Year |
Citation |
Score |
2020 |
Cao S, Li H, Liu Y, Wang M, Zhang M, Zhang S, Chen J, Xu J, Knutson JR, Brand L. Dehydrogenase Binding Sites Abolish the "Dark" Fraction of NADH: Implication for Metabolic Sensing Via FLIM. The Journal of Physical Chemistry. B. PMID 32660250 DOI: 10.1021/Acs.Jpcb.0C04835 |
0.407 |
|
2015 |
Xu J, Chen B, Callis P, Muiño PL, Rozeboom H, Broos J, Toptygin D, Brand L, Knutson JR. Picosecond fluorescence dynamics of tryptophan and 5-fluorotryptophan in monellin: slow water-protein relaxation unmasked. The Journal of Physical Chemistry. B. 119: 4230-9. PMID 25710196 DOI: 10.1021/acs.jpcb.5b01651 |
0.352 |
|
2013 |
Nanda V, Cristian L, Toptygin D, Brand L, Degrado WF. Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan. Chemical Physics. 422. PMID 24273370 DOI: 10.1016/J.Chemphys.2012.12.018 |
0.623 |
|
2012 |
Toptygin D, Brand L. Nonequilibrium Molecular Dynamics of Trp Zwitterion in Water: Picosecond Fluorescence Measurements Versus Computer Simulations Biophysical Journal. 102: 217a. DOI: 10.1016/J.Bpj.2011.11.1190 |
0.385 |
|
2011 |
Toptygin D, Brand L, Chirikjian GS. Global Analysis of Time-Resolved Anisotropy from Multiple Probes in a Rigid Globular Protein Biophysical Journal. 100: 136a. DOI: 10.1016/J.Bpj.2010.12.945 |
0.411 |
|
2011 |
Toptygin D, Woolf TB, Brand L. TDSS in Trp Fluorescence Reveals Multiple Protein and Solvent Relaxation Modes Biophysical Journal. 100: 609a. DOI: 10.1016/J.Bpj.2010.12.3507 |
0.342 |
|
2011 |
Brand L. Tryptophan Fluorescence from G. Weber to the Present Biophysical Journal. 100: 609a. DOI: 10.1016/J.Bpj.2010.12.3505 |
0.487 |
|
2010 |
Toptygin D, Woolf TB, Brand L. Picosecond protein dynamics: the origin of the time-dependent spectral shift in the fluorescence of the single Trp in the protein GB1. The Journal of Physical Chemistry. B. 114: 11323-37. PMID 20701310 DOI: 10.1021/jp104425t |
0.304 |
|
2010 |
Seliskar CJ, Brand L. Solvent dependence of the luminescence of N-arylaminonaphthalenesulfonates. Science (New York, N.Y.). 171: 799-800. PMID 17812024 DOI: 10.1126/Science.171.3973.799 |
0.438 |
|
2009 |
Xu J, Chen J, Toptygin D, Tcherkasskaya O, Callis P, King J, Brand L, Knutson JR. Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching. Journal of the American Chemical Society. 131: 16751-7. PMID 19919143 DOI: 10.1021/Ja904857T |
0.449 |
|
2009 |
Toptygin D, Woolf TB, Brand L. MD Simulations of the Time-Dependent Red Shift in the Fluorescence of Trp in Protein GB1 Biophysical Journal. 96: 47a. DOI: 10.1016/J.Bpj.2008.12.140 |
0.379 |
|
2009 |
Xu J, Tcherkasskaya O, Gronenborn AM, Callis P, Toptygin D, Gleason FK, Brand L, Knutson JR. Ultrafast Decay of Trp in Biological Macromolecules Biophysical Journal. 96: 46a. DOI: 10.1016/J.Bpj.2008.12.133 |
0.455 |
|
2008 |
Brand L, Johnson ML. Preface. Methods in Enzymology (fluorescence 2008). Methods in Enzymology. 450: xv-xvi. PMID 19152852 DOI: 10.1016/S0076-6879(08)03419-8 |
0.411 |
|
2008 |
Chen J, Toptygin D, Brand L, King J. Mechanism of the efficient tryptophan fluorescence quenching in human gammaD-crystallin studied by time-resolved fluorescence. Biochemistry. 47: 10705-21. PMID 18795792 DOI: 10.1021/Bi800499K |
0.361 |
|
2006 |
