| Year |
Citation |
Score |
| 2024 |
Ali A, Holman AP, Rodriguez A, Matveyenka M, Kurouski D. Tubulin-binding region alters tau-lipid interactions and changes toxicity of tau fibrils formed in the presence of phosphatidylserine lipids. Protein Science : a Publication of the Protein Society. 33: e5078. PMID 38895991 DOI: 10.1002/pro.5078 |
0.348 |
|
| 2024 |
Zhaliazka K, Kurouski D. Elucidation of molecular mechanisms by which amyloid β fibrils exert cell toxicity. Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids. 1869: 159510. PMID 38759921 DOI: 10.1016/j.bbalip.2024.159510 |
0.345 |
|
| 2024 |
Sitton J, Ali A, Osborne L, Holman AP, Rodriguez A, Kurouski D. Plasmalogens Alter the Aggregation Rate of Transthyretin and Lower Toxicity of Transthyretin Fibrils. The Journal of Physical Chemistry Letters. 4761-4766. PMID 38661515 DOI: 10.1021/acs.jpclett.4c00868 |
0.325 |
|
| 2024 |
Ali A, Dou T, Holman AP, Hung A, Osborne L, Pickett D, Rodriguez A, Zhaliazka K, Kurouski D. The influence of zwitterionic and anionic phospholipids on protein aggregation. Biophysical Chemistry. 306: 107174. PMID 38211368 DOI: 10.1016/j.bpc.2024.107174 |
0.333 |
|
| 2023 |
Zhaliazka K, Kurouski D. Nano-infrared analysis of amyloid β fibrils formed in the presence of lipids with unsaturated fatty acids. Nanoscale. 15: 19650-19657. PMID 38019134 DOI: 10.1039/d3nr05184f |
0.315 |
|
| 2023 |
Rodriguez A, Ali A, Holman AP, Dou T, Zhaliazka K, Kurouski D. Nanoscale Structural Characterization of Transthyretin Aggregates Formed at Different Time Points of Protein Aggregation Using Atomic Force Microscopy-Infrared Spectroscopy. Protein Science : a Publication of the Protein Society. e4838. PMID 37967043 DOI: 10.1002/pro.4838 |
0.394 |
|
| 2023 |
Ali A, Zhaliazka K, Holman AP, Kurouski D. Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid. Proteins. PMID 37909765 DOI: 10.1002/prot.26622 |
0.382 |
|
| 2023 |
Ali A, Zhaliazka K, Dou T, Holman AP, Kurouski D. Saturation of fatty acids in phosphatidic acid uniquely alters transthyretin stability changing morphology and toxicity of amyloid fibrils. Chemistry and Physics of Lipids. 257: 105350. PMID 37858615 DOI: 10.1016/j.chemphyslip.2023.105350 |
0.325 |
|
| 2023 |
Kurouski D. Elucidating the Role of Lipids in the Aggregation of Amyloidogenic Proteins. Accounts of Chemical Research. 56: 2898-2906. PMID 37824095 DOI: 10.1021/acs.accounts.3c00386 |
0.362 |
|
| 2023 |
Ali A, Zhaliazka K, Dou T, Holman AP, Kumar R, Kurouski D. Secondary structure and toxicity of transthyretin fibrils can be altered by unsaturated fatty acids. International Journal of Biological Macromolecules. 253: 127241. PMID 37804888 DOI: 10.1016/j.ijbiomac.2023.127241 |
0.321 |
|
| 2023 |
Joshi R, Zhaliazka K, Holman AP, Kurouski D. Elucidation of the Role of Lipids in Late Endosomes on the Aggregation of Insulin. Acs Chemical Neuroscience. 14: 3551-3559. PMID 37682720 DOI: 10.1021/acschemneuro.3c00475 |
0.342 |
|
| 2023 |
Frese A, Goode C, Zhaliazka K, Holman AP, Dou T, Kurouski D. Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils. Protein Science : a Publication of the Protein Society. 32: e4717. PMID 37402649 DOI: 10.1002/pro.4717 |
0.361 |
|
| 2023 |
Matveyenka M, Zhaliazka K, Kurouski D. Unsaturated fatty acids uniquely alter aggregation rate of α-synuclein and insulin and change the secondary structure and toxicity of amyloid aggregates formed in their presence. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 37: e22972. PMID 37302013 DOI: 10.1096/fj.202300003R |
0.384 |
