| Year |
Citation |
Score |
| 2019 |
Vanderkooi JM, Chance B. Temperature sensitivity of fluorescence probes in the presence of model membranes and mitochondria. Febs Letters. 22: 23-26. PMID 11946551 DOI: 10.1016/0014-5793(72)80209-6 |
0.31 |
|
| 2017 |
Zelent B, Bialas C, Gryczynski I, Chen P, Chib R, Lewerissa K, Corradini MG, Ludescher RD, Vanderkooi JM, Matschinsky FM. Tryptophan Fluorescence Yields and Lifetimes as a Probe of Conformational Changes in Human Glucokinase. Journal of Fluorescence. PMID 28432632 DOI: 10.1007/S10895-017-2099-X |
0.389 |
|
| 2010 |
Zelent B, Sharp KA, Vanderkooi JM. Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH. Biochimica Et Biophysica Acta. 1804: 1508-15. PMID 20298816 DOI: 10.1016/J.Bbapap.2010.03.003 |
0.377 |
|
| 2010 |
Sharp KA, Vanderkooi JM. Water in the half shell: structure of water, focusing on angular structure and solvation. Accounts of Chemical Research. 43: 231-9. PMID 19845327 DOI: 10.1021/Ar900154J |
0.306 |
|
| 2009 |
Vorobyev DY, Kuo CH, Chen JX, Kuroda DG, Scott JN, Vanderkooi JM, Hochstrasser RM. Ultrafast vibrational spectroscopy of a degenerate mode of guanidinium chloride. The Journal of Physical Chemistry. B. 113: 15382-91. PMID 19905022 DOI: 10.1021/Jp9069256 |
0.305 |
|
| 2009 |
Zelent B, Bryan MA, Sharp KA, Vanderkooi JM. Influence of surface groups of proteins on water studied by freezing/thawing hysteresis and infrared spectroscopy. Biophysical Chemistry. 141: 222-30. PMID 19251353 DOI: 10.1016/J.Bpc.2009.02.002 |
0.322 |
|
| 2009 |
Zelent B, Vanderkooi JM, Nucci NV, Gryczynski I, Gryczynski Z. Phosphate assisted proton transfer in water and sugar glasses: a study using fluorescence of pyrene-1-carboxylate and IR spectroscopy. Journal of Fluorescence. 19: 21-31. PMID 18496739 DOI: 10.1007/S10895-008-0375-5 |
0.358 |
|
| 2008 |
Scott JN, Nucci NV, Vanderkooi JM. Changes in water structure induced by the guanidinium cation and implications for protein denaturation. The Journal of Physical Chemistry. A. 112: 10939-48. PMID 18839935 DOI: 10.1021/Jp8058239 |
0.32 |
|
| 2008 |
Pentelute BL, Gates ZP, Dashnau JL, Vanderkooi JM, Kent SB. Mirror image forms of snow flea antifreeze protein prepared by total chemical synthesis have identical antifreeze activities. Journal of the American Chemical Society. 130: 9702-7. PMID 18598026 DOI: 10.1021/Ja801352J |
0.312 |
|
| 2008 |
Zelent B, Odili S, Buettger C, Shiota C, Grimsby J, Taub R, Magnuson MA, Vanderkooi JM, Matschinsky FM. Sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence. The Biochemical Journal. 413: 269-80. PMID 18370929 DOI: 10.1042/Bj20071718 |
0.308 |
|
| 2008 |
Nucci NV, Scott JN, Vanderkooi JM. Coupling of complex aromatic ring vibrations to solvent through hydrogen bonds: effect of varied on-ring and off-ring hydrogen-bonding substitutions. The Journal of Physical Chemistry. B. 112: 4022-35. PMID 18331017 DOI: 10.1021/Jp0758770 |
0.305 |
|
| 2008 |
Nucci NV, Zelent B, Vanderkooi JM. Pyrene-1-carboxylate in water and glycerol solutions: origin of the change of pK upon excitation. Journal of Fluorescence. 18: 41-9. PMID 17846872 DOI: 10.1007/S10895-007-0233-X |
0.375 |
|
| 2007 |
Ponkratov VV, Wiedersich J, Friedrich J, Vanderkooi JM. Experiments with proteins at low temperature: What do we learn on properties in their functional state? Journal of Chemical Physics. 126: 165104-165104. PMID 17477636 DOI: 10.1063/1.2723731 |
0.35 |
|
| 2007 |
Zelent B, Troxler T, Vanderkooi JM. Temperature dependence for fluorescence of beta-NADH in glycerol/water solution and in trehalose/sucrose glass. Journal of Fluorescence. 17: 37-42. PMID 17171438 DOI: 10.1007/S10895-006-0146-0 |
0.349 |
|
| 2006 |
Kaposi AD, Vanderkooi JM, Stavrov SS. Infrared absorption study of the heme pocket dynamics of carbonmonoxyheme proteins. Biophysical Journal. 91: 4191-200. PMID 16980362 DOI: 10.1529/Biophysj.105.068254 |
0.368 |
|
| 2006 |
Zelent B, Vanderkooi JM, Coleman RG, Gryczynski I, Gryczynski Z. Protonation of excited state pyrene-1-carboxylate by phosphate and organic acids in aqueous solution studied by fluorescence spectroscopy. Biophysical Journal. 91: 3864-71. PMID 16920831 DOI: 10.1529/Biophysj.106.088740 |
0.352 |
|
| 2006 |
Khajehpour M, Dashnau JL, Vanderkooi JM. Infrared spectroscopy used to evaluate glycosylation of proteins. Analytical Biochemistry. 348: 40-8. PMID 16298329 DOI: 10.1016/J.Ab.2005.10.009 |
0.373 |
|
| 2006 |
Ponkratov VV, Friedrich J, Vanderkooi JM. Hole burning experiments with proteins: Relaxations, fluctuations and glass-like features Journal of Non-Crystalline Solids. 352: 4379-4386. DOI: 10.1016/J.Jnoncrysol.2006.01.114 |
0.324 |
|
| 2005 |
Nucci NV, Vanderkooi JM. Temperature dependence of hydrogen bonding and freezing behavior of water in reverse micelles. The Journal of Physical Chemistry. B. 109: 18301-9. PMID 16853355 DOI: 10.1021/Jp051068+ |
