| Year |
Citation |
Score |
| 2019 |
Mei G, Mamaeva N, Ganapathy S, Wang P, DeGrip WJ, Rothschild KJ. Analog Retinal Redshifts Visible Absorption of QuasAr Transmembrane Voltage Sensors into Near-infrared. Photochemistry and Photobiology. PMID 31556123 DOI: 10.1111/Php.13169 |
0.389 |
|
| 2019 |
Lee HJ, Huang KC, Mei G, Zong C, Mamaeva NV, de Grip WJ, Rothschild KJ, Cheng JX. Electronic Pre-resonance Stimulated Raman Scattering Imaging of Red-shifted Proteorhodopsins: Towards Quantitation of Membrane Potential. The Journal of Physical Chemistry Letters. PMID 31313926 DOI: 10.1021/Acs.Jpclett.9B01337 |
0.345 |
|
| 2019 |
Ganapathy S, Kratz S, Chen Q, Hellingwerf KJ, de Groot HJM, Rothschild KJ, de Grip WJ. Red-shifted and near-infrared active analog pigments based upon archaerhodopsin-3. Photochemistry and Photobiology. PMID 30860604 DOI: 10.1111/Php.13093 |
0.42 |
|
| 2018 |
Mei G, Mamaeva N, Ganapathy S, Wang P, DeGrip WJ, Rothschild KJ. Raman spectroscopy of a near infrared absorbing proteorhodopsin: Similarities to the bacteriorhodopsin O photointermediate. Plos One. 13: e0209506. PMID 30586409 DOI: 10.1371/Journal.Pone.0209506 |
0.445 |
|
| 2017 |
Yi A, Li H, Mamaeva NV, de Cordoba RF, Lugtenburg J, DeGrip WJ, Spudich JL, Rothschild KJ. Structural Changes in an Anion Channelrhodopsin: Formation of the K and L Intermediates at 80 K. Biochemistry. PMID 28350445 DOI: 10.1021/Acs.Biochem.7B00002 |
0.407 |
|
| 2016 |
Yi A, Mamaeva NV, Li H, Spudich JL, Rothschild KJ. Resonance Raman Study of an Anion Channelrhodopsin: Effects of Mutations Near the Retinylidene Schiff Base. Biochemistry. PMID 27039989 DOI: 10.1021/Acs.Biochem.6B00104 |
0.458 |
|
| 2016 |
Rothschild KJ. The early development and application of FTIR difference spectroscopy to membrane proteins: A personal perspective Biomedical Spectroscopy and Imaging. 5: 231-267. DOI: 10.3233/Bsi-160148 |
0.46 |
|
| 2016 |
Yi A, Mamaeva N, Li H, Spudich JL, Rothschild KJ. NEAR-IR Resonance Raman Characterization of an Anion Channelrhodopsin from Guillardia Theta Biophysical Journal. 110: 117a. DOI: 10.1016/J.Bpj.2015.11.684 |
0.443 |
|
| 2015 |
Ogren JI, Yi A, Mamaev S, Li H, Spudich JL, Rothschild KJ. Proton transfers in a channelrhodopsin-1 studied by Fourier transform infrared (FTIR) difference spectroscopy and site-directed mutagenesis. The Journal of Biological Chemistry. 290: 12719-30. PMID 25802337 DOI: 10.1074/Jbc.M114.634840 |
0.469 |
|
| 2015 |
Ogren JI, Yi A, Mamaev S, Li H, Lugtenburg J, DeGrip WJ, Spudich JL, Rothschild KJ. Comparison of the structural changes occurring during the primary phototransition of two different channelrhodopsins from Chlamydomonas algae. Biochemistry. 54: 377-88. PMID 25469620 DOI: 10.1021/Bi501243Y |
0.512 |
|
| 2015 |
Yi A, Ogren JI, Mamaev S, Li H, Lugtenburg J, DeGrip WJ, Spudich JL, Rothschild KJ. Vibrational Studies of Channelrhodopsin-1 from Chlamydomonas Augustae: Protonation Changes during the Early Photocycle Biophysical Journal. 108: 460a. DOI: 10.1016/J.Bpj.2014.11.2510 |
0.514 |
|
| 2014 |
Ogren JI, Mamaev S, Russano D, Li H, Spudich JL, Rothschild KJ. Retinal chromophore structure and Schiff base interactions in red-shifted channelrhodopsin-1 from Chlamydomonas augustae. Biochemistry. 53: 3961-70. PMID 24869998 DOI: 10.1021/Bi500445C |
0.495 |
|
| 2014 |
Ogren JI, Russano D, Mamaev S, Li H, Wang J, Spudich JL, Rothschild KJ. Resonance Raman and Low Temperature FTIR Characterization of the Red Shifted Channelrhodopsin 1 from Chlamydomonas Augustae Biophysical Journal. 106: 381a. DOI: 10.1016/J.Bpj.2013.11.2157 |
0.478 |
|
| 2013 |
Ogren JI, Saint Clair EC, Mamaev S, Russano D, Kralj JM, Rothschild KJ. Near-Ir Resonance Raman and Uv-Visible Absorption Kinetic Spectroscopy of Optogenetic Archaerhodopsin Neuronal Silencers: Effects of Membrane Potential Biophysical Journal. 104: 680a. DOI: 10.1016/J.Bpj.2012.11.3753 |
0.755 |
|
| 2012 |
Clair EC, Ogren JI, Mamaev S, Kralj JM, Rothschild KJ. Conformational changes in the archaerhodopsin-3 proton pump: detection of conserved strongly hydrogen bonded water networks. Journal of Biological Physics. 38: 153-68. PMID 23277676 DOI: 10.1007/S10867-011-9246-4 |
0.762 |
|
| 2012 |
Saint Clair EC, Ogren JI, Mamaev S, Russano D, Kralj JM, Rothschild KJ. Near-IR resonance Raman spectroscopy of archaerhodopsin 3: effects of transmembrane potential. The Journal of Physical Chemistry. B. 116: 14592-601. PMID 23189985 DOI: 10.1021/Jp309996A |
0.747 |
|
| 2012 |