Toptygin D, Gronenborn AM, Brand L. Nanosecond relaxation dynamics of protein GB1 identified by the time-dependent red shift in the fluorescence of tryptophan and 5-fluorotryptophan. The Journal of Physical Chemistry. B. 110: 26292-302. PMID 17181288 DOI: 10.1021/Jp064528N |
0.481 |
|
2006 |
Eggeling C, Widengren J, Brand L, Schaffer J, Felekyan S, Seidel CA. Analysis of photobleaching in single-molecule multicolor excitation and Förster resonance energy transfer measurements. The Journal of Physical Chemistry. A. 110: 2979-95. PMID 16509620 DOI: 10.1021/Jp054581W |
0.362 |
|
2006 |
Xu J, Toptygin D, Graver KJ, Albertini RA, Savtchenko RS, Meadow ND, Roseman S, Callis PR, Brand L, Knutson JR. Ultrafast fluorescence dynamics of tryptophan in the proteins monellin and IIAGlc. Journal of the American Chemical Society. 128: 1214-21. PMID 16433538 DOI: 10.1021/Ja055746H |
0.377 |
|
2002 |
Palo K, Brand L, Eggeling C, Jäger S, Kask P, Gall K. Fluorescence intensity and lifetime distribution analysis: toward higher accuracy in fluorescence fluctuation spectroscopy. Biophysical Journal. 83: 605-18. PMID 12124251 DOI: 10.1016/S0006-3495(02)75195-3 |
0.371 |
|
2001 |
Eggeling C, Berger S, Brand L, Fries JR, Schaffer J, Volkmer A, Seidel CA. Data registration and selective single-molecule analysis using multi-parameter fluorescence detection. Journal of Biotechnology. 86: 163-80. PMID 11257530 DOI: 10.1016/S0168-1656(00)00412-0 |
0.347 |
|
2001 |
Toptygin D, Savtchenko RS, Meadow ND, Brand L. Homogeneous spectrally- and time-resolved fluorescence emission from single-tryptophan mutants of IIAGlc protein Journal of Physical Chemistry B. 105: 2043-2055. DOI: 10.1021/Jp003405E |
0.432 |
|
2000 |
Nanda V, Liang SM, Brand L. Hydrophobic clustering in acid-denatured IL-2 and fluorescence of a Trp NH-pi H-bond. Biochemical and Biophysical Research Communications. 279: 770-8. PMID 11162427 DOI: 10.1006/Bbrc.2000.4033 |
0.583 |
|
2000 |
Reshetnyak YK, Andreev OA, Borejdo J, Toptygin DD, Brand L, Burstein EA. The identification of tryptophan residues responsible for ATP-induced increase in intrinsic fluorescence of myosin subfragment 1. Journal of Biomolecular Structure & Dynamics. 18: 113-25. PMID 11021656 DOI: 10.1080/07391102.2000.10506651 |
0.325 |
|
2000 |
Nanda V, Brand L. Aromatic interactions in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan. Proteins. 40: 112-25. PMID 10813836 DOI: 10.1002/(Sici)1097-0134(20000701)40:1<112::Aid-Prot130>3.0.Co;2-C |
0.607 |
|
2000 |
Toptygin D, Brand L. Spectrally- and time-resolved fluorescence emission of indole during solvent relaxation: A quantitative model Chemical Physics Letters. 322: 496-502. |
0.325 |
|
1999 |
Russo AT, Brand L. A Nanosecond Time-Resolved Fluorescence Study of Recombinant Human Myelin Basic Protein Journal of Fluorescence. 9: 333-342. DOI: 10.1023/A:1020540125166 |
0.752 |
|
1998 |
Hirshfield KM, Toptygin D, Grandhige G, Packard BZ, Brand L. A nanosecond fluorescence study of the simultaneous influx of Ca2+ and Cd2+ into liposomes. Biophysical Chemistry. 71: 63-72. PMID 9591360 DOI: 10.1016/S0301-4622(97)00136-1 |
0.402 |
|
1998 |