0.307 |
|
| 2005 |
Vanderkooi JM, Dashnau JL, Zelent B. Temperature excursion infrared (TEIR) spectroscopy used to study hydrogen bonding between water and biomolecules. Biochimica Et Biophysica Acta. 1749: 214-33. PMID 15927875 DOI: 10.1016/J.Bbapap.2005.03.008 |
0.36 |
|
| 2005 |
Dashnau JL, Zelent B, Vanderkooi JM. Tryptophan interactions with glycerol/water and trehalose/sucrose cryosolvents: infrared and fluorescence spectroscopy and ab initio calculations. Biophysical Chemistry. 114: 71-83. PMID 15792863 DOI: 10.1016/J.Bpc.2004.10.003 |
0.42 |
|
| 2005 |
Chen H, Chung NN, Lemieux C, Zelent B, Vanderkooi JM, Gryczynski I, Wilkes BC, Schiller PW. [Aladan3]TIPP: a fluorescent delta-opioid antagonist with high delta-receptor binding affinity and delta selectivity. Biopolymers. 80: 325-31. PMID 15614807 DOI: 10.1002/Bip.20200 |
0.346 |
|
| 2005 |
Mei E, Gao F, Vinogradov S, Vanderkooi JM, Hochstrasser RM. Phosphorescence of individual horseradish peroxidases proteins having a modified heme group Chemical Physics Letters. 401: 30-34. DOI: 10.1016/J.Cplett.2004.10.133 |
0.324 |
|
| 2004 |
Nibbs J, Vinogradov SA, Vanderkooi JM, Zelent B. Flexibility in proteins: tuning the sensitivity to O2 diffusion by varying the lifetime of a phosphorescent sensor in horseradish peroxidase. Photochemistry and Photobiology. 80: 36-40. PMID 15339214 DOI: 10.1562/2004-01-17-Ra-046.1 |
0.334 |
|
| 2004 |
Khajehpour M, Troxler T, Vanderkooi JM. Probing the active site of trypsin with rose bengal: insights into the photodynamic inactivation of the enzyme. Photochemistry and Photobiology. 80: 359-65. PMID 15244504 DOI: 10.1111/J.1751-1097.2004.Tb00096.X |
0.327 |
|
| 2004 |
Khajehpour M, Troxler T, Nanda V, Vanderkooi JM. Melittin as model system for probing interactions between proteins and cyclodextrins. Proteins. 55: 275-87. PMID 15048821 DOI: 10.1002/Prot.20036 |
0.35 |
|
| 2004 |
Lesch H, Schlichter J, Friedrich J, Vanderkooi JM. Molecular probes: What is the range of their interaction with the environment? Biophysical Journal. 86: 467-472. PMID 14695290 DOI: 10.1016/S0006-3495(04)74124-7 |
0.342 |
|
| 2004 |
Ponkratov VV, Friedrich J, Vanderkooi JM, Burin AL, Berlin YA. Physics of proteins at low temperature Journal of Low Temperature Physics. 137: 289-317. DOI: 10.1023/B:Jolt.0000049058.81275.72 |
0.349 |
|
| 2004 |
Zelent B, Kaposi AD, Nucci NV, Sharp KA, Dalosto SD, Wright WW, Vanderkooi JM. Water channel of horseradish peroxidase studied by the charge-transfer absorption band of ferric heme Journal of Physical Chemistry B. 108: 10317-10324. DOI: 10.1021/Jp037664Q |
0.352 |
|
| 2004 |
Ponkratov VV, Friedrich J, Markovic D, Scheer H, Vanderkooi JM. Spectral Diffusion Experiment with a Denatured Protein Journal of Physical Chemistry B. 108: 1109-1114. DOI: 10.1021/Jp0359135 |
0.304 |
|
| 2003 |
Khajehpour M, Rietveld I, Vinogradov S, Prabhu NV, Sharp KA, Vanderkooi JM. Accessibility of oxygen with respect to the heme pocket in horseradish peroxidase. Proteins. 53: 656-66. PMID 14579357 DOI: 10.1002/Prot.10475 |
0.341 |
|
| 2003 |
Kaposi AD, Prabhu NV, Dalosto SD, Sharp KA, Wright WW, Stavrov SS, Vanderkooi JM. Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations. Biophysical Chemistry. 106: 1-14. PMID 14516907 DOI: 10.1016/S0301-4622(03)00122-4 |
0.37 |
|
| 2003 |
Wright WW, Guffanti GT, Vanderkooi JM. Protein in sugar films and in glycerol/water as examined by infrared spectroscopy and by the fluorescence and phosphorescence of tryptophan. Biophysical Journal. 85: 1980-95. PMID 12944311 DOI: 10.1016/S0006-3495(03)74626-8 |
0.4 |
|
| 2003 |
Khajehpour M, Troxler T, Vanderkooi JM. Effect of protein dynamics upon reactions that occur in the heme pocket of horseradish peroxidase. Biochemistry. 42: 2672-9. PMID 12614162 DOI: 10.1021/Bi020325N |
0.343 |
|
| 2003 |
Mei E, Tang J, Vanderkooi JM, Hochstrasser RM. Motions of single molecules and proteins in trehalose glass. Journal of the American Chemical Society. 125: 2730-5. PMID 12603162 DOI: 10.1021/Ja021197T |
0.358 |
|
| 2003 |
Walsh ST, Cheng RP, Wright WW, Alonso DO, Daggett V, Vanderkooi JM, DeGrado WF. The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR. Protein Science : a Publication of the Protein Society. 12: 520-31. PMID 12592022 DOI: 10.1110/Ps.0223003 |
0.34 |
|
| 2003 |
Dalosto SD, Prabhu NV, Vanderkooi JM, Sharp KA. A density functional theory study of conformers in the ferrous CO complex of horseradish peroxidase with distinct Fe-C-O configurations Journal of Physical Chemistry B. 107: 1884-1892. DOI: 10.1021/Jp022018X |
0.312 |
|
| 2002 |
Wright WW, Carlos Baez J, Vanderkooi JM. Mixed trehalose/sucrose glasses used for protein incorporation as studied by infrared and optical spectroscopy. Analytical Biochemistry. 307: 167-72. PMID 12137794 DOI: 10.1016/S0003-2697(02)00034-9 |
0.375 |
|
| 2002 |