Bayraktar H, Fields AP, Kralj JM, Spudich JL, Rothschild KJ, Cohen AE. Ultrasensitive measurements of microbial rhodopsin photocycles using photochromic FRET. Photochemistry and Photobiology. 88: 90-7. PMID 22010969 DOI: 10.1111/J.1751-1097.2011.01011.X |
0.726 |
|
| 2012 |
Ogren JI, Saint-Clair EC, Mamaev S, Kralj JM, Cohen AE, Rothschild KJ. Strongly Hydrogen Bonded Water Networks Detected in the Archaerhodopsin-3 Proton Pump Biophysical Journal. 102: 247a. DOI: 10.1016/J.Bpj.2011.11.1360 |
0.76 |
|
| 2011 |
Shirzad-Wasei N, Clair ES, Ogren JI, Stanzel C, Navarro J, deGrip WJ, Rothschild KJ. Expression and Spectroscopic Characterization of Melanopsin and Squid Rhodopsin Biophysical Journal. 100: 420a. DOI: 10.1016/J.Bpj.2010.12.2489 |
0.405 |
|
| 2010 |
Bergo VB, Clair ECS, Spudich EN, Spudich J, Rothschild KJ. Probing the Protein-Protein Signaling Mechanism in Intact Archaeal Cells Using Time-Resolved FTIR Difference Spectroscopy Biophysical Journal. 98: 560a. DOI: 10.1016/J.Bpj.2009.12.3033 |
0.786 |
|
| 2010 |
Jensen M, Clair ECS, Gabel A, Bergo VB, Spudich EN, Spudich JL, Rothschild KJ. Effects of Sensory Rhodopsin II Complexation with its Cognate Transducer HtrII on the Local Environment of Internal Water Molecules Biophysical Journal. 98: 287a. DOI: 10.1016/J.Bpj.2009.12.1567 |
0.776 |
|
| 2009 |
Bergo VB, Spudich EN, Spudich JL, Rothschild KJ. Active water in protein-protein communication within the membrane: the case of SRII-HtrII signal relay. Biochemistry. 48: 811-3. PMID 19187030 DOI: 10.1021/Bi802180A |
0.758 |
|
| 2009 |
Bergo VB, Sineshchekov OA, Kralj JM, Partha R, Spudich EN, Rothschild KJ, Spudich JL. His-75 in proteorhodopsin, a novel component in light-driven proton translocation by primary pumps. The Journal of Biological Chemistry. 284: 2836-43. PMID 19015272 DOI: 10.1074/Jbc.M803792200 |
0.814 |
|
| 2009 |
Kralj JM, Raber E, Sarmiento J, Shumate D, Stanzel C, Maxwell C, Navarro J, Rothschild KJ. Structural Changes of Cephalopod Rhodopsin and β-Arrestin Measured by FTIR Difference Spectroscopy and Isotope Editing Biophysical Journal. 96: 525a. DOI: 10.1016/J.Bpj.2008.12.2709 |
0.726 |
|
| 2009 |
Fields AP, Bayraktar H, Kralj J, Spudich JL, Rothschild KJ, Cohen AE. Spectral Shift FRET Assay and its Applications for Studying the Dynamics of Proteorhodopsin Biophysical Journal. 96: 329a. DOI: 10.1016/J.Bpj.2008.12.1658 |
0.739 |
|
| 2008 |
Amsden JJ, Kralj JM, Bergo VB, Spudich EN, Spudich JL, Rothschild KJ. Different structural changes occur in blue- and green-proteorhodopsins during the primary photoreaction. Biochemistry. 47: 11490-8. PMID 18842006 DOI: 10.1021/Bi800945T |
0.814 |
|
| 2008 |
Kralj JM, Spudich EN, Spudich JL, Rothschild KJ. Raman spectroscopy reveals direct chromophore interactions in the Leu/Gln105 spectral tuning switch of proteorhodopsins. The Journal of Physical Chemistry. B. 112: 11770-6. PMID 18717545 DOI: 10.1021/Jp802629E |
0.777 |
|
| 2008 |
Cappuccio JA, Blanchette CD, Sulchek TA, Arroyo ES, Kralj JM, Hinz AK, Kuhn EA, Chromy BA, Segelke BW, Rothschild KJ, Fletcher JE, Katzen F, Peterson TC, Kudlicki WA, Bench G, et al. Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles. Molecular & Cellular Proteomics : McP. 7: 2246-53. PMID 18603642 DOI: 10.1074/Mcp.M800191-Mcp200 |
0.716 |
|
| 2008 |
Kralj JM, Bergo VB, Amsden JJ, Spudich EN, Spudich JL, Rothschild KJ. Protonation state of Glu142 differs in the green- and blue-absorbing variants of proteorhodopsin. Biochemistry. 47: 3447-53. PMID 18284210 DOI: 10.1021/Bi7018964 |
0.797 |
|
| 2007 |
Amsden JJ, Kralj JM, Chieffo LR, Wang X, Erramilli S, Spudich EN, Spudich JL, Ziegler LD, Rothschild KJ. Subpicosecond protein backbone changes detected during the green-absorbing proteorhodopsin primary photoreaction. The Journal of Physical Chemistry. B. 111: 11824-31. PMID 17880126 DOI: 10.1021/Jp073490R |
0.825 |
|
| 2006 |
Bergo VB, Ntefidou M, Trivedi VD, Amsden JJ, Kralj JM, Rothschild KJ, Spudich JL. Conformational changes in the photocycle of Anabaena sensory rhodopsin: absence of the Schiff base counterion protonation signal. The Journal of Biological Chemistry. 281: 15208-14. PMID 16537532 DOI: 10.1074/Jbc.M600033200 |
0.814 |
|
| 2005 |
Maji SK, Amsden JJ, Rothschild KJ, Condron MM, Teplow DB. Conformational dynamics of amyloid beta-protein assembly probed using intrinsic fluorescence. Biochemistry. 44: 13365-76. PMID 16201761 DOI: 10.1021/Bi0508284 |
0.634 |
|
| 2005 |
Olejnik J, Gite S, Mamaev S, Rothschild KJ. N-terminal labeling of proteins using initiator tRNA. Methods (San Diego, Calif.). 36: 252-60. PMID 16076451 DOI: 10.1016/J.Ymeth.2005.04.003 |
0.322 |
|
| 2005 |