|
| 2023 |
Zhaliazka K, Serada V, Matveyenka M, Rizevsky S, Kurouski D. Protein-to-lipid ratio uniquely changes the rate of lysozyme aggregation but does not significantly alter toxicity of mature protein aggregates. Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids. 1868: 159305. PMID 36907244 DOI: 10.1016/j.bbalip.2023.159305 |
0.314 |
|
| 2023 |
Zhaliazka K, Kurouski D. Nanoscale Imaging of Individual Amyloid Aggregates Extracted from Brains of Alzheimer- and Parkinson Patients Reveals Presence of Lipids in α-Synuclein but not in Amyloid β1-42 Fibrils. Protein Science : a Publication of the Protein Society. e4598. PMID 36823759 DOI: 10.1002/pro.4598 |
0.35 |
|
| 2023 |
Zhaliazka K, Matveyenka M, Kurouski D. Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1-42 aggregates. The Febs Journal. PMID 36705524 DOI: 10.1111/febs.16738 |
0.345 |
|
| 2022 |
Matveyenka M, Rizevsky S, Pellois JP, Kurouski D. Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates. Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids. 1868: 159247. PMID 36272517 DOI: 10.1016/j.bbalip.2022.159247 |
0.371 |
|
| 2022 |
Zhaliazka K, Kurouski D. Nanoscale Characterization of Parallel and Antiparallel β-Sheet Amyloid Beta 1-42 Aggregates. Acs Chemical Neuroscience. 13: 2813-2820. PMID 36122250 DOI: 10.1021/acschemneuro.2c00180 |
0.389 |
|
| 2022 |
Matveyenka M, Zhaliazka K, Rizevsky S, Kurouski D. Lipids uniquely alter secondary structure and toxicity of lysozyme aggregates. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 36: e22543. PMID 36094052 DOI: 10.1096/fj.202200841R |
0.33 |
|
| 2022 |
Matveyenka M, Rizevsky S, Kurouski D. Amyloid aggregates exert cell toxicity causing irreversible damages in the endoplasmic reticulum. Biochimica Et Biophysica Acta. Molecular Basis of Disease. 1868: 166485. PMID 35840040 DOI: 10.1016/j.bbadis.2022.166485 |
0.308 |
|
| 2022 |
Rizevsky S, Zhaliazka K, Matveyenka M, Quinn K, Kurouski D. Lipids reverse supramolecular chirality and reduce toxicity of amyloid fibrils. The Febs Journal. PMID 35736671 DOI: 10.1111/febs.16564 |
0.398 |
|
| 2022 |
Matveyenka M, Rizevsky S, Kurouski D. Unsaturation in the Fatty Acids of Phospholipids Drastically Alters the Structure and Toxicity of Insulin Aggregates Grown in Their Presence. The Journal of Physical Chemistry Letters. 13: 4563-4569. PMID 35580189 DOI: 10.1021/acs.jpclett.2c00559 |
0.363 |
|
| 2022 |
Matveyenka M, Rizevsky S, Kurouski D. The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates. Febs Letters. 596: 1424-1433. PMID 35510803 DOI: 10.1002/1873-3468.14369 |
0.33 |
|
| 2022 |
Rizevsky S, Matveyenka M, Kurouski D. Nanoscale Structural Analysis of a Lipid-Driven Aggregation of Insulin. The Journal of Physical Chemistry Letters. 13: 2467-2473. PMID 35266717 DOI: 10.1021/acs.jpclett.1c04012 |
0.359 |
|
| 2020 |
Dou T, Li Z, Zhang J, Evilevitch A, Kurouski D. Nanoscale Structural Characterization of Individual Viral Particles Using Atomic Force Microscope Infrared (AFM-IR) and Tip-Enhanced Raman Spectroscopy (TERS). Analytical Chemistry. PMID 32683857 DOI: 10.1021/Acs.Analchem.0C01971 |
0.353 |
|
| 2020 |
Zhou L, Kurouski D. Structural Characterization of Individual α-Synuclein Oligomers Formed at Different Stages of Protein Aggregation by Atomic Force Microscope Infrared Spectroscopy. Analytical Chemistry. PMID 32347706 DOI: 10.1021/acs.analchem.0c00593 |
0.349 |
|
| 2020 |
Sanchez L, Ermolenkov A, Tang XT, Tamborindeguy C, Kurouski D. Non-invasive diagnostics of Liberibacter disease on tomatoes using a hand-held Raman spectrometer. Planta. 251: 64. PMID 32048047 DOI: 10.1007/S00425-020-03359-5 |