Stavrov SS, Wright WW, Vanderkooi JM, Fidy J, Kaposi AD. Optical and IR absorption as probe of dynamics of heme proteins. Biopolymers. 67: 255-8. PMID 12012441 DOI: 10.1002/Bip.10103 |
0.36 |
|
| 2002 |
Lesch H, Stadlbauer H, Friedrich J, Vanderkooi JM. Stability diagram and unfolding of a modified cytochrome c: what happens in the transformation regime? Biophysical Journal. 82: 1644-53. PMID 11867476 DOI: 10.1016/S0006-3495(02)75515-X |
0.401 |
|
| 2002 |
Tronin A, Edwards AM, Wright WW, Vanderkooi JM, Blasie JK. Orientation distributions for cytochrome c on polar and nonpolar interfaces by total internal reflection fluorescence. Biophysical Journal. 82: 996-1003. PMID 11806939 DOI: 10.1016/S0006-3495(02)75459-3 |
0.318 |
|
| 2002 |
Kaposi AD, Vanderkooi JM, Wright WW, Fidy J, Stavrov SS. Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase. Biophysical Journal. 81: 3472-82. PMID 11721008 DOI: 10.1016/S0006-3495(01)75978-4 |
0.342 |
|
| 2002 |
Ponkratov VV, Friedrich J, Vanderkooi JM. Solvent effects on conformational dynamics of proteins: Cytochrome c in a dried trehalose film Journal of Chemical Physics. 117: 4594-4601. DOI: 10.1063/1.1498459 |
0.337 |
|
| 2002 |
Prabhu NV, Dalosto SD, Sharp KA, Wright WW, Vanderkooi JM. Optical spectra of Fe(II) cytochrome c interpreted using molecular dynamics simulations and quantum mechanical calculations Journal of Physical Chemistry B. 106: 5561-5571. DOI: 10.1021/Jp014208Y |
0.407 |
|
| 2001 |
Friedrich J, Gafert J, Zollfrank J, Vanderkooi J, Fidy J. Spectral hole burning and selection of conformational substates in chromoproteins. Proceedings of the National Academy of Sciences of the United States of America. 91: 1029-33. PMID 11607456 DOI: 10.1073/Pnas.91.3.1029 |
0.303 |
|
| 2001 |
Kaposi AD, Wright WW, Fidy J, Stavrov SS, Vanderkooi JM, Rasnik I. Carbonmonoxy horseradish peroxidase as a function of pH and substrate: Influence of local electric fields on the optical and infrared spectra Biochemistry. 40: 3483-3491. PMID 11297414 DOI: 10.1021/Bi002784Z |
0.317 |
|
| 2001 |
Rasnik I, Sharp KA, Fee JA, Vanderkooi JM. Spectral analysis of cytochrome c: Effect of heme conformation, axial ligand, peripheral substituents, and local electric fields Journal of Physical Chemistry B. 105: 282-286. DOI: 10.1021/Jp002656K |
0.338 |
|
| 2000 |
Zhang H, Kolibal S, Vanderkooi JM, Cohen SA, Kallen RG. A carboxy-terminal α-helical segment in the rat skeletal muscle voltage-dependent Na+ channel is responsible for its interaction with the amino-terminus Biochimica Et Biophysica Acta. 1467: 406-418. PMID 11030598 DOI: 10.1016/S0005-2736(00)00238-8 |
0.301 |
|
| 2000 |
Kaposi AD, Fidy J, Manas ES, Vanderkooi JM, Wright WW. Horseradish peroxidase monitored by infrared spectroscopy: effect of temperature, substrate and calcium. Biochimica Et Biophysica Acta. 1435: 41-50. PMID 10561536 DOI: 10.1016/S0167-4838(99)00206-X |
0.353 |
|
| 2000 |
Manas ES, Wright WW, Sharp KA, Friedrich J, Vanderkooi JM. The influence of protein environment on the low temperature electronic spectroscopy of Zn-substituted cytochrome Journal of Physical Chemistry B. 104: 6932-6941. DOI: 10.1021/Jp0005975 |
0.371 |
|
| 2000 |
Manas ES, Getahun Z, Wright WW, DeGrado aWF, Vanderkooi JM. Infrared Spectra of Amide Groups in α-Helical Proteins: Evidence for Hydrogen Bonding between Helices and Water Journal of the American Chemical Society. 122: 9883-9890. DOI: 10.1021/Ja001782Z |
0.375 |
|
| 1999 |
Laberge M, Köhler M, Vanderkooi JM, Friedrich J. Sampling field heterogeneity at the heme of c-type cytochromes by spectral hole burning spectroscopy and electrostatic calculations. Biophysical Journal. 77: 3293-3304. PMID 10585951 DOI: 10.1016/S0006-3495(99)77160-2 |
0.332 |
|
| 1999 |
Zentko S, Scarrow RC, Wright WW, Vanderkooi JM. Protonation of porphyrin in iron-free cytochrome c: spectral properties of monocation free base porphyrin, a charge analogue of ferric heme. Biospectroscopy. 5: 141-50. PMID 10380081 DOI: 10.1002/(Sici)1520-6343(1999)5:3<141::Aid-Bspy4>3.0.Co;2-J |
0.369 |
|
| 1999 |
Ma JG, Vanderkooi JM, Zhang J, Jia SL, Shelnutt JA. Resonance Raman investigation of nickel microperoxidase-11 Biochemistry. 38: 2787-2795. PMID 10052950 DOI: 10.1021/Bi982332A |
0.35 |
|
| 1999 |
Schlichter J, Fritsch K-, Friedrich J, Vanderkooi JM. Conformational dynamics of a low temperature protein: Free base cytochrome-c Journal of Chemical Physics. 110: 3229-3234. DOI: 10.1063/1.477845 |
0.329 |
|
| 1999 |
Stewart CA, Vanderkooi JM. Tryptophan and Proteins Can Be Entrapped in UV Transmitting Glass Journal of Fluorescence. 9: 89-92. DOI: 10.1023/A:1020516630676 |
0.378 |
|
| 1998 |
Fidy J, Laberge M, Kaposi AD, Vanderkooi JM. Fluorescence line narrowing applied to the study of proteins. Biochimica Et Biophysica Acta. 1386: 331-51. PMID 9733992 DOI: 10.1016/S0167-4838(98)00101-0 |
