Year |
Citation |
Score |
2022 |
Asamoto DK, Kozachenko IA, López-Peña I, Kim JE. Corrigendum to "Bimolecular quenching of tryptophan fluorescence in a membrane protein: Evolution of local solvation and environment during folding into a bilayer" [Spectrochim. Acta Part A: Mol. Biomol. Spectrosc. 260 (2021) 119919]. Spectrochimica Acta. Part a, Molecular and Biomolecular Spectroscopy. 274: 121093. PMID 35305521 DOI: 10.1016/j.saa.2022.121093 |
0.337 |
|
2019 |
Asamoto DK, Kang G, Kim JE. Folding of the β-Barrel Membrane Protein OmpA into Nanodiscs. Biophysical Journal. PMID 31843264 DOI: 10.1016/J.Bpj.2019.11.3381 |
0.82 |
|
2019 |
Rivera JJ, Liang JH, Shimamura GR, Shafaat HS, Kim JE. Raman and Quantum Yield Studies of Trp48- in Azurin: Closed-Shell and Neutral Radical Species. The Journal of Physical Chemistry. B. PMID 31313925 DOI: 10.1021/Acs.Jpcb.9B04655 |
0.662 |
|
2019 |
Asamoto DK, Kim JE. UV Resonance Raman Spectroscopy as a Tool to Probe Membrane Protein Structure and Dynamics. Methods in Molecular Biology (Clifton, N.J.). 2003: 327-349. PMID 31218624 DOI: 10.1007/978-1-4939-9512-7_14 |
0.462 |
|
2016 |
Leigh BS, Monson KL, Kim JE. Visible and UV resonance Raman spectroscopy of the peroxide-based explosive HMTD and its photoproducts Forensic Chemistry. 2: 22-28. DOI: 10.1016/J.Forc.2016.08.002 |
0.352 |
|
2015 |
López-Peña I, Leigh BS, Schlamadinger DE, Kim JE. Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy. Biochemistry. PMID 26219819 DOI: 10.1021/Acs.Biochem.5B00514 |
0.762 |
|
2015 |
Larson BC, Pomponio JR, Shafaat HS, Kim RH, Leigh BS, Tauber MJ, Kim JE. Photogeneration and Quenching of Tryptophan Radical in Azurin. The Journal of Physical Chemistry. B. PMID 25625660 DOI: 10.1021/Jp511523Z |
0.729 |
|
2014 |
Shafaat HS, Kim JE. Resonance Raman Analysis of the Tryptophan Cation Radical. The Journal of Physical Chemistry Letters. 5: 3009-14. PMID 26278252 DOI: 10.1021/Jz5012324 |
0.687 |
|
2014 |
Mathews NR, Tarima S, Kim DG, Kim JE. Foveal contour changes following surgery for idiopathic epiretinal membrane. Investigative Ophthalmology & Visual Science. 55: 7754-60. PMID 25395487 DOI: 10.1167/Iovs.14-15075 |
0.324 |
|
2014 |
Armijo G, Okerblom J, Cauvi DM, Lopez V, Schlamadinger DE, Kim J, Arispe N, De Maio A. Interaction of heat shock protein 70 with membranes depends on the lipid environment. Cell Stress & Chaperones. 19: 877-86. PMID 24789271 DOI: 10.1007/S12192-014-0511-X |
0.753 |
|
2014 |
Shafaat HS, Kim JE. Resonance Raman analysis of the tryptophan cation radical Journal of Physical Chemistry Letters. 5: 3009-3014. DOI: 10.1021/jz5012324 |
0.622 |
|
2014 |
Kim J. Spectroscopic Studies of Membrane Protein Folding: Changes in Hydration Biophysical Journal. 106: 33a. DOI: 10.1016/J.Bpj.2013.11.256 |
0.471 |
|
2014 |
Kang G, Kim JE. Folding Dynamics and Molecular Interactions of Outer Membrane Protein A Biophysical Journal. 106: 265a. DOI: 10.1016/J.Bpj.2013.11.1552 |
0.826 |
|
2014 |
Leigh BS, Schlamadinger DE, Kim JE. Structures and Dynamics of Proteins Probed by UV Resonance Raman Spectroscopy Biophysical Methods For Biotherapeutics: Discovery and Development Applications. 243-268. DOI: 10.1002/9781118354698.ch9 |
0.728 |
|
2012 |
