149-60. PMID 3242618 DOI: 10.1021/Bi00426A012 |
0.363 |
|
| 1987 |
Malik NA, Anantharamaiah GM, Gawish A, Cheung HC. Structural and biological studies on synthetic peptide analogues of a low-affinity calcium-binding site of skeletal troponin C. Biochimica Et Biophysica Acta. 911: 221-30. PMID 3801495 DOI: 10.1016/0167-4838(87)90011-2 |
0.386 |
|
| 1987 |
Cheung HC, Wang CK, Malik NA. Interactions of troponin subunits: free energy of binary and ternary complexes. Biochemistry. 26: 5904-7. PMID 3676297 DOI: 10.1021/Bi00392A049 |
0.436 |
|
| 1987 |
Wang C, Lebowitz J, Cheung HC. Comparative Hydrodynamic Properties Of Rabbit Skeletal And Bovine Cardiac Troponin C And Bovine Brain Calmodulin Calcium-Binding Proteins in Health and Disease. 415-417. DOI: 10.1016/B978-0-12-521040-9.50073-5 |
0.344 |
|
| 1986 |
Aguirre R, Gonsoulin F, Cheung HC. Interaction of fluorescently labeled myosin subfragment 1 with nucleotides and actin. Biochemistry. 25: 6827-35. PMID 3801396 DOI: 10.1021/Bi00370A015 |
0.37 |
|
| 1986 |
Wang CK, Cheung HC. Proximity relationship in the binary complex formed between troponin I and troponin C. Journal of Molecular Biology. 191: 509-21. PMID 2950237 DOI: 10.1016/0022-2836(86)90145-2 |
0.491 |
|
| 1986 |
Hunsinger RN, Cheung HC. Probe of the (Ca2+ + Mg2+)-ATPase in erythrocyte membranes of cystic fibrosis patients. Clinica Chimica Acta; International Journal of Clinical Chemistry. 156: 165-77. PMID 2940033 DOI: 10.1016/0009-8981(86)90150-6 |
0.366 |
|
| 1985 |
Wang CK, Cheung HC. Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle. Biophysical Journal. 48: 727-39. PMID 4074834 DOI: 10.1016/S0006-3495(85)83831-5 |
0.349 |
|
| 1985 |
Cheung HC, Gonsoulin F, Garland F. An investigation of the SH1-SH2 and SH1-ATPase distances in myosin subfragment-1 by resonance energy transfer using nanosecond fluorimetry. Biochimica Et Biophysica Acta. 832: 52-62. PMID 2932161 DOI: 10.1016/0167-4838(85)90173-6 |
0.363 |
|
| 1984 |
Cheung HC, Liu BM. Distance between nucleotide site and cysteine-373 of G-actin by resonance energy transfer measurements Journal of Muscle Research and Cell Motility. 5: 65-80. PMID 6715528 DOI: 10.1007/Bf00713152 |
0.357 |
|
| 1983 |
Kanellis P, Yang J, Cheung HC, Lenkinski RE. Synthetic peptide analogs of skeletal troponin C: Fluorescence studies of analogs of the low-affinity calcium-binding site II Archives of Biochemistry and Biophysics. 220: 530-540. PMID 6824337 DOI: 10.1016/0003-9861(83)90444-7 |
0.313 |
|
| 1982 |
Cheung HC, Wang CK, Garland F. Fluorescence energy transfer studies of skeletal troponin C proximity between methionine-25 and cysteine-98 Biochemistry. 21: 5135-5142. PMID 7171543 DOI: 10.1021/Bi00264A005 |
0.491 |
|
| 1981 |
Liu BM, Cheung HC, Mestecky J. Nanosecond fluorescence spectroscopy of human immunoglobulin A Biochemistry. 20: 1997-2003. PMID 7225369 DOI: 10.1021/Bi00510A040 |
0.352 |
|
| 1980 |
Liu BM, Cheung HC, Chen KH, Habercom MS. Fluorescence decay kinetics of pyrene in membrane vesicles Biophysical Chemistry. 12: 341-355. PMID 7225521 DOI: 10.1016/0301-4622(80)80012-3 |