0.403 |
|
| 1998 |
Angiolillo PJ, Vanderkooi JM. The Photoexcited Triplet State as a Probe of Chromophore-Protein Interaction in Myoglobin Biophysical Journal. 75: 1491-1502. PMID 9726951 DOI: 10.1016/S0006-3495(98)74068-8 |
0.354 |
|
| 1998 |
Laberge M, Vreugdenhil AJ, Vanderkooi JM, Butler IS. Microperoxidase-11: molecular dynamics and Q-band excited resonance Raman of the oxidized, reduced and carbonyl forms. Journal of Biomolecular Structure & Dynamics. 15: 1039-50. PMID 9669550 DOI: 10.1080/07391102.1998.10508999 |
0.313 |
|
| 1998 |
Laberge M, Sharp KA, Vanderkooi JM. Effect of charge interactions on the carboxylate vibrational stretching frequency in c-type cytochromes investigated by continuum electrostatic calculations and FTIR spectroscopy Biophysical Chemistry. 71: 9-20. PMID 9591357 DOI: 10.1016/S0301-4622(97)00127-0 |
0.363 |
|
| 1998 |
Sudhakar K, Laberge M, Tsuneshige aA, Vanderkooi JM. Zinc-substituted hemoglobins: alpha- and beta-chain differences monitored by high-resolution emission spectroscopy. Biochemistry. 37: 7177-7184. PMID 9585529 DOI: 10.1021/Bi972786S |
0.344 |
|
| 1998 |
Ma JG, Laberge M, Song XZ, Jentzen W, Jia SL, Zhang J, Vanderkooi JM, Shelnutt JA. Protein-induced changes in nonplanarity of the porphyrin in nickel cytochrome c probed by resonance Raman spectroscopy Biochemistry. 37: 5118-5128. PMID 9548742 DOI: 10.1021/Bi972375B |
0.356 |
|
| 1997 |
Wright WW, Laberge M, Vanderkooi JM. Surface of Cytochrome c: Infrared Spectroscopy of Carboxyl Groups† Biochemistry. 36: 14724-14732. PMID 9398192 DOI: 10.1021/Bi971559N |
0.346 |
|
| 1997 |
Vanderkooi JM, Angiolillo PJ, Laberge M. Fluorescence Line Narrowing Spectroscopy : A Tool For Studying Proteins Methods in Enzymology. 278: 71-94. PMID 9170310 DOI: 10.1016/S0076-6879(97)78007-8 |
0.395 |
|
| 1997 |
Laberge M, Wright WW, Sudhakar K, Liebman PA, Vanderkooi JM. Conformational effects of calcium release from parvalbumin: comparison of computational simulations with spectroscopic investigations. Biochemistry. 36: 5363-5371. PMID 9154918 DOI: 10.1021/Bi962436Q |
0.314 |
|
| 1997 |
Laberge M, Sharp KA, Vanderkooi JM. Protein electric field effects on the CO stretch frequency of carbonmonoxycytochromes c as a function of carbonyl tilting and bending investigated with a continuum electrostatic approach Journal of Physical Chemistry B. 101: 7364-7367. DOI: 10.1021/Jp9706846 |
0.32 |
|
| 1997 |
Wright WW, Vanderkooi JM. Use of IR absorption of the carboxyl group of amino acids and their metabolites to determine pKs, to study proteins, and to monitor enzymatic activity Biospectroscopy. 3: 457-467. DOI: 10.1002/(Sici)1520-6343(1997)3:6<457::Aid-Bspy5>3.0.Co;2-Y |
0.301 |
|
| 1996 |
Angiolillo PJ, Vanderkooi JM. Hydrogen atoms are produced when tryptophan within a protein is irradiated with ultraviolet light. Photochemistry and Photobiology. 64: 492-495. PMID 8806227 DOI: 10.1111/J.1751-1097.1996.Tb03095.X |
0.322 |
|
| 1996 |
Köhler M, Gafert J, Friedrich J, Vanderkooi JM, Laberge M. Stark Effect Experiments In Cytochrome C-Type Proteins : Structural Hierarchies Biophysical Journal. 71: 77-85. PMID 8804590 DOI: 10.1016/S0006-3495(96)79237-8 |
0.327 |
|
| 1995 |
Sudhakar K, Phillips CM, Owen CS, Vanderkooi JM. Dynamics of parvalbumin studied by fluorescence emission and triplet absorption spectroscopy of tryptophan. Biochemistry. 34: 1355-63. PMID 7827083 DOI: 10.1021/Bi00004A030 |
0.317 |
|
| 1995 |
Anni H, Vanderkooi JM, Mayne L. Structure of zinc-substituted cytochrome c: nuclear magnetic resonance and optical spectroscopic studies. Biochemistry. 34: 5744-5753. PMID 7727435 DOI: 10.1021/Bi00017A006 |
0.35 |
|
| 1995 |
Angiolillo PJ, Vanderkooi JM. Electron paramagnetic resonance of the excited triplet state of metal-free and metal-substituted cytochrome c Biophysical Journal. 68: 2505-2518. PMID 7647253 DOI: 10.1016/S0006-3495(95)80433-9 |
0.354 |
|
| 1995 |
Sudhakar K, Erecinska M, Vanderkooi JM. Interaction of polyamines with the Ca(2+)-binding protein parvalbumin. European Journal of Biochemistry / Febs. 230: 498-502. PMID 7607221 DOI: 10.1111/J.1432-1033.1995.0498H.X |
0.322 |
|
| 1995 |
Angiolillo PJ, Vanderkooi JM. Another Probe of Protein Substates Physics Today. 48: 80-81. DOI: 10.1063/1.2807927 |
0.32 |
|
| 1995 |
Laberge M, Vanderkooi JM. Fluorescence line narrowing study of the ground-state and first-excited-state vibrational frequencies of Sn and Zn cytochromes c Biospectroscopy. 1: 413-421. DOI: 10.1002/Bspy.350010606 |
0.34 |
|
| 1994 |
Anni H, Vanderkooi JM, Sharp KA, Yonetani T, Hopkins SC, Herenyi L, Fidy J. Electric field and conformational effects of cytochrome c and solvent on cytochrome c peroxidase studied by high-resolution fluorescence spectroscopy. Biochemistry. 33: 3475-86. PMID 8142344 DOI: 10.1021/Bi00178A003 |
0.377 |
|
| 1994 |