Brown MP, Toptygin D, Lee KB, Animashaun T, Hughes RC, Lee YC, Brand L. The tryptophan fluorescence of Tetracarbidium conophorum agglutinin II and a solution-based assay for the binding of a biantennary glycopeptide. Journal of Protein Chemistry. 17: 149-59. PMID 9535277 DOI: 10.1023/A:1022583617208 |
0.392 |
|
1998 |
Eggeling C, Fries JR, Brand L, Günther R, Seidel CA. Monitoring conformational dynamics of a single molecule by selective fluorescence spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 95: 1556-61. PMID 9465054 DOI: 10.1073/Pnas.95.4.1556 |
0.35 |
|
1998 |
Wang K, Rodgers ME, Toptygin D, Munsen VA, Brand L. Fluorescence study of the multiple binding equilibria of the galactose repressor Biochemistry. 37: 41-50. PMID 9425024 DOI: 10.1021/Bi972004V |
0.372 |
|
1998 |
Packard BZ, Komoriya A, Nanda V, Brand L. Intramolecular excitonic dimers in protease substrates: Modification of the backbone moiety to probe the H-dimer structure Journal of Physical Chemistry B. 102: 1820-1827. DOI: 10.1021/Jp973419T |
0.4 |
|
1998 |
Packard BZ, Toptygin DD, Komoriya A, Brand L. Intramolecular resonance dipole-dipole interactions in a profluorescent protease substrate Journal of Physical Chemistry B. 102: 752-758. DOI: 10.1021/Jp972845B |
0.441 |
|
1997 |
Packard BZ, Toptygin DD, Komoriya A, Brand L. Characterization of fluorescence quenching in bifluorophoric protease substrates. Biophysical Chemistry. 67: 167-76. PMID 17029895 DOI: 10.1016/S0301-4622(97)00036-7 |
0.432 |
|
1997 |
Wu P, Brand L. N-terminal modification of proteins for fluorescence measurements Methods in Enzymology. 278: 321-330. PMID 9170320 DOI: 10.1016/S0076-6879(97)78017-0 |
0.377 |
|
1997 |
Packard BZ, Komoriya A, Toptygin DD, Brand L. Structural characteristics of fluorophores that form intramolecular H-type dimers in a protease substrate Journal of Physical Chemistry B. 101: 5070-5074. DOI: 10.1021/Jp9702210 |
0.401 |
|
1997 |
Toptygin D, Packard BZ, Brand L. Resolution of absorption spectra of rhodamine 6g aggregates in aqueous solution using the law of mass action Chemical Physics Letters. 277: 430-435. DOI: 10.1016/S0009-2614(97)00943-3 |
0.314 |
|
1996 |
Hirshfield KM, Toptygin D, Grandhige G, Kim H, Packard BZ, Brand L. Steady-state and time-resolved fluorescence measurements for studying molecular interactions: Interaction of a calcium-binding probe with proteins Biophysical Chemistry. 62: 25-38. PMID 8962469 DOI: 10.1016/S0301-4622(96)00027-0 |
0.396 |
|
1996 |
Packard BZ, Toptygin DD, Komoriya A, Brand L. Profluorescent protease substrates: Intramolecular dimers described by the exciton model Proceedings of the National Academy of Sciences of the United States of America. 93: 11640-11645. PMID 8876189 DOI: 10.1073/Pnas.93.21.11640 |
0.435 |
|
1995 |
Toptygin D, Brand L. Analysis of equilibrium binding data obtained by linear-response spectroscopic techniques Analytical Biochemistry. 224: 330-338. PMID 7710091 DOI: 10.1006/Abio.1995.1048 |
0.356 |
|
1995 |
Ladokhin AS, Brand L. Evidence for an excited-state reaction contributing to NADH fluorescence Journal of Fluorescence. 5: 99-106. DOI: 10.1007/Bf00718787 |
0.472 |
|
1994 |
Brand L. Conformational flexibility in a staphylococcal nuclease mutant K45C from time-resolved resonance energy transfer measurements Biochemistry®. 33: 10457-10462. PMID 8068683 DOI: 10.1021/Bi00200A029 |
