Year |
Citation |
Score |
2022 |
Heo L, Gamage K, Valdes-Garcia G, Lapidus LJ, Feig M. Characterizing Transient Protein-Protein Interactions by Trp-Cys Quenching and Computer Simulations. The Journal of Physical Chemistry Letters. 10175-10182. PMID 36279257 DOI: 10.1021/acs.jpclett.2c02723 |
0.351 |
|
2022 |
Witalka D, Lapidus LJ. Measurement of Submillisecond Protein Folding Using Trp Fluorescence and Photochemical Oxidation. Methods in Molecular Biology (Clifton, N.J.). 2376: 135-142. PMID 34845607 DOI: 10.1007/978-1-0716-1716-8_7 |
0.346 |
|
2020 |
Lapidus LJ. The road less traveled in protein folding: evidence for multiple pathways. Current Opinion in Structural Biology. 66: 83-88. PMID 33220553 DOI: 10.1016/j.sbi.2020.10.012 |
0.402 |
|
2018 |
Woodard J, Srivastava KR, Rahamim G, Grupi A, Hogan S, Witalka DJ, Nawrocki G, Haas E, Feig M, Lapidus LJ. Intramolecular Diffusion in α-Synuclein: It Depends on How You Measure It. Biophysical Journal. PMID 30224053 DOI: 10.1016/J.Bpj.2018.08.023 |
0.406 |
|
2018 |
Izadi D, Chen Y, Whitmore ML, Slivka JD, Ching K, Lapidus LJ, Comstock MJ. Combined Force Ramp and Equilibrium High-Resolution Investigations Reveal Multi-Path Heterogeneous Unfolding of Protein G. The Journal of Physical Chemistry. B. PMID 30215523 DOI: 10.1021/acs.jpcb.8b06199 |
0.308 |
|
2018 |
Sgouralis I, Whitmore M, Lapidus L, Comstock MJ, Pressé S. Single molecule force spectroscopy at high data acquisition: A Bayesian nonparametric analysis. The Journal of Chemical Physics. 148: 123320. PMID 29604816 DOI: 10.1063/1.5008842 |
0.336 |
|
2017 |
Lapidus LJ. Protein unfolding mechanisms and their effects on folding experiments. F1000research. 6: 1723. PMID 29034084 DOI: 10.12688/f1000research.12070.1 |
0.4 |
|
2017 |
Collier TJ, Srivastava KR, Justman C, Grammatopoulous T, Hutter-Paier B, Prokesch M, Havas D, Rochet JC, Liu F, Jock K, de Oliveira P, Stirtz GL, Dettmer U, Sortwell CE, Feany MB, ... ... Lapidus L, et al. Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form. Neurobiology of Disease. PMID 28711409 DOI: 10.1016/J.Nbd.2017.07.007 |
0.302 |
|
2017 |
Srivastava KR, Lapidus LJ. Prion protein dynamics before aggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28320943 DOI: 10.1073/pnas.1620400114 |
0.381 |
|
2016 |
Acharya S, Srivastava KR, Nagarajan S, Lapidus LJ. Monomer dynamics of the Alzheimer peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27490673 DOI: 10.1002/Cphc.201600706 |
0.491 |
|
2015 |
Acharya S, Saha S, Ahmad B, Lapidus LJ. Effects of Mutations on the Reconfiguration Rate of α-Synuclein. The Journal of Physical Chemistry. B. 119: 15443-50. PMID 26572968 DOI: 10.1021/Acs.Jpcb.5B10136 |
0.536 |
|
2015 |
Acharya S, Lapidus LJ. Reconfiguration of the Alzheimer's Peptide Kinetically Controls Aggregation in Alzheimer's Disease Biophysical Journal. 108: 65a-66a. DOI: 10.1016/J.Bpj.2014.11.391 |
0.513 |
|
2015 |
Srivastava KR, Lapidus LJ. Aggregation Propensity of Prion is Kinetically Controlled by Intramolecular Diffusion of Protein Chain Biophysical Journal. 108: 46a. DOI: 10.1016/j.bpj.2014.11.285 |
0.369 |
|
2014 |
Lapidus LJ, Acharya S, Schwantes CR, Wu L, Shukla D, King M, DeCamp SJ, Pande VS. Complex pathways in folding of protein G explored by simulation and experiment. Biophysical Journal. 107: 947-55. PMID 25140430 DOI: 10.1016/J.Bpj.2014.06.037 |
0.623 |
|
2014 |
Acharya S, Safaie BM, Wongkongkathep P, Ivanova MI, Attar A, Klärner FG, Schrader T, Loo JA, Bitan G, Lapidus LJ. Molecular basis for preventing α-synuclein aggregation by a molecular tweezer. The Journal of Biological Chemistry. 289: 10727-37. PMID 24567327 DOI: 10.1074/Jbc.M113.524520 |
0.504 |
|
2013 |