Vanderkooi JM, Wright WW, Erecinska M. Nitric oxide diffusion coefficients in solutions, proteins and membranes determined by phosphorescence. Biochimica Et Biophysica Acta. 1207: 249-54. PMID 8075157 DOI: 10.1016/0167-4838(94)00073-5 |
0.309 |
|
| 1994 |
Gafert J, Friedrich J, Vanderkooi JM, Fidy J. Correlation between Protein Conformation and Prosthetic Group Configuration as Tested by pH Effects: A Hole-Burning Study on Mesoporphyrin-IX-Substituted Horseradish Peroxidase The Journal of Physical Chemistry. 98: 2210-2214. DOI: 10.1021/J100059A040 |
0.31 |
|
| 1993 |
Sudhakar K, Wright WW, Williams SA, Phillips CM, Vanderkooi JM. Phenylalanine fluorescence and phosphorescence used as a probe of conformation for cod parvalbumin. Journal of Fluorescence. 3: 57-64. PMID 24234768 DOI: 10.1007/Bf00865318 |
0.388 |
|
| 1993 |
Vanderkooi JM, Kaposi A, Fidy J. Protein conformation monitored by energy-selective optical spectroscopy. Trends in Biochemical Sciences. 18: 71-6. PMID 8480364 DOI: 10.1016/0968-0004(93)90155-G |
0.397 |
|
| 1993 |
Logovinsky V, Kaposi AD, Vanderkooi JM. Native and denatured Zn cytochrome c studied by fluorescence line narrowing spectroscopy. Biochimica Et Biophysica Acta. 1161: 149-160. PMID 8381668 DOI: 10.1016/0167-4838(93)90208-9 |
0.411 |
|
| 1993 |
Sudhakar K, Phillips CM, Williams SA, Vanderkooi JM. Excited states of tryptophan in cod parvalbumin. Identification of a short-lived emitting triplet state at room temperature. Biophysical Journal. 64: 1503-11. PMID 8324187 DOI: 10.1016/S0006-3495(93)81519-4 |
0.359 |
|
| 1993 |
Kaposi AD, Fidy J, Stavrov SS, Vanderkooi JM. Optical fine-structure investigation of porphyrin-protein interactions: magnesium and metal-free myoglobin The Journal of Physical Chemistry. 97: 6319-6327. DOI: 10.1021/J100125A034 |
0.342 |
|
| 1992 |
Wright WW, Owen CS, Vanderkooi JM. Penetration of analogues of H2O and CO2 in proteins studied by room temperature phosphorescence of tryptophan. Biochemistry. 31: 6538-6544. PMID 1633165 DOI: 10.1021/Bi00143A025 |
0.358 |
|
| 1992 |
Fidy J, Vanderkooi JM, Zollfrank J, Friedrich J. More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. High resolution optical spectroscopic study. Biophysical Journal. 61: 381-91. PMID 1547326 DOI: 10.1016/S0006-3495(92)81844-1 |
0.369 |
|
| 1992 |
Kaposi AD, Vanderkooi JM. Vibronic energy map and excited state vibrational characteristics of magnesium myoglobin determined by energy-selective fluorescence. Proceedings of the National Academy of Sciences of the United States of America. 89: 11371-11375. PMID 1454822 DOI: 10.1073/Pnas.89.23.11371 |
0.356 |
|
| 1992 |
Dadak V, Vanderkooi JM, Wright WW. Electron transfer from excited tryptophan to cytochrome c: mechanism of phosphorescence quenching? Biochimica Et Biophysica Acta. 1100: 33-39. PMID 1314664 DOI: 10.1016/0005-2728(92)90123-J |
0.394 |
|
| 1991 |
Logovinsky V, Kaposi AD, Vanderkooi JM. Fluorescence line narrowed spectra of Zn and metal-free cytochrome c. Journal of Fluorescence. 1: 79-86. PMID 24242957 DOI: 10.1007/Bf00865203 |
0.368 |
|
| 1991 |
Zollfrank J, Friedrich J, Vanderkooi JM, Fidy J. Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase. Biophysical Journal. 59: 305-12. PMID 2009354 DOI: 10.1016/S0006-3495(91)82224-X |
0.375 |
|
| 1991 |
Papp S, King TE, Vanderkooi JM. Intrinsic tryptophan phosphorescence as a marker of conformation and oxygen diffusion in purified cytochrome oxidase. Febs Letters. 283: 113-6. PMID 1645290 DOI: 10.1016/0014-5793(91)80566-L |
0.343 |
|
| 1991 |
Vanderkooi JM, Calhoun DB, Owen CS, Papp S, Wright WW, Englander SW. Long-Range Electron Exchange Reactions of Excited Triplet Tryptophan in Proteins Molecular Crystals and Liquid Crystals. 194: 209-214. DOI: 10.1080/00268949108041166 |
0.365 |
|
| 1991 |
Zollfrank J, Friedrich J, Vanderkooi JM, Fidy J. Proteins and glasses: A comparative study of spectral diffusion phenomena The Journal of Chemical Physics. 95: 3134-3136. DOI: 10.1063/1.461780 |
0.319 |
|
| 1991 |
Fidy J, Holtom GR, Paul KG, Vanderkooi JM. Binding of naphthohydroxamic acid to horseradish peroxidase monitored by zinc mesoporphyrin fluorescence line narrowing The Journal of Physical Chemistry. 95: 4364-4370. DOI: 10.1021/J100164A036 |
0.424 |
|
| 1990 |
Fidy J, Paul KG, Vanderkooi JM. Differences in the binding of aromatic substrates to horseradish peroxidase revealed by fluorescence line narrowing. Biochemistry. 28: 7531-41. PMID 2611198 DOI: 10.1021/Bi00445A006 |
0.36 |
|
| 1990 |
Papp S, Vanderkooi JM, Owen CS, Holtom GR, Phillips CM. Reactions of excited triplet states of metal substituted myoglobin with dioxygen and quinone. Biophysical Journal. 58: 177-86. PMID 2383630 DOI: 10.1016/S0006-3495(90)82363-8 |
0.343 |
|
| 1990 |
Vanderkooi JM, Wright WW, Erecinska M. Oxygen gradients in mitochondria examined with delayed luminescence from excited-state triplet probes. Biochemistry. 29: 5332-8. PMID 2383550 DOI: 10.1021/Bi00474A018 |