0.348 |
|
1994 |
Wu P, Brand L. Resonance energy transfer: Methods and applications Analytical Biochemistry. 218: 1-13. PMID 8053542 DOI: 10.1006/Abio.1994.1134 |
0.325 |
|
1994 |
Wu P, Li YK, Talalay P, Brand L. Characterization of the three tyrosine residues of delta 5-3-ketosteroid isomerase by time-resolved fluorescence and circular dichroism. Biochemistry. 33: 7415-22. PMID 8003507 DOI: 10.1021/Bi00189A048 |
0.474 |
|
1993 |
Hirshfield KM, Toptygin D, Packard BS, Brand L. Dynamic fluorescence measurements of two-state systems: Applications to calcium-chelating probes Analytical Biochemistry. 209: 209-218. PMID 8470792 DOI: 10.1006/Abio.1993.1109 |
0.368 |
|
1993 |
Rice KG, Wu P, Brand L, Lee YC. Modification of oligosaccharide antenna flexibility induced by exoglycosidase trimming. Biochemistry. 32: 7264-70. PMID 8343515 DOI: 10.1021/Bi00079A024 |
0.301 |
|
1993 |
Toptygin D, Brand L. Fluorescence decay of DPH in lipid membranes: Influence of the external refractive index Biophysical Chemistry. 48: 205-220. PMID 8298058 DOI: 10.1016/0301-4622(93)85011-6 |
0.425 |
|
1993 |
Wu PG, James E, Brand L. Compact thermally-denatured state of a staphylococcal nuclease mutant from resonance energy transfer measurements Biophysical Chemistry. 48: 123-133. PMID 8298051 DOI: 10.1016/0301-4622(93)85004-2 |
0.351 |
|
1992 |
Wu P, Brand L. Orientation factor in steady-state and time-resolved resonance energy transfer measurements Biochemistry. 31: 7939-7947. PMID 1510980 DOI: 10.1021/Bi00149A027 |
0.318 |
|
1992 |
Chauvin F, Toptygin D, Roseman S, Brand L. Time-resolved intrinsic fluorescence of Enzyme I. The monomer/dimer transition. Biophysical Chemistry. 44: 163-73. PMID 1420946 DOI: 10.1016/0301-4622(92)80049-B |
0.393 |
|
1992 |
Neyroz P, Franzoni L, Spisni A, Masotti L, Brand L. The chemical synthesis of N-[1-(2-naphthol)]-phosphatidylethanolamine, a fluorescent phospholipid for excited-state proton transfer studies Chemistry and Physics of Lipids. 61: 255-263. PMID 1326418 DOI: 10.1016/0009-3084(92)90105-X |
0.454 |
|
1992 |
Toptygin D, Svobodova J, Konopasek I, Brand L. Fluorescence decay and depolarization in membranes The Journal of Chemical Physics. 96: 7919-7930. DOI: 10.1063/1.462344 |
0.375 |
|
1991 |
Rice KG, Wu RG, Brand L, Lee YC. Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer. Biochemistry. 30: 6646-55. PMID 2065052 DOI: 10.1021/Bi00241A003 |
0.324 |
|
1991 |
Wu PG, Rice KG, Brand L, Lee YC. Differential flexibilities in three branches of an N-linked triantennary glycopeptide. Proceedings of the National Academy of Sciences of the United States of America. 88: 9355-9. PMID 1924399 DOI: 10.1073/Pnas.88.20.9355 |
0.381 |
|
1987 |
Han MK, Walbridge DG, Knutson JR, Brand L, Roseman S. Nanosecond time-resolved fluorescence kinetic studies of the 5,5'-dithiobis(2-nitrobenzoic acid) reaction with enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system. Analytical Biochemistry. 161: 479-86. PMID 3578806 DOI: 10.1016/0003-2697(87)90477-5 |
0.454 |
|
1987 |