0.303 |
|
| 2020 |
Lee K, Yarbrough D, Kozman MM, Herrman TJ, Park J, Wang R, Kurouski D. Rapid detection and prediction of chlortetracycline and oxytetracycline in animal feed using surface-enhanced Raman spectroscopy (SERS) Food Control. 114: 107243. DOI: 10.1016/J.Foodcont.2020.107243 |
0.302 |
|
| 2019 |
Rizevsky S, Kurouski D. Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed By Atomic Force Microscope Infrared Spectroscopy (AFM-IR). Chembiochem : a European Journal of Chemical Biology. PMID 31299124 DOI: 10.1002/Cbic.201900394 |
0.537 |
|
| 2019 |
Farber C, Shires M, Ong K, Byrne D, Kurouski D. Raman spectroscopy as an early detection tool for rose rosette infection. Planta. PMID 31222494 DOI: 10.1007/S00425-019-03216-0 |
0.314 |
|
| 2019 |
Farber C, Wang R, Chemelewski R, Mullet J, Kurouski D. Nanoscale Structural Organization of Plant Epicuticular Wax Probed by Atomic Force Microscope Infrared Spectroscopy. Analytical Chemistry. PMID 30624904 DOI: 10.1021/Acs.Analchem.8B05294 |
0.326 |
|
| 2018 |
Egging V, Nguyen J, Kurouski D. Detection and Identification of Fungal Infections in Intact Wheat and Sorghum Grain Using a Hand-Held Raman Spectrometer. Analytical Chemistry. PMID 29898358 DOI: 10.1021/Acs.Analchem.8B01863 |
0.31 |
|
| 2018 |
Farber C, Kurouski D. Detection and Identification of Plant Pathogens on Maize Kernels with a Handheld Raman Spectrometer. Analytical Chemistry. PMID 29461798 DOI: 10.1021/Acs.Analchem.8B00222 |
0.315 |
|
| 2017 |
Kurouski D. Advances of Vibrational Circular Dichroism (VCD) in bioanalytical chemistry. A review. Analytica Chimica Acta. 990: 54-66. PMID 29029743 DOI: 10.1016/J.Aca.2017.08.014 |
0.377 |
|
| 2017 |
Kurouski D, Large N, Chiang N, Henry A, Seideman T, Schatz GC, Van Duyne RP. Unraveling the Near- and Far-Field Relationship of 2D Surface-Enhanced Raman Spectroscopy Substrates Using Wavelength-Scan Surface-Enhanced Raman Excitation Spectroscopy The Journal of Physical Chemistry C. 121: 14737-14744. DOI: 10.1021/Acs.Jpcc.7B04787 |
0.324 |
|
| 2016 |
Deckert-Gaudig T, Kurouski D, Hedegaard MA, Singh P, Lednev IK, Deckert V. Spatially resolved spectroscopic differentiation of hydrophilic and hydrophobic domains on individual insulin amyloid fibrils. Scientific Reports. 6: 33575. PMID 27650589 DOI: 10.1038/Srep33575 |
0.664 |
|
| 2016 |
Breydo L, Kurouski D, Rasool S, Milton S, Wu JW, Uversky VN, Lednev IK, Glabe CG. Structural differences between amyloid beta oligomers. Biochemical and Biophysical Research Communications. PMID 27363332 DOI: 10.1016/J.Bbrc.2016.06.122 |
0.616 |
|
| 2016 |
Kurouski D. Advances of tip-enhanced Raman spectroscopy (TERS) in electrochemistry, biochemistry, and surface science Vibrational Spectroscopy. DOI: 10.1016/J.Vibspec.2016.06.004 |
0.322 |
|
| 2016 |
Jiang N, Kurouski D, Pozzi EA, Chiang N, Hersam MC, Van Duyne RP. Tip-enhanced Raman spectroscopy: From concepts to practical applications Chemical Physics Letters. 659: 16-24. DOI: 10.1016/J.Cplett.2016.06.035 |
0.36 |
|
| 2015 |
Kurouski D, Van Duyne RP, Lednev IK. Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review. The Analyst. PMID 26042229 DOI: 10.1039/C5An00342C |
0.686 |
|
| 2015 |
Shanmugasundaram M, Kurouski D, Wan W, Stubbs G, Dukor RK, Nafie LA, Lednev IK. Rapid Filament Supramolecular Chirality Reversal of HET-s (218-289) Prion Fibrils Driven by pH Elevation. The Journal of Physical Chemistry. B. 119: 8521-5. PMID 26023710 DOI: 10.1021/Acs.Jpcb.5B04779 |