0.315 |
|
| 1990 |
Vanderkooi JM, Englander SW, Papp S, Wright WW, Owen CS. Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence. Proceedings of the National Academy of Sciences of the United States of America. 87: 5099-103. PMID 2367526 DOI: 10.1073/Pnas.87.13.5099 |
0.339 |
|
| 1990 |
Pachence JM, Amador S, Maniara G, Vanderkooi J, Dutton PL, Blasie JK. Orientation and lateral mobility of cytochrome c on the surface of ultrathin lipid multilayer films. Biophysical Journal. 58: 379-89. PMID 2169915 DOI: 10.1016/S0006-3495(90)82384-5 |
0.312 |
|
| 1990 |
Berger JW, Vanderkooi JM. THE ANAEROBIC PHOTOLYSIS OF LENS α-CRYSTALLIN: EVIDENCE FOR TRIPLET STATE MEDIATED PHOTODAMAGE Photochemistry and Photobiology. 52: 855-860. PMID 2089435 DOI: 10.1111/J.1751-1097.1990.Tb08693.X |
0.341 |
|
| 1989 |
Green TJ, Wilson DF, Vanderkooi JM, DeFeo SP. Phosphorimeters for analysis of decay profiles and real time monitoring of exponential decay and oxygen concentrations. Analytical Biochemistry. 174: 73-9. PMID 3218748 DOI: 10.1016/0003-2697(88)90520-9 |
0.306 |
|
| 1989 |
Berger JW, Vanderkooi JM. Characterization of lens alpha-crystallin tryptophan microenvironments by room temperature phosphorescence spectroscopy. Biochemistry. 28: 5501-5508. PMID 2775720 DOI: 10.1021/Bi00439A027 |
0.368 |
|
| 1989 |
Papp S, Vanderkooi JM. Tryptophan phosphorescence at room temperature as a tool to study protein structure and dynamics. Photochemistry and Photobiology. 49: 775-784. PMID 2672058 DOI: 10.1111/J.1751-1097.1989.Tb05576.X |
0.388 |
|
| 1989 |
Vanderkooi JM, Berger JW. Excited triplet states used to study biological macromolecules at room temperature Biochimica Et Biophysica Acta. 976: 1-27. PMID 2669975 DOI: 10.1016/S0005-2728(89)80185-9 |
0.356 |
|
| 1989 |
Fidy J, Paul KG, Vanderkooi JM. The mechanism of phototautomerization in mesoporphyrin horseradish peroxidase: studies by fluorescence line-narrowing spectroscopy The Journal of Physical Chemistry. 93: 2253-2261. DOI: 10.1021/J100343A014 |
0.322 |
|
| 1988 |
Maniara G, Vanderkooi JM, Bloomgarden DC, Koloczek H. PHOSPHORESCENCE FROM 2‐(p‐TOLUIDINYL)NAPHTHALENE‐6‐SULFONATE AND l‐ANILINONAPHTHALENE‐8‐SULFONATE, COMMONLY USED FLUORESCENCE PROBES OF BIOLOGICAL STRUCTURES Photochemistry and Photobiology. 47: 207-208. PMID 3344289 DOI: 10.1111/J.1751-1097.1988.Tb02715.X |
0.334 |
|
| 1988 |
Kanagy C, Vanderkooi JM, Bonner WD. Luminescence from the carbon monoxide derivative of Agaricus bispora tyrosinase. Archives of Biochemistry and Biophysics. 267: 668-75. PMID 2975158 DOI: 10.1016/0003-9861(88)90075-6 |
0.323 |
|
| 1988 |
Vanderkooi JM, Papp S, Pikula S, Martonosi A. Tryptophan phosphorescence of the Ca2+-ATPase of sarcoplasmic reticulum. Biochimica Et Biophysica Acta. 957: 230-236. PMID 2973355 DOI: 10.1016/0167-4838(88)90277-4 |
0.349 |
|
| 1988 |
Vanderkooi JM, Paul KG, Songstad J, Ernster L, Lönnberg H, Berg J, Bartók M, Pelczer I, Dombi G. Non-quenching by iodide of fluorescence in mesoporphyrin-substituted peroxidase Acta Chemica Scandinavica. 42: 125-126. DOI: 10.3891/Acta.Chem.Scand.42B-0125 |
0.329 |
|
| 1987 |
Vanderkooi JM, Calhoun DB, Englander SW. On the prevalence of room-temperature protein phosphorescence. Science (New York, N.Y.). 236: 568-9. PMID 3576185 DOI: 10.1126/Science.3576185 |
0.359 |
|
| 1987 |
Larralde C, Sassa S, Vanderkooi JM, Koloczek H, Laclette JP, Goodsaid F, Sciutto E, Owen CS. Analysis of porphyrins and enzymes in porphyrin synthesis in Taenia solium cysticercus from man and pig Molecular and Biochemical Parasitology. 22: 203-213. PMID 3574346 DOI: 10.1016/0166-6851(87)90051-X |
0.342 |
|
| 1987 |
Koloczek H, Horie T, Yonetani T, Anni H, Maniara G, Vanderkooi JM. Interaction between cytochrome c and cytochrome c peroxidase: excited-state reactions of zinc- and tin-substituted derivatives. Biochemistry. 26: 3142-3148. PMID 3038178 DOI: 10.1021/Bi00385A030 |
0.354 |
|
| 1987 |
Koloczek H, Vanderkooi JM. Domain structural flexibility in rhodanese examined by quenching of a phosphorescent probe. Biochimica Et Biophysica Acta. 916: 236-244. PMID 2445385 DOI: 10.1016/0167-4838(87)90114-2 |
0.317 |
|
| 1987 |
Koloczek H, Fidy J, Vanderkooi JM. Fluorescence line‐narrowing spectra of Zn‐cytochrome c. Temperature dependence The Journal of Chemical Physics. 87: 4388-4394. DOI: 10.1063/1.452899 |
0.409 |
|
| 1987 |
Fidy J, Koloczek H, Paul K, Vanderkooi JM. The pH dependence of phototautomerism in horse radish peroxidase monitored by fluorescence site-selection spectroscopy Chemical Physics Letters. 142: 562-566. DOI: 10.1016/0009-2614(87)80661-9 |
0.366 |
|
| 1986 |
Griffin EA, Vanderkooi JM, Maniara G, Erecińska M. Anthracycline binding to synthetic and natural membranes. A study using resonance energy transfer. Biochemistry. 25: 7875-80. PMID 3467794 DOI: 10.1021/Bi00372A013 |