Schlamadinger DE, Leigh BS, Kim JE. UV resonance Raman study of TrpZip2 and related peptides: π-π interactions of tryptophan. Journal of Raman Spectroscopy : Jrs. 43: 1459-1464. PMID 25525290 DOI: 10.1002/Jrs.4061 |
0.734 |
|
2012 |
Schlamadinger DE, Wang Y, McCammon JA, Kim JE. Spectroscopic and computational study of melittin, cecropin A, and the hybrid peptide CM15. The Journal of Physical Chemistry. B. 116: 10600-8. PMID 22845179 DOI: 10.1021/Jp304021T |
0.749 |
|
2012 |
Wang Y, Schlamadinger DE, Kim JE, McCammon JA. Comparative molecular dynamics simulations of the antimicrobial peptide CM15 in model lipid bilayers. Biochimica Et Biophysica Acta. 1818: 1402-9. PMID 22387432 DOI: 10.1016/J.Bbamem.2012.02.017 |
0.732 |
|
2012 |
Kang G, López-Peña I, Oklejas V, Gary CS, Cao W, Kim JE. Förster resonance energy transfer as a probe of membrane protein folding. Biochimica Et Biophysica Acta. 1818: 154-61. PMID 21925139 DOI: 10.1016/J.Bbamem.2011.08.029 |
0.825 |
|
2012 |
Lopez-Pena I, Kang G, Oklejas V, Cao W, Kim JE. FRET Investigation of Membrane Protein Folding: Evolution of Tertiary Structure of Soluble and Transmembrane Domains during Folding into Synthetic Bilayers Biophysical Journal. 102: 471a. DOI: 10.1016/J.Bpj.2011.11.2583 |
0.807 |
|
2012 |
Okerblom J, Williams MR, Cauvi DM, Schlamadinger D, Kim J, Arispe N, De Maio A. The HSP70 Interaction with Phosphatidyl Serine on Membranes is the Initial Step its Release Into the Extracellular Medium Biophysical Journal. 102: 236a. DOI: 10.1016/J.Bpj.2011.11.1300 |
0.738 |
|
2011 |
Schlamadinger DE, Daschbach MM, Gokel GW, Kim JE. UV resonance Raman study of cation-π interactions in an indole crown ether. Journal of Raman Spectroscopy : Jrs. 42: 633-638. PMID 25635155 DOI: 10.1002/Jrs.2781 |
0.733 |
|
2011 |
Stoll S, Shafaat HS, Krzystek J, Ozarowski A, Tauber MJ, Kim JE, Britt RD. Hydrogen bonding of tryptophan radicals revealed by EPR at 700 GHz. Journal of the American Chemical Society. 133: 18098-101. PMID 22007694 DOI: 10.1021/Ja208462T |
0.743 |
|
2011 |
Macrae MX, Schlamadinger D, Kim JE, Mayer M, Yang J. Using charge to control the functional properties of self-assembled nanopores in membranes. Small (Weinheim An Der Bergstrasse, Germany). 7: 2016-20. PMID 21626687 DOI: 10.1002/Smll.201100394 |
0.698 |
|
2011 |
Schlamadinger DE, Kim JE. Thermodynamics of membrane protein folding measured by fluorescence spectroscopy. Journal of Visualized Experiments : Jove. PMID 21559004 DOI: 10.3791/2669 |
0.777 |
|
2011 |
Sanchez KM, Kang G, Wu B, Kim JE. Tryptophan-lipid interactions in membrane protein folding probed by ultraviolet resonance Raman and fluorescence spectroscopy. Biophysical Journal. 100: 2121-30. PMID 21539779 DOI: 10.1016/J.Bpj.2011.03.018 |
0.814 |
|
2010 |
Schlamadinger DE, Kats DI, Kim JE. Quenching of TryptophanFluorescence in Unfolded Cytochrome c: A Biophysics Experiment for Physical Chemistry Students. Journal of Chemical Education. 87: 961-964. PMID 25593364 DOI: 10.1021/Ed900029C |
0.732 |
|
2010 |
Shafaat HS, Leigh BS, Tauber MJ, Kim JE. Spectroscopic comparison of photogenerated tryptophan radicals in azurin: effects of local environment and structure. Journal of the American Chemical Society. 132: 9030-9. PMID 20536238 DOI: 10.1021/Ja101322G |
0.753 |
|
2010 |