Walbridge DG, Knutson JR, Brand L. Nanosecond time-resolved fluorescence measurements during protein denaturation. Analytical Biochemistry. 161: 467-78. PMID 3578805 DOI: 10.1016/0003-2697(87)90476-3 |
0.454 |
|
1987 |
Neyroz P, Brand L, Roseman S. Sugar transport by the bacterial phosphotransferase system. The intrinsic fluorescence of enzyme I. The Journal of Biological Chemistry. 262: 15900-7. PMID 3316210 |
0.318 |
|
1986 |
Davenport L, Knutson JR, Brand L. Excited-state proton transfer of equilenin and dihydroequilenin: interaction with bilayer vesicles. Biochemistry. 25: 1186-95. PMID 3964666 DOI: 10.1021/Bi00353A037 |
0.44 |
|
1986 |
Laws WR, Alexander Ross JB, Wyssbrod HR, Beechem JM, Brand L, Sutherland JC. Time-resolved fluorescence and1H NMR studies of tyrosine and tyrosine analogues: Correlation of NMR-determined rotamer populations and fluorescence kinetics Biochemistry. 25: 599-607. PMID 3955016 DOI: 10.1021/Bi00351A013 |
0.457 |
|
1986 |
Beechem JM, Brand L. Global analysis of fluorescence decay: applications to some unusual experimental and theoretical studies Photochemistry and Photobiology. 44: 323-329. PMID 3786453 DOI: 10.1111/J.1751-1097.1986.Tb04671.X |
0.431 |
|
1986 |
Davenport L, Knutson JR, Brand L. Anisotropy decay associated fluorescence spectra and analysis of rotational heterogeneity. 2. 1,6-Diphenyl-1,3,5-hexatriene in lipid bilayers. Biochemistry. 25: 1811-6. PMID 3754764 DOI: 10.1021/Bi00355A054 |
0.368 |
|
1986 |
Ameloot M, Beechem JM, Brand L. Simultaneous analysis of multiple fluorescence decay curves by Laplace transforms. Deconvolution with reference or excitation profiles Biophysical Chemistry. 23: 155-171. PMID 3708094 DOI: 10.1016/0301-4622(86)85001-3 |
0.44 |
|
1986 |
Knutson JR, Davenport L, Brand L. Anisotropy decay associated fluorescence spectra and analysis of rotational heterogeneity. 1. Theory and applications. Biochemistry. 25: 1805-10. PMID 3707911 DOI: 10.1021/Bi00355A053 |
0.424 |
|
1986 |
Davenport L, Knutson JR, Brand L. Studies of membrane heterogeneity using fluorescence associative techniques. Faraday Discussions of the Chemical Society. 81-94. PMID 3582620 DOI: 10.1039/Dc9868100081 |
0.468 |
|
1986 |
Ameloot M, Beechem JM, Brand L. Compartmental modeling of excited-state reactions: identifiabilityof the rate constants from fluorecences decay surfaces Chemical Physics Letters. 129: 211-219. DOI: 10.1016/0009-2614(86)80199-3 |
0.321 |
|
1985 |
Beechem JM, Brand L. Time-resolved fluorescence of proteins Annual Review of Biochemistry. 43-71. PMID 3896124 DOI: 10.1146/Annurev.Bi.54.070185.000355 |
0.43 |
|
1985 |
Beechem JM, Ameloot M, Brand L. GLOBAL AND TARGET ANALYSIS OF COMPLEX DECAY PHENOMENA Analytical Instrumentation. 14: 379-402. DOI: 10.1080/10739148508543585 |
0.354 |
|
1985 |
Beechem JM, Ameloot M, Brand L. Global analysis of fluorescence decay surfaces: excited-state reactions Chemical Physics Letters. 120: 466-472. DOI: 10.1016/0009-2614(85)85642-6 |
0.418 |
|
1984 |
NEYROZ P, DAVENPORT L, BRAND L. A Fluorescent Phospholipid Derivative for Excited‐State Proton Transfer Studies at the Membrane Surface Annals of the New York Academy of Sciences. 435: 564-565. DOI: 10.1111/J.1749-6632.1984.Tb13884.X |
0.371 |
|
1983 |