0.334 |
|
| 1986 |
Calhoun DB, Vanderkooi JM, Holtom GR, Englander SW. Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure. Proteins. 1: 109-15. PMID 3130621 DOI: 10.1002/Prot.340010202 |
0.386 |
|
| 1985 |
Vanderkooi JM, Moy VT, Maniara G, Koloczek H, Paul KG. Site-selected fluorescence spectra of porphyrin derivatives of heme proteins. Biochemistry. 24: 7931-5. PMID 3004569 DOI: 10.1021/Bi00348A013 |
0.41 |
|
| 1985 |
Vanderkooi JM, Maniara G, Erecinska M. Mobility of fluorescent derivatives of cytochrome c in mitochondria. The Journal of Cell Biology. 100: 435-41. PMID 2981887 DOI: 10.1083/Jcb.100.2.435 |
0.36 |
|
| 1984 |
Horie T, Maniara G, Vanderkooi JM. Interaction of electron acceptors with the excited triplet state of Zn cytochrome c Febs Letters. 177: 287-290. PMID 6094249 DOI: 10.1016/0014-5793(84)81301-0 |
0.381 |
|
| 1984 |
Dixit BPSN, Moy VT, Vanderkooi JM. Reactions of excited-state cytochrome c derivatives. delayed fluorescence and phosphorescence of zinc, tin, and metal-free cytochrome C at room temperature Biochemistry. 23: 2103-2107. DOI: 10.1021/Bi00304A035 |
0.373 |
|
| 1983 |
Calhoun DB, Vanderkooi JM, Englander SW. Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence Biochemistry. 22: 1533-1539. PMID 6342663 DOI: 10.1021/Bi00276A003 |
0.368 |
|
| 1983 |
Calhoun DB, Vanderkooi JM, Woodrow GV, Englander SW. Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence Biochemistry. 22: 1526-1532. PMID 6342662 DOI: 10.1021/Bi00276A002 |
0.377 |
|
| 1982 |
Horie T, Vanderkooi JM. Phosphorescence of tryptophan from parvalbumin and actin in liquid solution Febs Letters. 147: 69-73. PMID 7140992 DOI: 10.1016/0014-5793(82)81013-2 |
0.401 |
|
| 1982 |
Cherenkevich SN, Vanderkooi JM, Deutsch C. Changes in membrane fluidity associated with lymphocyte stimulation by succinyl-concanavalin A. Biochimica Et Biophysica Acta. 686: 170-6. PMID 7082660 DOI: 10.1016/0005-2736(82)90109-2 |
0.345 |
|
| 1982 |
Cherenkevich SN, Vanderkooi JM, Holian A. The lipid integrity of membranes of guinea pig alveolar macrophages studied by nanosecond fluorescence decay of 1,6-diphenyl-1,3,5-hexatriene: The influence of temperature and benzyl alcohol1 Archives of Biochemistry and Biophysics. 214: 305-310. PMID 7082004 DOI: 10.1016/0003-9861(82)90035-2 |
0.302 |
|
| 1982 |
Cherenkevich SN, Vanderkooi JM, Restifo R, Daniele RP, Holian A. The lipid integrity of membranes of guinea pig alveolar macrophages studied by nanosecond fluorescence decay of 1,6-diphenyl-1,3,5-hexatriene: the effect of stimulation by concanavalin A and formyl peptides. Archives of Biochemistry and Biophysics. 214: 299-304. PMID 7082003 DOI: 10.1016/0003-9861(82)90034-0 |
0.319 |
|
| 1982 |
Dixit BPSN, Waring AJ, Wells KO, Wong PS, Woodrow GV, Vanderkooi JM. Rotational Motion of Cytochrome c Derivatives Bound to Membranes Measured by Fluorescence and Phosphorescence Anisotropy Febs Journal. 126: 1-9. PMID 6290209 DOI: 10.1111/J.1432-1033.1982.Tb06737.X |
0.38 |
|
| 1982 |
Angiolillo PJ, Leigh JS, Vanderkooi JM. Resolved fluorescence emission spectra of iron-free cytochrome c. Photochemistry and Photobiology. 36: 133-7. PMID 6289365 DOI: 10.1111/J.1751-1097.1982.Tb04354.X |
0.375 |
|
| 1981 |
Luedtke R, Owen CS, Vanderkooi JM, Karush F. Proximity relationships within the Fc segment of rabbit immunoglobulin G analyzed by resonance energy transfer Biochemistry. 20: 2927-2936. PMID 7248259 DOI: 10.1021/Bi00513A033 |
0.338 |
|
| 1981 |
Dixit SN, Waring AJ, Vanderkooi JM. Triplet absorption and phosphorescence emission in zinc cytochrome c Febs Letters. 125: 86-88. PMID 6262128 DOI: 10.1016/0014-5793(81)81002-2 |
0.359 |
|
| 1980 |
Vanderkooi JM, Glatz P, Casadei J, Woodrow GV. Cytochrome c interaction with yeast cytochrome b2. Heme distances determined by energy transfer in fluorescence resonance. Febs Journal. 110: 189-196. PMID 6254760 DOI: 10.1111/J.1432-1033.1980.Tb04854.X |
0.394 |
|
| 1979 |
Waring AJ, Glatz P, Vanderkooi JM. Subzero temperature study of the inner mitochondrial membrane and related phospholipid membrane systems with the fluorescent probe, trans-parinaric acid. Biochimica Et Biophysica Acta. 557: 391-398. PMID 497190 DOI: 10.1016/0005-2736(79)90337-7 |
0.364 |
|
| 1979 |
Glatz P, Chance B, Vanderkooi JM. Microsecond luminescence emission from copper cytochrome c. Biochemistry. 18: 3466-70. PMID 224910 DOI: 10.1021/Bi00583A005 |
0.356 |
|
| 1979 |
Vanderkooi JM, Weiss CJ, Woodrow GV. Fluorescent derivatives of nucleotides. Metal ion interactions and pH dependency. Biophysical Journal. 25: 263-75. PMID 45395 DOI: 10.1016/S0006-3495(79)85290-X |
0.381 |
|
| 1977 |
Vanderkooi JM, Landesberg R, Selick H, McDonald GG. Interaction of general anesthetics with phospholipid vesicles and biological membranes Biochimica Et Biophysica Acta. 464: 1-16. PMID 831785 DOI: 10.1016/0005-2736(77)90366-2 |