Bergo VB, Spudich EN, Rothschild KJ, Spudich JL. Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer. The Journal of Biological Chemistry. 280: 28365-9. PMID 15951432 DOI: 10.1074/Jbc.M505555200 |
0.786 |
|
| 2004 |
Bergo V, Amsden JJ, Spudich EN, Spudich JL, Rothschild KJ. Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction. Biochemistry. 43: 9075-83. PMID 15248764 DOI: 10.1021/Bi0361968 |
0.82 |
|
| 2004 |
Mamaev S, Olejnik J, Olejnik EK, Rothschild KJ. Cell-free N-terminal protein labeling using initiator suppressor tRNA. Analytical Biochemistry. 326: 25-32. PMID 14769332 DOI: 10.1016/J.Ab.2003.11.002 |
0.308 |
|
| 2003 |
Bergo V, Spudich EN, Spudich JL, Rothschild KJ. Conformational changes detected in a sensory rhodopsin II-transducer complex. The Journal of Biological Chemistry. 278: 36556-62. PMID 12821665 DOI: 10.1074/Jbc.M303719200 |
0.784 |
|
| 2003 |
Bergo V, Mamaev S, Olejnik J, Rothschild KJ. Methionine changes in bacteriorhodopsin detected by FTIR and cell-free selenomethionine substitution. Biophysical Journal. 84: 960-6. PMID 12547777 DOI: 10.1016/S0006-3495(03)74912-1 |
0.802 |
|
| 2002 |
Bergo V, Spudich EN, Spudich JL, Rothschild KJ. A Fourier transform infrared study of Neurospora rhodopsin: similarities with archaeal rhodopsins. Photochemistry and Photobiology. 76: 341-9. PMID 12403457 DOI: 10.1562/0031-8655(2002)076<0341:Aftiso>2.0.Co;2 |
0.794 |
|
| 2000 |
Bergo V, Spudich EN, Scott KL, Spudich JL, Rothschild KJ. FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor. Biochemistry. 39: 2823-30. PMID 10715101 DOI: 10.1021/Bi991676D |
0.799 |
|
| 2000 |
Gite S, Mamaev S, Olejnik J, Rothschild K. Ultrasensitive fluorescence-based detection of nascent proteins in gels. Analytical Biochemistry. 279: 218-25. PMID 10706791 DOI: 10.1006/Abio.1999.4472 |
0.363 |
|
| 1999 |
DeGrip WJ, DeLange F, Klaassen CH, Verdegem PJ, Wallace-Williams S, Creemers AF, Bergo V, Bovee PH, Raap J, Rothschild KJ, DeGroot HJ, Lugtenburg J. Photoactivation of rhodopsin: interplay between protein and chromophore. Novartis Foundation Symposium. 224: 102-18; discussion 1. PMID 10614048 DOI: 10.1002/9780470515693.Ch7 |
0.763 |
|
| 1999 |
DeLange F, Bovee-Geurts PHM, Pistorius AMA, Rothschild KJ, DeGrip WJ. Probing intramolecular orientations in rhodopsin and metarhodopsin II by polarized infrared difference spectroscopy Biochemistry. 38: 13200-13209. PMID 10529192 DOI: 10.1021/Bi9909501 |
0.459 |
|
| 1999 |
Rothschild KJ, Gite S. tRNA-mediated protein engineering Current Opinion in Biotechnology. 10: 64-70. PMID 10047513 DOI: 10.1016/S0958-1669(99)80012-3 |
0.311 |
|
| 1998 |
DeLange F, Klaassen CHW, Wallace-Williams SE, Bovee-Geurtst PHM, Liu XM, DeGrip WJ, Rothschild KJ. Tyrosine structural changes detected during the photoactivation of rhodopsin Journal of Biological Chemistry. 273: 23735-23739. PMID 9726981 DOI: 10.1074/jbc.273.37.23735 |
0.353 |
|
| 1998 |
Liu X, Lee MJ, Coleman M, Rath P, Nilsson A, Fischer WB, Bizounok M, Herzfeld J, Karstens WF, Raap J, Lugtenburg J, Rothschild KJ. Detection of threonine structural changes upon formation of the M-intermediate of bacteriorhodopsin: evidence for assignment to Thr-89. Biochimica Et Biophysica Acta. 1365: 363-72. PMID 9711293 DOI: 10.1016/S0005-2728(98)00088-7 |
0.658 |
|
| 1998 |
Olejnik J, Krzymanska-Olejnik E, Rothschild KJ. Photocleavable aminotag phosphoramidites for 5'-termini DNA/RNA labeling Nucleic Acids Research. 26: 3572-3576. PMID 9671821 DOI: 10.1093/Nar/26.15.3572 |
0.304 |
|
| 1998 |
Kluge T, Olejnik J, Smilowitz L, Rothschild KJ. Conformational changes in the core structure of bacteriorhodopsin Biochemistry. 37: 10279-10285. PMID 9665736 DOI: 10.1021/Bi9802465 |
0.467 |
|
| 1998 |
Rath P, DeGrip WJ, Rothschild KJ. Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups Biophysical Journal. 74: 192-198. PMID 9449322 DOI: 10.1016/S0006-3495(98)77779-3 |
0.426 |
|
| 1998 |
Rath P, Delange F, Degrip WJ, Rothschild KJ. Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation Biochemical Journal. 329: 713-717. PMID 9445403 |
0.337 |
|
| 1997 |
Hunt JF, Rath P, Rothschild KJ, Engelman DM. Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix. Biochemistry. 36: 15177-92. PMID 9398245 DOI: 10.1021/Bi970147B |
0.368 |
|
| 1997 |
Hunt JF, Earnest TN, Bousché O, Kalghatgi K, Reilly K, Horváth C, Rothschild KJ, Engelman DM. A biophysical study of integral membrane protein folding. Biochemistry. 36: 15156-76. PMID 9398244 DOI: 10.1021/Bi970146J |
0.394 |
|
| 1997 |
Russell TS, Coleman M, Rath P, Nilsson A, Rothschild KJ. Threonine-89 participates in the active site of bacteriorhodopsin: Evidence for a role in color regulation and schiff base proton transfer Biochemistry. 36: 7490-7497. PMID 9200698 DOI: 10.1021/Bi970287L |