Knutson JR, Beechem JM, Brand L. Simultaneous analysis of multiple fluorescence decay curves: A global approach Chemical Physics Letters. 102: 501-507. DOI: 10.1016/0009-2614(83)87454-5 |
0.405 |
|
1982 |
Knutson JR, Walbridge DG, Brand L. Decay-associated fluorescence spectra and the heterogeneous emission of alcohol dehydrogenase. Biochemistry. 21: 4671-9. PMID 6753925 DOI: 10.1021/Bi00262A024 |
0.487 |
|
1981 |
Ross JB, Schmidt CJ, Brand L. Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry. 20: 4369-77. PMID 7025898 DOI: 10.1021/bi00518a021 |
0.37 |
|
1981 |
Cavalieri RL, Beck JC, Brand L, Mitzner W, London WT, Johnson JW. The relationship of amniotic fluid fluorescence polarization to neonatal lung function. American Journal of Obstetrics and Gynecology. 141: 652-7. PMID 6895576 DOI: 10.1016/S0002-9378(15)33306-8 |
0.332 |
|
1981 |
Ross JBA, Rousslang KW, Brand L. Time-resolved fluorescence and anisotropy decay of the tryptophan in adrenocorticotropin-(1-24) Biochemistry. 20: 4361-4369. PMID 6269589 DOI: 10.1021/bi00518a020 |
0.365 |
|
1981 |
Brand L, Ross JB, Laws WR. Nanosecond fluorometry and the luminescence of biological macromolecules. Annals of the New York Academy of Sciences. 366: 197-207. PMID 6266315 DOI: 10.1111/J.1749-6632.1981.Tb20754.X |
0.303 |
|
1981 |
Barkley MD, Kowalczyk AA, Brand L. Fluorescence decay studies of anisotropic rotations of small molecules The Journal of Chemical Physics. 75: 3581-3593. DOI: 10.1002/Chin.198152044 |
0.402 |
|
1979 |
Badea MG, DeToma RP, Brand L. Nanosecond relaxation processes in liposomes. Biophysical Journal. 24: 197-212. PMID 708822 DOI: 10.1016/S0006-3495(78)85356-9 |
0.49 |
|
1979 |
Badea MG, Brand L. Time-resolved fluorescence measurements. Methods in Enzymology. 61: 378-425. PMID 481233 DOI: 10.1016/0076-6879(79)61019-4 |
0.445 |
|
1979 |
Laws WR, Posner GH, Brand L. A covalent fluorescence probe based on excited-state proton transfer. Archives of Biochemistry and Biophysics. 193: 88-100. PMID 453860 DOI: 10.1016/0003-9861(79)90011-0 |
0.493 |
|
1979 |
Laws WR, Brand L. Analysis of two-state excited-state reactions. The fluorescence decay of 2-naphthol The Journal of Physical Chemistry. 83: 795-802. DOI: 10.1021/J100470A007 |
0.42 |
|
1979 |
LAWS WR, BRAND L. ChemInform Abstract: ANALYSIS OF TWO-STATE EXCITED-STATE REACTIONS. THE FLUORESCENCE DECAY OF 2-NAPHTHOL Chemischer Informationsdienst. 10. DOI: 10.1002/chin.197930047 |
0.311 |
|
1978 |
Easter JH, Detoma RP, Brand L. Fluorescence measurements of environmental relaxation at the lipid-water interface region of bilayer membranes. Biochimica Et Biophysica Acta. 508: 27-38. PMID 629967 DOI: 10.1016/0005-2736(78)90186-4 |
0.429 |
|
1978 |
Gafni A, Brand L. The interaction of liver alcohol dehydrogenase with NADH as studied by differential protein denaturation. Biochimica Et Biophysica Acta. 537: 446-55. PMID 215220 DOI: 10.1016/0005-2795(78)90529-9 |
0.516 |
|
1978 |
Gafni A, Brand L. Excited state proton transfer reactions of acridine studied by nanosecond fluorometry Chemical Physics Letters. 58: 346-350. DOI: 10.1016/0009-2614(78)85050-7 |
0.499 |
|
1978 |
Easter JH, Detoma RP, Brand L. Fluorescence measurements of environmental relaxation at the lipid-water interface region of bilayer membranes Bba - Biomembranes. 508: 27-38. DOI: 10.1016/0005-2736(78)90186-4 |