0.667 |
|
| 2015 |
Kurouski D, Van Duyne RP. In situ detection and identification of hair dyes using surface-enhanced Raman spectroscopy (SERS). Analytical Chemistry. 87: 2901-6. PMID 25635868 DOI: 10.1021/Ac504405U |
0.309 |
|
| 2015 |
Rosario-Alomar MF, Quiñones-Ruiz T, Kurouski D, Sereda V, Ferreira EB, Jesús-Kim LD, Hernández-Rivera S, Zagorevski DV, López-Garriga J, Lednev IK. Hydrogen sulfide inhibits amyloid formation. The Journal of Physical Chemistry. B. 119: 1265-74. PMID 25545790 DOI: 10.1021/Jp508471V |
0.651 |
|
| 2015 |
Kurouski D, Handen JD, Dukor RK, Nafie LA, Lednev IK. Supramolecular chirality in peptide microcrystals. Chemical Communications (Cambridge, England). 51: 89-92. PMID 25351531 DOI: 10.1039/C4Cc05002A |
0.624 |
|
| 2015 |
Shanmugasundaram M, Kurouski D, Wan W, Stubbs G, Dukor RK, Nafie LA, Lednev IK. Rapid Filament Supramolecular Chirality Reversal of HET-s (218-289) Prion Fibrils Driven by pH Elevation Journal of Physical Chemistry B. 119: 8521-8525. DOI: 10.1021/acs.jpcb.5b04779 |
0.541 |
|
| 2014 |
Kurouski D, Lu X, Popova L, Wan W, Shanmugasundaram M, Stubbs G, Dukor RK, Lednev IK, Nafie LA. Is supramolecular filament chirality the underlying cause of major morphology differences in amyloid fibrils? Journal of the American Chemical Society. 136: 2302-12. PMID 24484302 DOI: 10.1021/Ja407583R |
0.748 |
|
| 2014 |
Kurouski D, Deckert-Gaudig T, Deckert V, Lednev IK. Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS). Biophysical Journal. 106: 263-71. PMID 24411258 DOI: 10.1016/J.Bpj.2013.10.040 |
0.677 |
|
| 2014 |
Kurouski D, Sorci M, Postiglione T, Belfort G, Lednev IK. Detection and structural characterization of insulin prefibrilar oligomers using surface enhanced Raman spectroscopy Biotechnology Progress. 30: 488-495. PMID 24376182 DOI: 10.1002/Btpr.1852 |
0.669 |
|
| 2013 |
Kurouski D, Luo H, Sereda V, Robb FT, Lednev IK. Deconstruction of stable cross-Beta fibrillar structures into toxic and nontoxic products using a mutated archaeal chaperonin. Acs Chemical Biology. 8: 2095-101. PMID 23875676 DOI: 10.1021/Cb400238A |
0.648 |
|
| 2013 |
Bhat V, Olenick MB, Schuchardt BJ, Mikles DC, Deegan BJ, McDonald CB, Seldeen KL, Kurouski D, Faridi MH, Shareef MM, Gupta V, Lednev IK, Farooq A. Heat-induced fibrillation of BclXL apoptotic repressor. Biophysical Chemistry. 179: 12-25. PMID 23714425 DOI: 10.1016/J.Bpc.2013.04.002 |
0.639 |
|
| 2013 |
Kurouski D, Kar K, Wetzel R, Dukor RK, Lednev IK, Nafie LA. Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism. Febs Letters. 587: 1638-43. PMID 23583713 DOI: 10.1016/J.Febslet.2013.03.038 |
0.636 |
|
| 2013 |
McDonald CB, Bhat V, Kurouski D, Mikles DC, Deegan BJ, Seldeen KL, Lednev IK, Farooq A. Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factor. Biophysical Chemistry. 175: 54-62. PMID 23528987 DOI: 10.1016/J.Bpc.2013.02.008 |
0.543 |
|
| 2013 |
Kurouski D, Postiglione T, Deckert-Gaudig T, Deckert V, Lednev IK. Amide I vibrational mode suppression in surface (SERS) and tip (TERS) enhanced Raman spectra of protein specimens. The Analyst. 138: 1665-73. PMID 23330149 DOI: 10.1039/C2An36478F |
0.586 |
|
| 2013 |
Srinivasan S, Patke S, Wang Y, Ye Z, Litt J, Srivastava SK, Lopez MM, Kurouski D, Lednev IK, Kane RS, Colón W. Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2. The Journal of Biological Chemistry. 288: 2744-55. PMID 23223242 DOI: 10.1074/Jbc.M112.394155 |
0.657 |
|
| 2013 |