Zhu L, Kurt N, Choi J, Lapidus LJ, Cavagnero S. Sub-millisecond chain collapse of the Escherichia coli globin ApoHmpH. The Journal of Physical Chemistry. B. 117: 7868-77. PMID 23750553 DOI: 10.1021/Jp400174E |
0.354 |
|
2013 |
Wu L, Lapidus LJ. Combining ultrarapid mixing with photochemical oxidation to probe protein folding. Analytical Chemistry. 85: 4920-4. PMID 23593999 DOI: 10.1021/ac3033646 |
0.382 |
|
2013 |
Lapidus LJ. Exploring the top of the protein folding funnel by experiment. Current Opinion in Structural Biology. 23: 30-5. PMID 23122360 DOI: 10.1016/j.sbi.2012.10.003 |
0.394 |
|
2012 |
Narayanan R, Zhu L, Velmurugu Y, Roca J, Kuznetsov SV, Prehna G, Lapidus LJ, Ansari A. Exploring the energy landscape of nucleic acid hairpins using laser temperature-jump and microfluidic mixing. Journal of the American Chemical Society. 134: 18952-63. PMID 23078026 DOI: 10.1021/Ja301218E |
0.343 |
|
2012 |
Voelz VA, Jäger M, Yao S, Chen Y, Zhu L, Waldauer SA, Bowman GR, Friedrichs M, Bakajin O, Lapidus LJ, Weiss S, Pande VS. Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment. Journal of the American Chemical Society. 134: 12565-77. PMID 22747188 DOI: 10.1021/Ja302528Z |
0.765 |
|
2012 |
Waldauer SA, Wu L, Yao S, Bakajin O, Lapidus LJ. Microfluidic mixers for studying protein folding. Journal of Visualized Experiments : Jove. PMID 22525257 DOI: 10.3791/3976 |
0.758 |
|
2012 |
Ahmad B, Chen Y, Lapidus LJ. Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion. Proceedings of the National Academy of Sciences of the United States of America. 109: 2336-41. PMID 22308332 DOI: 10.1073/pnas.1109526109 |
0.365 |
|
2011 |
Zhu L, Ghosh K, King M, Cellmer T, Bakajin O, Lapidus LJ. Evidence of multiple folding pathways for the villin headpiece subdomain. The Journal of Physical Chemistry. B. 115: 12632-7. PMID 21923150 DOI: 10.1021/Jp206238Y |
0.415 |
|
2011 |
Voelz VA, Jäger M, Zhu L, Yao S, Bakajin O, Weiss S, Lapidus LJ, Pande VS. Markov State Models of Millisecond Folder ACBP Reveals New Views of the Folding Reaction Biophysical Journal. 100: 515a. DOI: 10.1016/J.Bpj.2010.12.3015 |
0.423 |
|
2011 |
Zhu L, Voelz VA, Bakajin O, Pande VS, Lapidus LJ. Revealing the Early Events of ACBP Folding by Ultrarapid Mixing Biophysical Journal. 100: 396a. DOI: 10.1016/J.Bpj.2010.12.2353 |
0.442 |
|
2011 |
Chen Y, Voelz VA, Bakajin O, Pande VS, Lapidus LJ. Diffusion of Unfolded Acyl-Coenzyme A-Binding Protein Over a Complete Range of Denaturant Biophysical Journal. 100: 211a. DOI: 10.1016/J.Bpj.2010.12.1362 |
0.469 |
|
2010 |
Waldauer SA, Bakajin O, Lapidus LJ. Extremely slow intramolecular diffusion in unfolded protein L. Proceedings of the National Academy of Sciences of the United States of America. 107: 13713-7. PMID 20643973 DOI: 10.1073/Pnas.1005415107 |
0.754 |
|
2010 |
Voelz VA, Singh VR, Wedemeyer WJ, Lapidus LJ, Pande VS. Unfolded-state dynamics and structure of protein L characterized by simulation and experiment. Journal of the American Chemical Society. 132: 4702-9. PMID 20218718 DOI: 10.1021/Ja908369H |
0.43 |
|
2010 |
DeCamp SJ, Waldauer SA, Bakajin O, Lapidus LJ. Circular Dichroism Measurements in a Microfluidic Serpentine Mixer Biophysical Journal. 98: 446a. DOI: 10.1016/J.Bpj.2009.12.2423 |
0.747 |
|
2010 |
Zhu L, Bakajin O, Lapidus L. Direct Observation of Villin Folding in a Microfluidic Mixer Biophysical Journal. 98: 445a. DOI: 10.1016/J.Bpj.2009.12.2421 |
0.538 |
|
2010 |
Lapidus LJ, Chen Y, Singh VR, Waldauer SA, Buscarino E, Voelz VA, Pande VS. Connecting Unfolded Protein Dynamics and Aggregation Biophysical Journal. 98: 257a. DOI: 10.1016/J.Bpj.2009.12.1396 |
0.753 |
|
2009 |