Cogen AL, Yamasaki K, Muto J, Sanchez KM, Crotty Alexander L, Tanios J, Lai Y, Kim JE, Nizet V, Gallo RL. Staphylococcus epidermidis antimicrobial delta-toxin (phenol-soluble modulin-gamma) cooperates with host antimicrobial peptides to kill group A Streptococcus. Plos One. 5: e8557. PMID 20052280 DOI: 10.1371/Journal.Pone.0008557 |
0.728 |
|
2010 |
Cogen AL, Yamasaki K, Sanchez KM, Dorschner RA, Lai Y, MacLeod DT, Torpey JW, Otto M, Nizet V, Kim JE, Gallo RL. Selective antimicrobial action is provided by phenol-soluble modulins derived from Staphylococcus epidermidis, a normal resident of the skin. The Journal of Investigative Dermatology. 130: 192-200. PMID 19710683 DOI: 10.1038/Jid.2009.243 |
0.727 |
|
2010 |
Schlamadinger DE, Shafaat HS, Sanchez KM, Gable JE, Kim JE. Tryptophan residues as membrane protein anchors Aip Conference Proceedings. 1267: 170-171. DOI: 10.1063/1.3482447 |
0.8 |
|
2010 |
Kim JE, Shafaat HS, Leigh BS, Tauber MJ. Structural and Electronic Insights into Tryptophan Radicals in Proteins Biophysical Journal. 98: 565a. DOI: 10.1016/J.Bpj.2009.12.3064 |
0.758 |
|
2010 |
Kim JE, Sanchez KM, Schlamadinger DE, Gable JE, Wu B. Spectroscopic Study of Anchoring Aromatic Residues in Membrane Proteins and Peptides: Applications to Protein Folding and Vesicle Disruption Biophysical Journal. 98: 239a. DOI: 10.1016/J.Bpj.2009.12.1297 |
0.821 |
|
2009 |
Schlamadinger DE, Gable JE, Kim JE. Toxins and antimicrobial peptides: Interactions with membranes. Proceedings of Spie--the International Society For Optical Engineering. 7397. PMID 25593677 DOI: 10.1117/12.827439 |
0.73 |
|
2009 |
Gable JE, Schlamadinger DE, Cogen AL, Gallo RL, Kim JE. Fluorescence and UV resonance Raman study of peptide-vesicle interactions of human cathelicidin LL-37 and its F6W and F17W mutants. Biochemistry. 48: 11264-72. PMID 19894716 DOI: 10.1021/Bi900996Q |
0.762 |
|
2009 |
Schlamadinger DE, Gable JE, Kim JE. Hydrogen bonding and solvent polarity markers in the uv resonance raman spectrum of tryptophan: application to membrane proteins. The Journal of Physical Chemistry. B. 113: 14769-78. PMID 19817473 DOI: 10.1021/Jp905473Y |
0.756 |
|
2009 |
Tirrell TF, Paddock ML, Conlan AR, Smoll EJ, Nechushtai R, Jennings PA, Kim JE. Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal center. Biochemistry. 48: 4747-52. PMID 19388667 DOI: 10.1021/Bi900028R |
0.336 |
|
2009 |
Shafaat HS, Leigh BS, Tauber MJ, Kim JE. Resonance Raman characterization of a stable tryptophan radical in an azurin mutant. The Journal of Physical Chemistry. B. 113: 382-8. PMID 19072535 DOI: 10.1021/Jp809329A |
0.758 |
|
2009 |
Shafaat HS, Sanchez KM, Neary TJ, Kim JE. Ultraviolet resonance Raman spectroscopy of a β-sheet peptide: A model for membrane protein folding Journal of Raman Spectroscopy. 40: 1060-1064. DOI: 10.1002/Jrs.2237 |
0.816 |
|
2008 |
Sanchez KM, Schlamadinger DE, Gable JE, Kim JE. Förster Resonance Energy Transfer and Conformational Stability of Proteins: An Advanced Biophysical Module for Physical Chemistry Students. Journal of Chemical Education. 85: 1253-1256. PMID 19756254 DOI: 10.1021/Ed085P1253 |
0.797 |
|
2008 |
Sanchez KM, Gable JE, Schlamadinger DE, Kim JE. Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA. Biochemistry. 47: 12844-52. PMID 18991402 DOI: 10.1021/Bi800860K |
0.81 |
|
2008 |