0.32 |
|
1977 |
Gafni A, DeToma RP, Manrow RE, Brand L. Nanosecond decay studies of a fluorescence probe bound to apomyoglobin. Biophysical Journal. 17: 155-68. PMID 836933 DOI: 10.1016/S0006-3495(77)85633-6 |
0.628 |
|
1977 |
Detoma RP, Brand L. Excited state solvation dynamics of 2-anilinonaphthalene Chemical Physics Letters. 47: 231-236. DOI: 10.1016/0009-2614(77)80007-9 |
0.353 |
|
1976 |
De Toma RP, Easter JH, Brand L. Dynamic interactions of fluorescence probes with the solvent environment. Journal of the American Chemical Society. 98: 5001-7. PMID 950424 DOI: 10.1002/Chin.197645037 |
0.397 |
|
1976 |
Easter JH, DeToma RP, Brand L. Nanosecond time-resolved emission spectroscopy of a fluorescence probe adsorbed to L-alpha-egg lecithin vesicles. Biophysical Journal. 16: 571-83. PMID 945086 DOI: 10.1016/S0006-3495(76)85712-8 |
0.469 |
|
1976 |
Gafni A, Brand L. Fluorescence decay studies of reduced nicotinamide adenine dinucleotide in solution and bound to liver alcohol dehydrogenase. Biochemistry. 15: 3165-71. PMID 8086 DOI: 10.1021/Bi00660A001 |
0.63 |
|
1976 |
Gafni A, Modlin RL, Brand L. Nanosecond fluorescence decay studies of 2-hydroxy-1-naphthaleneacetic acid. Excited-state proton transfer The Journal of Physical Chemistry. 80: 898-904. DOI: 10.1021/J100549A027 |
0.618 |
|
1976 |
GAFNI A, MODLIN RL, BRAND L. ChemInform Abstract: NANOSECOND FLUORESCENCE DECAY STUDIES OF 2-HYDROXY-1-NAPHTHALENEACETIC ACID. EXCITED-STATE PROTON TRANSFER Chemischer Informationsdienst. 7: no-no. DOI: 10.1002/chin.197626038 |
0.577 |
|
1975 |
Gafni A, Modlin RL, Brand L. Analysis of fluorescence decay curves by means of the Laplace transformation. Biophysical Journal. 15: 263-80. PMID 1122338 DOI: 10.1016/S0006-3495(75)85817-6 |
0.551 |
|
1973 |
Easter JH, Brand L. Nanosecond time-resolved emission spectroscopy of a fluorescence probe bound to L- -egg lecithin vesicles. Biochemical and Biophysical Research Communications. 52: 1086-92. PMID 4736321 DOI: 10.1016/0006-291X(73)91049-8 |
0.49 |
|
1973 |
Bowie LJ, Irwin R, Loken M, De Luca M, Brand L. Excited-state proton transfer and the mechanism of action of firefly luciferase. Biochemistry. 12: 1852-7. PMID 4704471 DOI: 10.1021/Bi00734A002 |
0.353 |
|
1973 |
Brand L, Gohlke JR. Fluorescence probes for structure. Annual Review of Biochemistry. 41: 843-68. PMID 4563443 DOI: 10.1146/annurev.bi.41.070172.004211 |
0.304 |
|
1972 |
Loken MR, Hayes JW, Gohlke JR, Brand L. Excited-state proton transfer as a biological probe. Determination of rate constants by means of nanosecond fluorometry Biochemistry. 11: 4779-4786. PMID 4676272 DOI: 10.1021/Bi00775A022 |
0.397 |
|
1972 |
Heitz JR, Brand L. Fluorescence changes associated with denaturation of alcohol dehydrogenase. Archives of Biochemistry and Biophysics. 144: 286-91. PMID 4330126 DOI: 10.1016/0003-9861(71)90480-2 |
0.439 |
|
1971 |
Seliskar CJ, Brand L. Electronic spectra of 2-aminonaphthalene-6-sulfonate and related molecules. II. Effects of solvent medium on the absorption and fluorescence spectra Journal of the American Chemical Society. 93: 5414-5420. DOI: 10.1021/Ja00750A017 |
0.608 |
|
1971 |
