Recent Publications

Nagarajan S, Lapidus LJ. “Fluorescent Probe DCVJ Shows High Sensitivity for Characterization of Amyloid Β-Peptide Early in the Lag Phase.” Chembiochem. (2017) Nov 16;18(22):2205-2211. doi: 10.1002/cbic.201700387

Lapidus LJ. “Protein unfolding mechanisms and their effects on folding experiments.” F1000Res. (2017) Sep 22;6:1723. doi: 10.12688/f1000research.12070.1

Srivastava KR, Lapidus LJ. “Prion protein dynamics before aggregation.” Proc Natl Acad Sci U S A. (2017) Mar 20. pii: 201620400. doi: 10.1073/pnas.1620400114

Dutta G, Nagarajan S, Lapidus LJ, Lillehoj PB. “Enzyme-free electrochemical immunosensor based on methylene blue and the electro-oxidation of hydrazine on Pt nanoparticles.” Biosens Bioelectron. (2016) Nov 3. pii: S0956-5663(16)31136-8. doi: 10.1016/j.bios.2016.10.094

Acharya S, Srivastava KR, Nagarajan S, Lapidus LJ. “Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.” Chemphyschem. (2016) Aug 4;. doi:10.1002/cphc.201600706

Srivastava KR, French KC, Tzul FO, Makhatadze GI, Lapidus LJ. “Intramolecular diffusion controls aggregation of the PAPf39 peptide.” Biophys Chem. (2016) Sep;216:37-43. doi:10.1016/j.bpc.2016.06.004

Acharya S, Saha S, Ahmad B, Lapidus LJ. “Effects of Mutations on the Reconfiguration Rate of ?-Synuclein.” J Phys Chem B. (2015) Dec 17;119(50):15443-50. doi:10.1021/acs.jpcb.5b10136

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.” Biophys J. (2014) Aug 19;107(4):947-55. doi:10.1016/j.bpj.2014.06.037

Acharya S, Safaie BM, Wongkongkathep P, Ivanova MI, Attar A, Klärner FG, Schrader T, Loo JA, Bitan G, Lapidus LJ. “Molecular basis for preventing ?-synuclein aggregation by a molecular tweezer.” J Biol Chem. (2014) Apr 11;289(15):10727-37. doi:10.1074/jbc.M113.524520

Zhu L, Kurt N, Choi J, Lapidus LJ, Cavagnero S. “Sub-millisecond chain collapse of the Escherichia coli globin ApoHmpH.” J Phys Chem B. (2013) Jul 3;117(26):7868-77. doi:10.1021/jp400174e

Wu L, Lapidus LJ. “Combining ultrarapid mixing with photochemical oxidation to probe protein folding.” Anal Chem. (2013) May 21;85(10):4920-4. doi:10.1021/ac3033646

Lapidus LJ. “Exploring the top of the protein folding funnel by experiment.” Curr Opin Struct Biol. (2013) Feb;23(1):30-5. doi:10.1016/j.sbi.2012.10.003

Lapidus LJ. “Understanding protein aggregation from the view of monomer dynamics.” Mol Biosyst. (2013) Jan 27;9(1):29-35. doi:10.1039/c2mb25334h

Waldauer SA, Wu L, Yao S, Bakajin O, Lapidus LJ. “Microfluidic mixers for studying protein folding.” J Vis Exp. (2012) Apr 10;. doi:10.3791/3976

Ahmad B, Chen Y, Lapidus LJ. “Aggregation of ?-synuclein is kinetically controlled by intramolecular diffusion.” Proc Natl Acad Sci U S A. (2012) Feb 14;109(7):2336-41. doi:10.1073/pnas.1109526109

Ahmad B, Lapidus LJ. “Curcumin prevents aggregation in ?-synuclein by increasing reconfiguration rate.” J Biol Chem. (2012) Mar 16;287(12):9193-9. doi:10.1074/jbc.M111.325548

Zhu L, Ghosh K, King M, Cellmer T, Bakajin O, Lapidus LJ. “Evidence of multiple folding pathways for the villin headpiece subdomain.” J Phys Chem B. (2011) Nov 3;115(43):12632-7. doi:10.1021/jp206238y

Chen Y, Wedemeyer WJ, Lapidus LJ. “A general polymer model of unfolded proteins under folding conditions.” J Phys Chem B. (2010) Dec 9;114(48):15969-75. doi:10.1021/jp104746g

Waldauer SA, Bakajin O, Lapidus LJ. “Extremely slow intramolecular diffusion in unfolded protein L.” Proc Natl Acad Sci U S A. (2010) Aug 3;107(31):13713-7. doi:10.1073/pnas.1005415107

Chen Y, Parrini C, Taddei N, Lapidus LJ. “Conformational properties of unfolded HypF-N.” J Phys Chem B. (2009) Dec 17;113(50):16209-13. doi:10.1021/jp904189b

DeCamp SJ, Naganathan AN, Waldauer SA, Bakajin O, Lapidus LJ. “Direct observation of downhill folding of lambda-repressor in a microfluidic mixer.” Biophys J. (2009) Sep 16;97(6):1772-7. doi:10.1016/j.bpj.2009.07.003

Saravanan RS, Slabaugh E, Singh VR, Lapidus LJ, Haas T, Brandizzi F. “The targeting of the oxysterol-binding protein ORP3a to the endoplasmic reticulum relies on the plant VAP33 homolog PVA12.” Plant J. (2009) Jun;58(5):817-30. doi:10.1111/j.1365-313X.2009.03815.x

Singh VR, Kopka M, Chen Y, Wedemeyer WJ, Lapidus LJ. “Dynamic similarity of the unfolded states of proteins L and G.” Biochemistry. (2007) Sep 4;46(35):10046-54. doi:10.1021/bi700270j

Lapidus LJ, Yao S, McGarrity KS, Hertzog DE, Tubman E, Bakajin O. “Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer.” Biophys J. (2007) Jul 1;93(1):218-24. doi:10.1529/biophysj.106.103077