0.459 |
|
| 1997 |
Ludlam GJ, Rothschild KJ. Similarity of bacteriorbodopsin structural changes triggered by chromophore removal and light-driven proton transport Febs Letters. 407: 285-288. PMID 9175869 DOI: 10.1016/S0014-5793(97)00351-7 |
0.446 |
|
| 1996 |
Ludlam CF, Arkin IT, Liu XM, Rothman MS, Rath P, Aimoto S, Smith SO, Engelman DM, Rothschild KJ. Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophysical Journal. 70: 1728-36. PMID 8785331 DOI: 10.1016/S0006-3495(96)79735-7 |
0.467 |
|
| 1996 |
Rath P, Spudich E, Neal DD, Spudich JL, Rothschild KJ. Asp76 is the schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I Biochemistry. 35: 6690-6696. PMID 8639619 DOI: 10.1021/Bi9600355 |
0.424 |
|
| 1996 |
Sonar S, Lee CP, Ludlam CFC, Liu XM, Coleman M, Marti T, RajBhandary UL, Rothschild KJ. Site-directed isotope labeling of membrane proteins: A new tool for spectroscopists Techniques in Protein Chemistry. 7: 151-159. DOI: 10.1016/S1080-8914(96)80019-6 |
0.413 |
|
| 1995 |
Nilsson A, Rath P, Olejnik J, Coleman M, Rothschild KJ. Protein conformational changes during the bacteriorhodopsin photocycle: A fourier transform infrared/resonance Raman study of the alkaline form of the mutant Asp-85 → Asn Journal of Biological Chemistry. 270: 29746-29751. PMID 8530365 DOI: 10.1074/Jbc.270.50.29746 |
0.522 |
|
| 1995 |
Ludlam CF, Sonar S, Lee CP, Coleman M, Herzfeld J, RajBhandary UL, Rothschild KJ. Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR-->N transition. Biochemistry. 34: 2-6. PMID 7819197 DOI: 10.1021/Bi00001A001 |
0.629 |
|
| 1995 |
Arkin IT, Rothman M, Ludlam CF, Aimoto S, Engelman DM, Rothschild KJ, Smith SO. Structural model of the phospholamban ion channel complex in phospholipid membranes. Journal of Molecular Biology. 248: 824-34. PMID 7752243 DOI: 10.1006/Jmbi.1995.0263 |
0.408 |
|
| 1995 |
DeCaluwé GL, Bovee-Geurts PH, Rath P, Rothschild KJ, de Grip WJ. Effect of carboxyl mutations on functional properties of bovine rhodopsin. Biophysical Chemistry. 56: 79-87. PMID 7662872 DOI: 10.1016/0301-4622(95)00018-S |
0.394 |
|
| 1995 |
Liu XM, Sonar S, Lee CP, Coleman M, RajBhandary UL, Rothschild KJ. Site-directed isotope labeling and FTIR spectroscopy: assignment of tyrosine bands in the bR-->M difference spectrum of bacteriorhodopsin. Biophysical Chemistry. 56: 63-70. PMID 7662870 DOI: 10.1016/0301-4622(95)00016-Q |
0.477 |
|
| 1995 |
Olejnik J, Sonar S, Krzymañska-Olejnik E, Rothschild KJ. Photocleavable biotin derivatives: A versatile approach for the isolation of biomolecules Proceedings of the National Academy of Sciences of the United States of America. 92: 7590-7594. PMID 7638235 DOI: 10.1073/Pnas.92.16.7590 |
0.303 |
|
| 1995 |
Coleman M, Nilsson A, Russell TS, Rath P, Pandey R, Rothschild KJ. Asp 46 can substitute for Asp 96 as the Schiff base proton donor in bacteriorhodopsin Biochemistry. 34: 15599-15606. PMID 7492563 DOI: 10.1021/Bi00047A027 |
0.434 |
|
| 1995 |
Sonar S, Liu Xiao-Mei, Lee Chan-Ping, Coleman M, He Yi-Wu, Pelletier S, Herzfeld J, RajBhandary UL, Rothschild KJ. Site-directed isotope labeling and FT-IR spectroscopy: The Tyr 185/Pro 186 peptide bond of bacteriorhodopsin is perturbed during the primary photoreaction Journal of the American Chemical Society. 117: 11614-11615. DOI: 10.1021/Ja00151A041 |
0.571 |
|
| 1995 |
Rothschild KJ. Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: The peptide carbonyl group of Tyr 185 is structurally active during the bR → N transition Biochemistry®. 34: 2-6. |
0.316 |
|
| 1994 |
Rath P, Olson KD, Spudich JL, Rothschild KJ. The schiff base counterion of bacteriorhodopsin is protonated in sensory rhodopsin I: Spectroscopic and functional characterization of the mutated proteins D76N and D76A Biochemistry. 33: 5600-5606. PMID 8180184 DOI: 10.1021/Bi00184A032 |
0.495 |
|
| 1994 |
Rath P, Bovee-Geurts PHM, DeGrip WJ, Rothschild KJ. Photoactivation of rhodopsin involves alterations in cysteine side chains: Detection of an S-H band in the Meta I→Meta II FTIR difference spectrum Biophysical Journal. 66: 2085-2091. PMID 8075342 DOI: 10.1016/S0006-3495(94)81003-3 |
0.439 |
|
| 1994 |
Sonar S, Marti T, Rath P, Fischer W, Coleman M, Nilsson A, Khorana HG, Rothschild KJ. A redirected proton pathway in the bacteriorhodopsin mutant Tyr-57-->Asp. Evidence for proton translocation without Schiff base deprotonation. The Journal of Biological Chemistry. 269: 28851-8. PMID 7961844 |
0.555 |
|
| 1994 |