Seliskar CJ, Brand L. Electronic spectra of 2-aminonaphthalene-6-sulfonate and related molecules. I. General properties and excited-state reactions Journal of the American Chemical Society. 93: 5405-5414. DOI: 10.1021/Ja00750A016 |
0.583 |
|
1971 |
SELISKAR CJ, BRAND L. ChemInform Abstract: ELEKTRONENSPEKTREN VON 2-AMINO-NAPHTHALIN-6-SULFONAT UND VERWANDTEN MOLEKUELEN 1. MITT. ALLGEMEINE EIGENSCHAFTEN UND RK. IM ANGEREGTEN ZUSTAND 2. MITT. EINFLUSS DES LOESUNGSMITTELS AUF DIE ABSORPTIONS- UND FLUORESZENZSPEKTREN Chemischer Informationsdienst. Organische Chemie. 2. DOI: 10.1002/Chin.197152107 |
0.528 |
|
1970 |
Witholt B, Brand L. Multioscillator fluorescence depolarization. Anisotropy of dye binding. Biochemistry. 9: 1948-58. PMID 5462516 DOI: 10.1021/Bi00811A015 |
0.407 |
|
1970 |
Conrad RH, Heitz JR, Brand L. Characterization of a fluorescent complex between auramine O and horse liver alcohol dehydrogenase. Biochemistry. 9: 1540-6. PMID 4314230 DOI: 10.1021/Bi00809A010 |
0.308 |
|
1970 |
Brand L. Fluorescence Assay in Biology and Medicine. Vol. 2. Sidney Udenfriend. With a contribution by J. D. Winefordner, P. A. St. John, and W. J. McCarthy. Academic Press, New York, 1969. xii, 660 pp., illus. $19.50. Molecular Biology series Science. 170: 1393-1393. DOI: 10.1126/Science.170.3965.1393 |
0.328 |
|
1968 |
Turner DC, Brand L. Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates. Biochemistry. 7: 3381-90. PMID 5693059 DOI: 10.1021/Bi00850A011 |
0.348 |
|
1968 |
Witholt B, Brand L. Versatile Spectrophotofluorometer‐Polarization Fluorometer Review of Scientific Instruments. 39: 1271-1278. DOI: 10.1063/1.1683649 |
0.341 |
|
1967 |
Edelhoch H, Brand L, Wilchek M. Fluorescence studies with tryptophyl peptides. Biochemistry. 6: 547-59. PMID 6047638 DOI: 10.1021/Bi00854A024 |
0.343 |
|
1967 |
Brand L, Gohlke JR, Rao DS. Evidence for binding of rose bengal and anilinonaphthalenesulfonates at the active site regions of liver alcohol dehydrogenase Biochemistry. 6: 3510-3518. PMID 5624041 DOI: 10.1021/Bi00863A024 |
0.304 |
|
1967 |
Brand L, Witholt B. [87] Fluorescence measurements Methods in Enzymology. 11: 776-856. DOI: 10.1016/S0076-6879(67)11091-4 |
0.46 |
|
1964 |
BRAND L, SHALTIEL S. MODIFICATION OF HISTIDINE RESIDUES LEADING TO THE APPEARANCE OF VISIBLE FLUORESCENCE. Biochimica Et Biophysica Acta. 88: 338-51. PMID 14249842 DOI: 10.1016/0926-6577(64)90189-5 |
0.339 |
|
1962 |
BRAND L, EVERSE J, KAPLAN NO. Structural characteristics of dehydrogenases. Biochemistry. 1: 423-34. PMID 13872460 DOI: 10.1021/Bi00909A009 |
0.447 |
|
1960 |
BRAND L, DAHL C, MAHLER HR. Biochemical studies of the developing avian embryo. 4. Some respiratory pigments. The Journal of Biological Chemistry. 235: 2456-67. PMID 13803842 |
0.403 |
|
1959 |
BRAND L, MAHLER HR. Biochemical studies of the developing avian embryo. III. The oxidation of reduced pyridine nucleotide. The Journal of Biological Chemistry. 234: 1615-24. PMID 13654427 |
0.406 |
|
1958 |
MAHLER HR, WITTENBERGER MH, BRAND L. Biochemical studies of the developing avian embryo. II. Enzymes of the citric acid cycle. The Journal of Biological Chemistry. 233: 770-82. PMID 13587491 |
0.426 |
|
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