Lednev IK, Kurouski D. 146 Amyloid fibril polymorphism probed by advanced vibrational spectroscopy Journal of Biomolecular Structure and Dynamics. 31: 94-95. DOI: 10.1080/07391102.2013.786388 |
0.663 |
|
| 2013 |
Kurouski D, Deckert-Gaudig T, Deckert V, Lednev IK. Structural Characterization of Insulin Fibril Surfaces using Tip Enhanced Raman Spectroscopy (TERS) Biophysical Journal. 104: 49a. DOI: 10.1016/J.Bpj.2012.11.311 |
0.666 |
|
| 2012 |
Bhat V, Kurouski D, Olenick MB, McDonald CB, Mikles DC, Deegan BJ, Seldeen KL, Lednev IK, Farooq A. Acidic pH promotes oligomerization and membrane insertion of the BclXL apoptotic repressor. Archives of Biochemistry and Biophysics. 528: 32-44. PMID 22960132 DOI: 10.1016/J.Abb.2012.08.009 |
0.526 |
|
| 2012 |
Kurouski D, Dukor RK, Lu X, Nafie LA, Lednev IK. Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure. Biophysical Journal. 103: 522-31. PMID 22947868 DOI: 10.1016/J.Bpj.2012.04.042 |
0.671 |
|
| 2012 |
Kurouski D, Deckert-Gaudig T, Deckert V, Lednev IK. Structure and composition of insulin fibril surfaces probed by TERS. Journal of the American Chemical Society. 134: 13323-9. PMID 22813355 DOI: 10.1021/Ja303263Y |
0.655 |
|
| 2012 |
Kurouski D, Washington J, Ozbil M, Prabhakar R, Shekhtman A, Lednev IK. Disulfide bridges remain intact while native insulin converts into amyloid fibrils. Plos One. 7: e36989. PMID 22675475 DOI: 10.1371/Journal.Pone.0036989 |
0.656 |
|
| 2012 |
Kurouski D, Luo H, Sereda V, Robb FT, Lednev IK. Rapid degradation kinetics of amyloid fibrils under mild conditions by an archaeal chaperonin. Biochemical and Biophysical Research Communications. 422: 97-102. PMID 22564742 DOI: 10.1016/J.Bbrc.2012.04.113 |
0.649 |
|
| 2012 |
Kurouski D, Dukor RK, Lu X, Nafie LA, Lednev IK. Spontaneous inter-conversion of insulin fibril chirality. Chemical Communications (Cambridge, England). 48: 2837-9. PMID 22241279 DOI: 10.1039/C2Cc16895B |
0.658 |
|
| 2012 |
Kurouski D, Lauro W, Dukor RK, Lu X, Lombardi RA, Nafie LA, Lednev IK. Evaluation of the Amyloid Fibril Stability Biophysical Journal. 102: 256a. DOI: 10.1016/J.Bpj.2011.11.1410 |
0.668 |
|
| 2011 |
Kurouski D, Lednev IK. The impact of protein disulfide bonds on the amyloid fibril morphology. International Journal of Biomedical Nanoscience and Nanotechnology. 2: 167-176. PMID 24693331 DOI: 10.1504/Ijbnn.2011.041000 |
0.68 |
|
| 2011 |
Heldt CL, Kurouski D, Sorci M, Grafeld E, Lednev IK, Belfort G. Isolating toxic insulin amyloid reactive species that lack B-sheets and have wide pH stability Biophysical Journal. 100: 2792-2800. PMID 21641325 DOI: 10.1016/J.Bpj.2011.04.046 |
0.652 |
|
| 2011 |
Heldt CL, Kurouski D, Sorci M, Grafeld E, Lednev IK, Belfort G. Isolating Toxic Insulin Amyloid Oligomers that Lack Beta-Sheets and have Wide pH Stability Biophysical Journal. 100: 390a. DOI: 10.1016/J.Bpj.2010.12.2316 |
0.669 |
|
| 2010 |
Kurouski D, Lombardi RA, Dukor RK, Lednev IK, Nafie LA. Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism. Chemical Communications (Cambridge, England). 46: 7154-6. PMID 20820535 DOI: 10.1039/C0Cc02423F |
0.635 |
|
| 2010 |
Kurouski D, Lauro W, Lednev IK. Amyloid fibrils are "alive": spontaneous refolding from one polymorph to another. Chemical Communications (Cambridge, England). 46: 4249-51. PMID 20532285 DOI: 10.1039/B926758A |
0.622 |
|
| 2010 |
Lednev IK, Kurouski D, Lauro W. Amyloid fibrils are "alive" as evident from deep UV Raman spectroscopic examination: An instrumentation driven discovery Aip Conference Proceedings. 1267: 172-173. DOI: 10.1063/1.3482448 |
0.606 |
|
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