Chen Y, Parrini C, Taddei N, Lapidus LJ. Conformational properties of unfolded HypF-N. The Journal of Physical Chemistry. B. 113: 16209-13. PMID 19928868 DOI: 10.1021/jp904189b |
0.427 |
|
2009 |
DeCamp SJ, Naganathan AN, Waldauer SA, Bakajin O, Lapidus LJ. Direct observation of downhill folding of lambda-repressor in a microfluidic mixer. Biophysical Journal. 97: 1772-7. PMID 19751683 DOI: 10.1016/J.Bpj.2009.07.003 |
0.761 |
|
2009 |
Chen Y, Lapidus L. Intramolecular Diffusion of the Amyloidgenic Protein HypF Biophysical Journal. 96: 89a. DOI: 10.1016/J.Bpj.2008.12.367 |
0.489 |
|
2009 |
DeCamp S, Waldauer SA, Lapidus LJ. Exploring the Folding Landscape of Lambda Repressor with Microfluidic Mixing Biophysical Journal. 96: 589a. DOI: 10.1016/J.Bpj.2008.12.3083 |
0.728 |
|
2009 |
Waldauer SA, Kane A, Bakajin O, Lapidus L. Measuring Intramolecular Diffusion During Protein Folding Using an Ultrarapid Microfluidic Mixer Biophysical Journal. 96: 589a. DOI: 10.1016/J.Bpj.2008.12.3082 |
0.753 |
|
2009 |
Singh V, Chen Y, Wedemeyer B, Lapidus L. Dynamics and Statistical Properties of Disordered Proteins Biophysical Journal. 96: 68a. DOI: 10.1016/J.Bpj.2008.12.254 |
0.519 |
|
2008 |
Waldauer SA, Bakajin O, Ball T, Chen Y, Decamp SJ, Kopka M, Jäger M, Singh VR, Wedemeyer WJ, Weiss S, Yao S, Lapidus LJ. Ruggedness in the folding landscape of protein L. Hfsp Journal. 2: 388-95. PMID 19436489 DOI: 10.2976/1.3013702 |
0.771 |
|
2008 |
Singh VR, Lapidus LJ. The intrinsic stiffness of polyglutamine peptides. The Journal of Physical Chemistry. B. 112: 13172-6. PMID 18817433 DOI: 10.1021/jp805636p |
0.325 |
|
2007 |
Singh VR, Kopka M, Chen Y, Wedemeyer WJ, Lapidus LJ. Dynamic similarity of the unfolded states of proteins L and G. Biochemistry. 46: 10046-54. PMID 17685556 DOI: 10.1021/bi700270j |
0.447 |
|
2007 |
Lapidus LJ, Yao S, McGarrity KS, Hertzog DE, Tubman E, Bakajin O. Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer. Biophysical Journal. 93: 218-24. PMID 17416618 DOI: 10.1529/Biophysj.106.103077 |
0.349 |
|
2006 |
Buscaglia M, Lapidus LJ, Eaton WA, Hofrichter J. Effects of denaturants on the dynamics of loop formation in polypeptides. Biophysical Journal. 91: 276-88. PMID 16617069 DOI: 10.1529/Biophysj.105.071167 |
0.365 |
|
2003 |
Sadqi M, Lapidus LJ, Muñoz V. How fast is protein hydrophobic collapse? Proceedings of the National Academy of Sciences of the United States of America. 100: 12117-22. PMID 14530404 DOI: 10.1073/Pnas.2033863100 |
0.448 |
|
2003 |
Buscaglia M, Schuler B, Lapidus LJ, Eaton WA, Hofrichter J. Kinetics of intramolecular contact formation in a denatured protein. Journal of Molecular Biology. 332: 9-12. PMID 12946342 DOI: 10.1016/S0022-2836(03)00891-X |
0.412 |
|
2002 |
Lapidus LJ, Steinbach PJ, Eaton WA, Szabo A, Hofrichter J. Effects of chain stiffness on the dynamics of loop formation in polypeptides. Appendix: Testing a 1-dimensional diffusion model for peptide dynamics Journal of Physical Chemistry B. 106: 11628-11640. DOI: 10.1021/Jp020829V |
0.318 |
|
2001 |
Lapidus LJ, Eaton WA, Hofrichter J. Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. Physical Review Letters. 87: 258101. PMID 11736610 DOI: 10.1103/Physrevlett.87.258101 |
0.323 |
|
2000 |
Eaton WA, Muñoz V, Hagen SJ, Jas GS, Lapidus LJ, Henry ER, Hofrichter J. Fast kinetics and mechanisms in protein folding. Annual Review of Biophysics and Biomolecular Structure. 29: 327-59. PMID 10940252 DOI: 10.1146/Annurev.Biophys.29.1.327 |
0.44 |
|
1999 |
Lapidus LJ, Enzer D, Gabrielse G. Stochastic phase switching of a parametrically driven electron in a penning trap Physical Review Letters. 83: 899-902. DOI: 10.1103/Physrevlett.83.899 |
0.493 |
|
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