Fischer WB, Sonar S, Marti T, Khorana HG, Rothschild KJ. Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction. Biochemistry. 33: 12757-62. PMID 7947680 DOI: 10.1021/bi00209a005 |
0.542 |
|
| 1994 |
Sonar S, Lee CP, Coleman M, Patel N, Liu X, Marti T, Khorana HG, RajBhandary UL, Rothschild KJ. Site-directed isotope labelling and FTIR spectroscopy of bacteriorhodopsin. Nature Structural Biology. 1: 512-7. PMID 7664078 DOI: 10.1038/Nsb0894-512 |
0.602 |
|
| 1993 |
Baenziger JE, Miller KW, Rothschild KJ. Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: Evidence for specific protein structural changes upon desensitization Biochemistry. 32: 5448-5454. PMID 8499448 DOI: 10.1021/Bi00071A022 |
0.762 |
|
| 1993 |
He Y, Krebs MP, Fischer WB, Khorana HG, Rothschild KJ. FTIR difference spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: detection of a stable O-like species and characterization of its photocycle at low temperature. Biochemistry. 32: 2282-90. PMID 8443171 DOI: 10.1021/Bi00060A021 |
0.638 |
|
| 1993 |
Rath P, Krebs MP, He Y, Khorana HG, Rothschild KJ. Fourier transform Raman spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: formation of a stable O-like species during light adaptation and detection of its transient N-like photoproduct. Biochemistry. 32: 2272-81. PMID 8443170 DOI: 10.1021/Bi00060A020 |
0.591 |
|
| 1993 |
Sonar S, Krebs MP, Khorana HG, Rothschild KJ. Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species. Biochemistry. 32: 2263-71. PMID 8443169 DOI: 10.1021/Bi00060A019 |
0.563 |
|
| 1993 |
Rath P, DeCaluwé LLJ, Bovee-Geurts PHM, DeGrip WJ, Rothschild KJ. Fourier transform infrared difference spectroscopy of rhodopsin mutants: Light activation of rhodopsin causes hydrogen-bonding change in residue aspartic acid-83 during meta II formation Biochemistry. 32: 10277-10282. PMID 8399169 DOI: 10.1021/Bi00090A001 |
0.527 |
|
| 1993 |
Rath P, Marti T, Sonar S, Khorana HG, Rothschild KJ. Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin. Resonance Raman spectroscopy of the mutants D85N and D85A. The Journal of Biological Chemistry. 268: 17742-9. PMID 8349659 |
0.563 |
|
| 1993 |
Sonar S, Patel N, Fischer W, Rothschild KJ. Cell-free synthesis, functional refolding, and spectroscopic characterization of bacteriorhodopsin, an integral membrane protein Biochemistry. 32: 13777-13781. PMID 8268152 DOI: 10.1021/Bi00213A004 |
0.415 |
|
| 1993 |
Rothschild KJ, Marti T, Sonar S, He YW, Rath P, Fischer W, Khorana HG. Asp96 deprotonation and transmembrane alpha-helical structural changes in bacteriorhodopsin. The Journal of Biological Chemistry. 268: 27046-52. PMID 8262942 |
0.595 |
|
| 1992 |
Rothschild KJ, He YW, Sonar S, Marti T, Khorana HG. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds. The Journal of Biological Chemistry. 267: 1615-22. PMID 1730706 |
0.598 |
|
| 1992 |
Baenziger JE, Miller KW, McCarthy MP, Rothschild KJ. Probing conformational changes in the nicotinic acetylcholine receptor by Fourier transform infrared difference spectroscopy Biophysical Journal. 62: 64-66. PMID 1600101 DOI: 10.1016/S0006-3495(92)81780-0 |
0.71 |
|
| 1992 |
Rothschild KJ. FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model Journal of Bioenergetics and Biomembranes. 24: 147-167. PMID 1526959 DOI: 10.1007/Bf00762674 |
0.511 |
|
| 1992 |
Bousché O, Sonar S, Krebs MP, Khorana HG, Rothschild KJ. Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay. Photochemistry and Photobiology. 56: 1085-95. PMID 1337213 DOI: 10.1111/J.1751-1097.1992.Tb09732.X |
0.635 |
|
| 1991 |
Bousché O, Braiman M, He YW, Marti T, Khorana HG, Rothschild KJ. Vibrational spectroscopy of bacteriorhodopsin mutants: Evidence that Asp-96 deprotonates during the M → N transition Journal of Biological Chemistry. 266: 11063-11067. PMID 2040618 |
0.341 |
|
| 1991 |
Bousche O, Spudich EN, Spudich JL, Rothschild KJ. Conformational changes in sensory rhodopsin I: Similarities and differences with bacteriorhodopsin, halorhodopsin, and rhodopsin Biochemistry. 30: 5395-5400. PMID 2036407 DOI: 10.1021/Bi00236A010 |
0.507 |
|
| 1991 |
Braiman MS, Bousche O, Rothschild KJ. Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates Proceedings of the National Academy of Sciences of the United States of America. 88: 2388-2392. PMID 2006176 DOI: 10.1073/Pnas.88.6.2388 |
0.723 |
|
| 1991 |
Rath P, Bousche O, Merill AR, Cramer WA, Rothschild KJ. Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1 Biophysical Journal. 59: 516-522. PMID 1710937 DOI: 10.1016/S0006-3495(91)82268-8 |
0.415 |
|
| 1991 |