Babakhani A, Gorfe AA, Kim JE, McCammon JA. Thermodynamics of peptide insertion and aggregation in a lipid bilayer. The Journal of Physical Chemistry. B. 112: 10528-34. PMID 18681475 DOI: 10.1021/Jp804710V |
0.401 |
|
2008 |
Sanchez KM, Neary TJ, Kim JE. Ultraviolet resonance Raman spectroscopy of folded and unfolded states of an integral membrane protein. The Journal of Physical Chemistry. B. 112: 9507-11. PMID 18588328 DOI: 10.1021/Jp800772J |
0.806 |
|
2007 |
Babakhani A, Gorfe AA, Gullingsrud J, Kim JE, Andrew McCammon J. Peptide insertion, positioning, and stabilization in a membrane: insight from an all-atom molecular dynamics simulation. Biopolymers. 85: 490-7. PMID 17274025 DOI: 10.1002/Bip.20698 |
0.383 |
|
2006 |
Kim JE, Arjara G, Richards JH, Gray HB, Winkler JR. Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. The Journal of Physical Chemistry. B. 110: 17656-62. PMID 16942111 DOI: 10.1021/Jp061991R |
0.777 |
|
2006 |
Lee JC, Kim JE, Pletneva EV, Faraone-Mennella J, Gray HB, Winkler JR. Protein folding, misfolding, and disease Metal Ions in Life Sciences. 1: 9-60. DOI: 10.1002/0470028114.ch2 |
0.761 |
|
2004 |
Kim JE, Pribisko MA, Gray HB, Winkler JR. Zinc-porphyrin Solvation in folded and unfolded states of Zn-cytochrome c. Inorganic Chemistry. 43: 7953-60. PMID 15578829 DOI: 10.1021/Ic048972L |
0.602 |
|
2003 |
Kim JE, Pan D, Mathies RA. Picosecond dynamics of G-protein coupled receptor activation in rhodopsin from time-resolved UV resonance Raman spectroscopy. Biochemistry. 42: 5169-75. PMID 12731857 DOI: 10.1021/Bi030026D |
0.554 |
|
2003 |
Kim JE, Tauber MJ, Mathies RA. Analysis of the mode-specific excited-state energy distribution and wavelength-dependent photoreaction quantum yield in rhodopsin. Biophysical Journal. 84: 2492-501. PMID 12668457 DOI: 10.1016/S0006-3495(03)75054-1 |
0.661 |
|
2002 |
McCamant DW, Kim JE, Mathies RA. Vibrational Relaxation in beta-Carotene Probed by Picosecond Stokes and Anti-Stokes Resonance Raman Spectroscopy. The Journal of Physical Chemistry. A. 106: 6030-8. PMID 17235377 DOI: 10.1021/Jp0203595 |
0.704 |
|
2002 |
Kim JE, Mathies RA. Anti-stokes Raman study of vibrational cooling dynamics in the primary photochemistry of rhodopsin. The Journal of Physical Chemistry. A. 106: 8508-15. PMID 16552447 DOI: 10.1021/Jp021069R |
0.513 |
|
2002 |
Pan D, Ganim Z, Kim JE, Verhoeven MA, Lugtenburg J, Mathies RA. Time-resolved resonance Raman analysis of chromophore structural changes in the formation and decay of rhodopsin's BSI intermediate. Journal of the American Chemical Society. 124: 4857-64. PMID 11971736 DOI: 10.1021/Ja012666E |
0.506 |
|
2001 |
Kim JE, McCamant DW, Zhu L, Mathies RA. Resonance Raman Structural Evidence that the Cis-to-Trans Isomerization in Rhodopsin Occurs in Femtoseconds. The Journal of Physical Chemistry. B. 105: 1240-9. PMID 16755302 DOI: 10.1021/Jp001236S |
0.741 |
|
2001 |
Kim JE, Tauber MJ, Mathies RA. Wavelength dependent cis-trans isomerization in vision. Biochemistry. 40: 13774-8. PMID 11705366 DOI: 10.1021/Bi0116137 |
0.638 |
|
1999 |
Zhu L, Kim J, Mathies RA. Picosecond time-resolved Raman system for studying photochemical reaction dynamics: application to the primary events in vision Journal of Raman Spectroscopy. 30: 777-783. DOI: 10.1002/(Sici)1097-4555(199909)30:9<777::Aid-Jrs449>3.0.Co;2-C |
0.504 |
|
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