0.347 |
|
| 1977 |
Vanderkooi JM, Landesberg R, Hayden GW, Owen CS. Metal-Free and Metal-Substituted Cytochromes c. Use in Characterization of the Cytochrome c Binding Site Febs Journal. 81: 339-347. PMID 202455 DOI: 10.1111/J.1432-1033.1977.Tb11957.X |
0.344 |
|
| 1977 |
Goldfine H, Khuller GK, Borie RP, Silverman B, Selick H, Johnston NC, Vanderkooi JM, Horwitz AF. Effects of growth temperature and supplementation with exogenous fatty acids on some physical properties of Clostridium butyricum phospholipids Biochimica Et Biophysica Acta (Bba)/Lipids and Lipid Metabolism. 488: 341-352. PMID 198003 DOI: 10.1016/0005-2760(77)90193-X |
0.307 |
|
| 1977 |
Vanderkooi JM, Ierokomas A, Nakamura H, Martonosi A. Fluorescence energy transfer between Ca2+ transport ATPase molecules in artificial membranes. Biochemistry. 16: 1262-1267. PMID 139160 DOI: 10.1021/Bi00626A003 |
0.345 |
|
| 1976 |
Andrich MP, Vanderkooi JM. Temperature dependence of 1,6-diphenyl-1,3,5-hexatriene fluorescence in phophoslipid artificial membranes. Biochemistry. 15: 1257-1261. PMID 1252446 DOI: 10.1021/Bi00651A013 |
0.353 |
|
| 1976 |
Vanderkooi JM, Adar F, Erecińska M. Metallocytochromes c: characterization of electronic absorption and emission spectra of Sn4+ and Zn2+ cytochromes c. European Journal of Biochemistry / Febs. 64: 381-7. PMID 179813 DOI: 10.1111/J.1432-1033.1976.Tb10312.X |
0.423 |
|
| 1976 |
Vanderkooi JM. Photoreduction of membrane bound cytochrome c by excited-state phencthiazine Biochemical and Biophysical Research Communications. 69: 1043-1049. PMID 179539 DOI: 10.1016/0006-291X(76)90478-2 |
0.35 |
|
| 1975 |
Fischkoff S, Vanderkooi JM. Oxygen diffusion in biological and artificial membranes determined by the fluorochrome pyrene. The Journal of General Physiology. 65: 663-676. PMID 1176942 DOI: 10.1085/Jgp.65.5.663 |
0.329 |
|
| 1975 |
Wilson DF, Miyata Y, Erecińska M, Vanderkooi JM. An aryl azide suitable for photoaffinity labeling of amine groups in proteins. Archives of Biochemistry and Biophysics. 171: 102-7. PMID 242266 DOI: 10.1016/0003-9861(75)90012-0 |
0.318 |
|
| 1975 |
Erecińska M, Vanderkooi JM, Wilson DF. Cytochrome c interactions with membranes. A photoaffinity-labeled cytochrome c. Archives of Biochemistry and Biophysics. 171: 108-16. PMID 172021 DOI: 10.1016/0003-9861(75)90013-2 |
0.326 |
|
| 1975 |
Vanderkooi JM, Erecińska M. Cytochrome c interaction with membranes. Absorption and emission spectra and binding characteristics of iron-free cytochrome c. European Journal of Biochemistry / Febs. 60: 199-207. PMID 1265 DOI: 10.1111/J.1432-1033.1975.Tb20992.X |
0.423 |
|
| 1975 |
Vanderkooi JM, Fischkoff S, Andrich M, Podo F, Owen CS. Diffusion in two dimensions: Comparison between diffusional fluorescence quenching in phospholipid vesicles and in isotropic solution Journal of Chemical Physics. 63: 3661-3666. DOI: 10.1063/1.431761 |
0.313 |
|
| 1974 |
Vanderkooi J, Callis J, Chance B. Use of the fluorescent dye, Pyrene, to study the dynamic aspects of membrane structure The Histochemical Journal. 6: 301-310. PMID 4838361 DOI: 10.1007/Bf01312248 |
0.347 |
|
| 1974 |
Vanderkooi J, Erecińska M. Cytochrome c interaction with membranes. Interaction of cytochrome c with isolated membrane fragments and purified enzymes. Archives of Biochemistry and Biophysics. 162: 385-91. PMID 4366145 DOI: 10.1016/0003-9861(74)90196-9 |
0.325 |
|
| 1973 |
Vanderkooi J, Erecińska M, Chance B. Cytochrome c interaction with membranes. II. Comparative study of the interaction of c cytochromes with the mitochondrial membrane. Archives of Biochemistry and Biophysics. 157: 531-40. PMID 4354322 DOI: 10.1016/0003-9861(73)90672-3 |
0.314 |
|
| 1973 |
Vanderkooi J, Erecińska M, Chance B. Cytochrome c interaction with membranes. I. Use of a fluorescent chromophore in the study of cytochrome c interaction with artificial and mitochondrial membranes. Archives of Biochemistry and Biophysics. 154: 219-29. PMID 4347678 DOI: 10.1016/0003-9861(73)90052-0 |
0.361 |
|
| 1971 |
Vanderkooi JM, Martonosi A. Sarcoplasmic reticulum. XII. The interaction of 8-anilino-1-naphthalene sulfonate with skeletal muscle microsomes. Archives of Biochemistry and Biophysics. 144: 87-98. PMID 4330132 DOI: 10.1016/0003-9861(71)90457-7 |
0.37 |
|
| 1971 |
Vanderkooi JM, Martonosi A. Sarcoplasmic reticulum: XIII. Changes in the fluorescence of 8-anilino-1-naphthalene sulfonate during Ca2 transport☆ Archives of Biochemistry and Biophysics. 144: 99-106. DOI: 10.1016/0003-9861(71)90458-9 |
0.307 |
|
| 1969 |
Vanderkooi J, Martonosi A. Sarcoplasmic reticulum. 8. Use of 8-anilino-1-naphthalene sulfonate as conformational probe on biological membranes. Archives of Biochemistry and Biophysics. 133: 153-163. PMID 4309361 DOI: 10.1016/0003-9861(69)90499-8 |
0.393 |
|
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