Subramaniam S, Greenhalgh DA, Rath P, Rothschild KJ, Khorana HG. Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization. Proceedings of the National Academy of Sciences of the United States of America. 88: 6873-7. PMID 1650486 DOI: 10.1073/Pnas.88.15.6873 |
0.505 |
|
| 1990 |
Earnest TN, Herzfeld J, Rothschild KJ. Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. Biophysical Journal. 58: 1539-46. PMID 2275968 DOI: 10.1016/S0006-3495(90)82498-X |
0.629 |
|
| 1990 |
Duñach M, Marti T, Gobind Khorana H, Rothschild KJ. UV-visible spectroscopy of bacteriorhodopsin mutants: Substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal it-dark adaptation Proceedings of the National Academy of Sciences of the United States of America. 87: 9873-9877. PMID 2263638 DOI: 10.1073/Pnas.87.24.9873 |
0.418 |
|
| 1990 |
Rothschild KJ, Braiman MS, He YW, Marti T, Khorana HG. Vibrational spectroscopy of bacteriorhodopsin mutants: Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pump mechanism Journal of Biological Chemistry. 265: 16985-16991. PMID 2211604 |
0.724 |
|
| 1990 |
Duñach M, Berkowitz S, Marti T, He YW, Subramaniam S, Khorana HG, Rothschild KJ. Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants: Evidence for two forms of tyrosine-185 → phenylalanine Journal of Biological Chemistry. 265: 16978-16984. PMID 2211603 |
0.34 |
|
| 1990 |
Rothschild KJ, He YW, Mogi T, Marti T, Stern LJ, Khorana HG. Vibrational spectroscopy of bacteriorhodopsin mutants: evidence for the interaction of proline-186 with the retinylidene chromophore. Biochemistry. 29: 5954-60. PMID 2166567 DOI: 10.1021/Bi00477A011 |
0.638 |
|
| 1989 |
Rothschild KJ, Gray D, Mogi T, Marti T, Braiman MS, Stern LJ, Khorana HG. Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs tryptophan-86. Biochemistry. 28: 7052-9. PMID 2819048 DOI: 10.1021/Bi00443A041 |
0.76 |
|
| 1989 |
Rothschild KJ, Braiman MS, Mogi T, Stern LJ, Khorana HG. Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket. Febs Letters. 250: 448-52. PMID 2753143 DOI: 10.1016/0014-5793(89)80774-4 |
0.717 |
|
| 1989 |
Rothschild KJ, He YW, Gray D, Roepe PD, Pelletier SL, Brown RS, Herzfeld J. Fourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycle. Proceedings of the National Academy of Sciences of the United States of America. 86: 9832-5. PMID 2602377 DOI: 10.1073/Pnas.86.24.9832 |
0.676 |
|
| 1989 |
Stern LJ, Ahl PL, Marti T, Mogi T, Duñach M, Berkowitz S, Rothschild KJ, Khorana HG. Substitution of membrane-embedded aspartic acids in bacteriorhodopsin causes specific changes in different steps of the photochemical cycle. Biochemistry. 28: 10035-42. PMID 2575917 |
0.517 |
|
| 1989 |
Ahl PL, Stern LJ, Mogi T, Khorana HG, Rothschild KJ. Substitution of amino acids in helix F of bacteriorhodopsin: effects on the photochemical cycle. Biochemistry. 28: 10028-34. PMID 2575916 DOI: 10.1021/bi00452a022 |
0.522 |
|
| 1988 |
Rothschild KJ, Bousché O, Braiman MS, Hasselbacher CA, Spudich JL. Fourier transform infrared study of the halorhodopsin chloride pump Biochemistry®. 27: 2420-2424. PMID 3382631 DOI: 10.1021/Bi00407A026 |
0.737 |
|
| 1988 |
Roepe PD, Ahl PL, Herzfeld J, Lugtenburg J, Rothschild KJ. Tyrosine protonation changes in bacteriorhodopsin. A Fourier transform infrared study of BR548 and its primary photoproduct. The Journal of Biological Chemistry. 263: 5110-7. PMID 3356682 |
0.642 |
|
| 1988 |
Braiman MS, Rothschild KJ. Fourier transform infrared techniques for probing membrane protein structure Annual Review of Biophysics and Biophysical Chemistry. 17: 541-570. PMID 3293599 |
0.651 |
|
| 1988 |
DeGrip WJ, Gray D, Gillespie J, Bovee PH, Van den Berg EM, Lugtenburg J, Rothschild KJ. Photoexcitation of rhodopsin: conformation changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy. Photochemistry and Photobiology. 48: 497-504. PMID 3231685 DOI: 10.1111/J.1751-1097.1988.Tb02852.X |
0.507 |
|
| 1988 |
Ahl PL, Stern LJ, Düring D, Mogi T, Khorana HG, Rothschild KJ. Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy. The Journal of Biological Chemistry. 263: 13594-601. PMID 3047127 |
0.597 |
|
| 1988 |
Braiman MS, Mogi T, Marti T, Stern LJ, Khorana HG, Rothschild KJ. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. Biochemistry. 27: 8516-20. PMID 2851326 DOI: 10.1021/Bi00423A002 |
0.779 |
|
| 1988 |
Braiman MS, Mogi T, Stern LJ, Hackett NR, Chao BH, Khorana HG, Rothschild KJ. Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonates during the photocycle. Proteins. 3: 219-29. PMID 2843849 DOI: 10.1002/Prot.340030403 |
0.766 |
|
| 1988 |
Rothschild KJ. Infrared studies of bacteriorhodopsin Photochemistry and Photobiology. 47: 883-887. DOI: 10.1111/J.1751-1097.1988.Tb01671.X |