0.314 |
|
| 1980 |
Garland F, Graves DE, Yielding LW, Cheung HC. Comparative studies of the binding of ethidium bromide and its photoreactive analogues to nucleic acids by fluorescence and rapid kinetics Biochemistry. 19: 3221-3226. PMID 7190829 DOI: 10.1021/Bi00555A019 |
0.319 |
|
| 1980 |
Harvey SC, Cheung HC. Transport properties of particles with segmental flexibility. II. Decay of fluorescence polarization anisotropy from hinged macromolecules Biopolymers. 19: 913-930. DOI: 10.1002/Bip.1980.360190414 |
0.532 |
|
| 1979 |
Garland F, Cheung HC. Fluorescence stopped-flow study of the mechanism of nucleotide binding to myosin subfragment Biochemistry. 18: 5281-5289. PMID 518834 DOI: 10.1021/Bi00591A003 |
0.34 |
|
| 1978 |
Habercom MS, Cheung HC. Ligand binding to sarcoplasmic reticulum. The effects of Ca2+, Mg2+, and ATP binding on the fluorescence of membrane-bound pyrene Archives of Biochemistry and Biophysics. 191: 756-763. PMID 742899 DOI: 10.1016/0003-9861(78)90417-4 |
0.44 |
|
| 1977 |
Harvey SC, Cheung HC. Fluorescence depolarization studies on the flexibility of myosin rod. Biochemistry. 16: 5181-7. PMID 921927 DOI: 10.1021/Bi00643A004 |
0.545 |
|
| 1977 |
Harvey SC, Cheung HC, Thames KE. Cooperativity in F-actin filaments on binding of myosin subfragments, demonstrated by fluorescence of 1, N6- ethenoadenosine diphosphate. Archives of Biochemistry and Biophysics. 179: 391-6. PMID 322615 DOI: 10.1016/0003-9861(77)90126-6 |
0.548 |
|
| 1976 |
Harvey SC, Cheung HC. Fluorescence studies of 1,N6-ethenoadenosine triphosphate bound to G-actin: the nucleotide base is inaccessible to water. Biochemical and Biophysical Research Communications. 73: 865-8. PMID 15625854 DOI: 10.1016/0006-291X(76)90201-1 |
0.538 |
|
| 1976 |
Garland F, Cheung HC. Binding of 1,N6-ethenoadenosine 5′-diphosphate to heavy meromyosin and to myosin subfragment-1 Febs Letters. 66: 198-201. PMID 782915 DOI: 10.1016/0014-5793(76)80503-0 |
0.315 |
|
| 1976 |
Harvey SC, Cheung HC. Fluorescence studies of 1,N6-ethenoadenosine triphosphate bound to G-actin: The nucleotide base is inaccessible to water Biochemical and Biophysical Research Communications. 73: 865-868. DOI: 10.1016/0006-291X(76)90201-1 |
0.485 |
|
| 1974 |
Thames KE, Cheung HC, Harvey SC. Binding of 1,N6-ethanoadenosine triphosphate to actin. Biochemical and Biophysical Research Communications. 60: 1252-61. PMID 4214008 DOI: 10.1016/0006-291X(74)90333-7 |
0.561 |
|
| 1972 |
Harvey SC, Cheung HC. Computer simulation of fluorescence depolarization due to brownian motion. Proceedings of the National Academy of Sciences of the United States of America. 69: 3670-2. PMID 16592039 DOI: 10.1073/Pnas.69.12.3670 |
0.502 |
|
| 1969 |
Cheung HC, Morales MF. Studies of myosin conformation by fluorescent techniques. Biochemistry. 8: 2177-82. PMID 4977582 DOI: 10.1021/Bi00833A059 |
0.314 |
|
| 1969 |
Cheung HC. Conformation of myosin Effects of substrate and modifiers Bba - Protein Structure. 194: 478-485. PMID 4243908 DOI: 10.1016/0005-2795(69)90108-1 |
0.319 |
|
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