0.383 |
|
| 1988 |
Roepe P, Gray D, Lugtenburg J, Van Den Berg EMM, Herzfeld J, Rothschild KJ. FTIR evidence for tryptophan perturbations during the bacteriorhodopsin photocycle Journal of the American Chemical Society. 110: 7223-7224. DOI: 10.1021/Ja00229A052 |
0.552 |
|
| 1987 |
Rothschild KJ, Gillepsie J, DeGrip WJ. Evidence for rhodopsin refolding during the decay of Meta II Biophysical Journal. 51: 345-350. PMID 3828465 DOI: 10.1016/S0006-3495(87)83341-6 |
0.388 |
|
| 1987 |
Marrero H, Rothschild KJ. Conformational changes in bacteriorhodopsin studied by infrared attenuated total reflection Biophysical Journal. 52: 629-635. PMID 3676442 DOI: 10.1016/S0006-3495(87)83254-X |
0.448 |
|
| 1987 |
Braiman MS, Ahl PL, Rothschild KJ. Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct Proceedings of the National Academy of Sciences of the United States of America. 84: 5221-5225. PMID 3474649 DOI: 10.1073/Pnas.84.15.5221 |
0.711 |
|
| 1987 |
Roepe P, Scherrer P, Ahl PL, Das Gupta SK, Bogomolni RA, Herzfeld J, Rothschild KJ. Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 2. Tyrosines-26 and -64. Biochemistry. 26: 6708-17. PMID 3427039 DOI: 10.1021/Bi00395A021 |
0.627 |
|
| 1987 |
Roepe P, Ahl PL, Das Gupta SK, Herzfeld J, Rothschild KJ. Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 1. M412 and L550 intermediates. Biochemistry. 26: 6696-707. PMID 3427038 DOI: 10.1021/Bi00395A020 |
0.651 |
|
| 1987 |
Marrero H, Rothschild KJ. Bacteriorhodopsin's M412 and BR605 protein conformations are similar Significance for proton transport Febs Letters. 223: 289-293. DOI: 10.1016/0014-5793(87)80306-X |
0.438 |
|
| 1986 |
Earnest TN, Roepe P, Braiman MS, Gillespie J, Rothschild KJ. Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy Biochemistry. 25: 7793-7798. PMID 3801443 DOI: 10.1021/Bi00372A002 |
0.707 |
|
| 1986 |
Rothschild KJ, Roepe P, Ahl PL, Earnest TN, Bogomolni RA, Das Gupta SK, Mulliken CM, Herzfeld J. Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature. Proceedings of the National Academy of Sciences of the United States of America. 83: 347-51. PMID 3001733 DOI: 10.1073/Pnas.83.2.347 |
0.622 |
|
| 1986 |
Rothschild KJ. [25] Fourier transform infrared studies of an active proton transport pump Methods in Enzymology. 127: 343-353. PMID 2874474 DOI: 10.1016/0076-6879(86)27028-7 |
0.443 |
|
| 1985 |
Rothschild KJ, Roepe P, Gillespie J. Fourier transform infrared spectroscopic evidence for the existence of two conformations of the bacteriorhodopsin primary photoproduct at low temperature Bba - Bioenergetics. 808: 140-148. PMID 4005227 DOI: 10.1016/0005-2728(85)90036-2 |
0.421 |
|
| 1985 |
de Grip WJ, Gillespie J, Rothschild KJ. Carboxyl group involvement in the meta I and meta II stages in rhodopsin bleaching. A Fourier transform infrared spectroscopic study. Biochimica Et Biophysica Acta. 809: 97-106. PMID 2992584 DOI: 10.1016/0005-2728(85)90172-0 |
0.428 |
|
| 1984 |
Rothschild KJ, Roepe P, Lugtenburg J, Pardoen JA. Fourier transform infrared evidence for Schiff base alteration in the first step of the bacteriorhodopsin photocycle Biochemistry. 23: 6103-6109. PMID 6525348 DOI: 10.1021/Bi00320A031 |
0.448 |
|
| 1984 |
Rothschild KJ, Marrero H, Braiman M, Mathies R. Primary photochemistry of bacteriorhodopsin: comparison of Fourier transform infrared difference spectra with resonance Raman spectra Photochemistry and Photobiology. 40: 675-679. PMID 6514815 DOI: 10.1111/J.1751-1097.1984.Tb05359.X |
0.748 |
|
| 1984 |
de Grip W, Gillespie J, Rothschild K. FTIR study of rhodopsin recombinants: Evidence for protein conformational changes Vision Research. 24: 1694. DOI: 10.1016/0042-6989(84)90337-7 |
0.395 |
|
| 1983 |
Rothschild KJ, Cantore WA, Marrero H. Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching Science. 219: 1329-1330. DOI: 10.1126/Science.6828860 |
0.471 |
|
| 1983 |
Argade PV, Rothschild KJ. Quantitative analysis of resonance Raman spectra of purple membrane from Halobacterium halobium: L550 intermediate Biochemistry. 22: 3460-3466. DOI: 10.1021/Bi00283A024 |
0.369 |
|
| 1982 |
Rothschild KJ, Marrero H. Infrared evidence that the Schiff base of bacteriorhodopsin is protonated: bR570 and K intermediates Proceedings of the National Academy of Sciences of the United States of America. 79: 4045-4049. PMID 6955790 DOI: 10.1073/Pnas.79.13.4045 |
0.461 |
|
| 1982 |
Rothschild KJ, Argade PV, Earnest TN, Huang KS, London E, Liao MJ, Bayley H, Khorana HG, Herzfeld J. The site of attachment of retinal in bacteriorhodopsin. A resonance Raman study. The Journal of Biological Chemistry. 257: 8592-5. PMID 6807975 |
0.586 |
|
| 1982 |
Argade PV, Rothschild KJ. [76] Kinetic resonance raman spectroscopy of purple membrane using rotating sample Methods in Enzymology. 88: 643-648. DOI: 10.1016/0076-6879(82)88079-8 |
0.388 |
|
| 1982 |
Clark NA, Rothschild KJ. [42] Preparation of oriented multilamellar arrays of natural and artificial biological membranes Methods in Enzymology. 88: 326-333. DOI: 10.1016/0076-6879(82)88045-2 |
0.316 |
|
| 1981 |
Rothschild KJ, Zagaeski M, Cantore WA. Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy Biochemical and Biophysical Research Communications. 103: 483-489. PMID 7332553 DOI: 10.1016/0006-291X(81)90478-2 |
0.467 |
|
| 1981 |
Argade PV, Rothschild KJ, Kawamoto AH, Herzfeld J, Herlihy WC. Resonance Raman spectroscopy of specifically [epsilon-15N]lysine-labeled bacteriorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 78: 1643-6. PMID 6785758 DOI: 10.1073/Pnas.78.3.1643 |
0.599 |
|
| 1980 |
Hsiao TL, Rothschild KJ. Circular dichroism of oriented photoreceptor membrane film Biochemical and Biophysical Research Communications. 94: 618-624. PMID 7396925 DOI: 10.1016/0006-291X(80)91277-2 |
0.358 |
|
| 1980 |
Rothschild KJ, Clark NA, Rosen KM, Sanches R, Hsiao TL. Spectroscopic study of photoreceptor membrane incorporated into a multilamellar film Biochemical and Biophysical Research Communications. 92: 1266-1272. PMID 7370034 DOI: 10.1016/0006-291X(80)90423-4 |
0.341 |
|
| 1980 |
Rothschild KJ, DeGrip WJ, Sanches R. Fourier transform infrared study of photoreceptor membrane. I. Group assignments based on rhodopsin delipidation and reconstitution Bba - Biomembranes. 596: 338-351. PMID 7362819 DOI: 10.1016/0005-2736(80)90121-2 |
0.435 |
|
| 1980 |
Clark NA, Rothschild KJ, Luippold DA, Simon BA. Surface-induced lamellar orientation of multilayer membrane arrays. Theoretical analysis and a new method with application to purple membrane fragments Biophysical Journal. 31: 65-96. PMID 7272434 DOI: 10.1016/S0006-3495(80)85041-7 |
0.3 |
|
| 1980 |
Rothschild KJ, Sanches R, Hsiao TL, Clark NA. A spectroscopic study of rhodopsin alpha-helix orientation Biophysical Journal. 31: 53-64. PMID 7272433 DOI: 10.1016/S0006-3495(80)85040-5 |
0.326 |
|
| 1979 |
Rothschild KJ, Clark NA. Anomalous amide I infrared absorption of purple membrane Science. 204: 311-312. PMID 432645 DOI: 10.1126/Science.432645 |
0.351 |
|
| 1979 |
Rothschild KJ, Clark NA. Polarized infrared spectroscopy of oriented purple membrane Biophysical Journal. 25: 473-487. PMID 262400 DOI: 10.1016/S0006-3495(79)85317-5 |
0.379 |
|
| 1977 |
Rothschild KJ, Asher IM, Stanley HE, Anastassakis E. Raman spectroscopy of uncomplexed valinomycin. 2. Nonpolar and polar solution. Journal of the American Chemical Society. 99: 2032-9. PMID 864130 DOI: 10.1021/Ja00449A003 |
0.491 |
|
| 1977 |
Asher IM, Rothschild KJ, Anastassakis E, Stanley HE. Raman spectroscopy of uncomplexed valinomycin. I. The solid state. Journal of the American Chemical Society. 99: 2024-32. PMID 864129 DOI: 10.1002/Chin.197724046 |
0.443 |
|
| 1976 |
Rothschild KJ, Andrew JR, De Grip WJ, Stanley HE. Opsin structure probed by raman spectroscopy of photoreceptor membranes. Science (New York, N.Y.). 191: 1176-8. PMID 1257742 DOI: 10.1126/Science.1257742 |
0.532 |
|
| 1975 |
Rothschild KJ, Stanley HE. Models of ionic transport in biological membranes. Raman spectroscopy as a probe of valinomycin, gramidicin A, and rhodopsin conformations American Journal of Clinical Pathology. 63: 695-713. PMID 48337 DOI: 10.1093/Ajcp/63.5.695 |
0.459 |
|
| 1975 |
Stanley HE, Rothschild KJ, Asher IM, Phillies CDJ, Carew EB, Bansil R, Michaels IA. RESONANCE AND NON-RESONANCE RAMAN SPECTROSCOPY: A PROBE OF PEPTIDE AND PROTEIN CONFORMATION American Chemical Society, Polymer Preprints, Division of Polymer Chemistry. 16: var pagings. |
0.595 |
|
| 1974 |
Asher IM, Rothschild KJ, Stanley HE. Raman spectroscopic study of the valinomycin--KSCN complex. Journal of Molecular Biology. 89: 205-22. PMID 4444048 DOI: 10.1016/0022-2836(74)90171-5 |
0.429 |
|
| 1974 |
Rothschild KJ, Stanley HE. Raman spectroscopic investigation of gramicidin A' conformations Science. 185: 616-618. PMID 4135320 DOI: 10.1126/Science.185.4151.616 |
0.438 |
|
| 1973 |
Rothschild KJ, Asher IM, Anastassakis E, Stanley HE. Raman spectroscopic evidence for two conformations of uncomplexed valinomycin in the solid state. Science (New York, N.Y.). 182: 384-6. PMID 4755634 DOI: 10.1126/Science.182.4110.384 |
0.471 |
|
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