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Leonid P. Breydo, Ph.D. - Publications

Affiliations: 
2002 University of Missouri - Columbia, Columbia, MO, United States 
Area:
Organic Chemistry, Biochemistry
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65 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Darling AL, Breydo L, Rivas EG, Gebru NT, Zheng D, Baker JD, Blair LJ, Dickey CA, Koren J, Uversky VN. Repeated repeat problems: Combinatorial effect of C9orf72-derived dipeptide repeat proteins. International Journal of Biological Macromolecules. PMID 30639592 DOI: 10.1016/J.Ijbiomac.2019.01.035  0.724
2018 Breydo L, Almehdar HA, El-Fakharany EM, Redwan EM, Uversky VN. Not all AMLETs are made equal: complexes of cow and camel α-lactalbumin with oleic acid show different structure and stability. Journal of Biomolecular Structure & Dynamics. 36: 4405-4412. PMID 29237329 DOI: 10.1080/07391102.2017.1417163  0.436
2017 Niyangoda C, Miti T, Breydo L, Uversky V, Muschol M. Carbonyl-based blue autofluorescence of proteins and amino acids. Plos One. 12: e0176983. PMID 28542206 DOI: 10.1371/Journal.Pone.0176983  0.484
2017 Nascimento TP, Sales AE, Porto TS, Costa RMPB, Breydo L, Uversky VN, Porto ALF, Converti A. Purification, biochemical, and structural characterization of a novel fibrinolytic enzyme from Mucor subtilissimus UCP 1262. Bioprocess and Biosystems Engineering. PMID 28500420 DOI: 10.1007/S00449-017-1781-3  0.442
2017 Redington JM, Breydo L, Uversky VN. When Good Goes Awry: The Aggregation of Protein Therapeutics. Protein and Peptide Letters. 24: 340-347. PMID 28190397 DOI: 10.2174/0929866524666170209153421  0.49
2017 Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. Disorder in Milk Proteins: α-Lactalbumin. Part C. Peculiarities of Metal Binding. Current Protein & Peptide Science. 17: 735-745. PMID 27238572 DOI: 10.2174/1389203717666160530151534  0.468
2017 Redington JM, Breydo L, Almehdar HA, Redwan EM, Uversky VN. α-Lactalbumin: Of Camels and Cows. Protein and Peptide Letters. 23: 1072-1080. PMID 27184498 DOI: 10.2174/0929866523666160517123738  0.483
2017 Uversky VN, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Permyakov EA. Disorder in Milk Proteins: α-Lactalbumin. Part B. A Multifunctional Whey Protein Acting as an Oligomeric Molten Globular "Oil Container" in the Anti-Tumorigenic Drugs, Liprotides. Current Protein & Peptide Science. 17: 612-28. PMID 26916155 DOI: 10.2174/1389203717666151203003151  0.491
2016 Breydo L, Redington JM, Uversky VN. Effects of Intrinsic and Extrinsic Factors on Aggregation of Physiologically Important Intrinsically Disordered Proteins. International Review of Cell and Molecular Biology. 329: 145-185. PMID 28109327 DOI: 10.1016/Bs.Ircmb.2016.08.011  0.5
2016 Santamaria N, Alhothali M, Alfonso MH, Breydo L, Uversky VN. Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis. Cellular and Molecular Life Sciences : Cmls. 74: 1297-1318. PMID 27838743 DOI: 10.1007/S00018-016-2416-6  0.495
2016 Fratz-Berilla EJ, Breydo L, Gouya L, Puy H, Uversky VN, Ferreira GC. Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients. Biochimica Et Biophysica Acta. PMID 27838491 DOI: 10.1016/J.Bbadis.2016.11.011  0.453
2016 Stojanovski BM, Breydo L, Uversky VN, Ferreira GC. The unfolding pathways of the native and molten globule states of 5-aminolevulinate synthase. Biochemical and Biophysical Research Communications. PMID 27751851 DOI: 10.1016/J.Bbrc.2016.10.037  0.424
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  0.468
2016 Lobbens ES, Breydo L, Skamris T, Vestergaard B, Jäger AK, Jorgensen L, Uversky V, van de Weert M. Mechanistic study of the inhibitory activity of Geum urbanum extract against α-Synuclein fibrillation. Biochimica Et Biophysica Acta. 1864: 1160-9. PMID 27353564 DOI: 10.1016/J.Bbapap.2016.06.009  0.463
2016 Ferreira LA, Breydo L, Reichardt C, Uversky VN, Zaslavsky BY. Effects of osmolytes on solvent features of water in aqueous solutions. Journal of Biomolecular Structure & Dynamics. 1-41. PMID 27026414 DOI: 10.1080/07391102.2016.1170633  0.403
2016 Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. Disorder in Milk Proteins: α -Lactalbumin. Part A. Structural Properties and Conformational Behavior. Current Protein & Peptide Science. 17: 352-67. PMID 26956441 DOI: 10.2174/138920371704160405001222  0.497
2016 Stojanovski BM, Breydo L, Uversky VN, Ferreira GC. Murine erythroid 5-aminolevulinate synthase: Truncation of a disordered N-terminal extension is not detrimental for catalysis. Biochimica Et Biophysica Acta. 1864: 441-52. PMID 26854603 DOI: 10.1016/J.Bbapap.2016.02.002  0.461
2016 Stojanovski B, Breydo L, Uversky VN, Ferreira GC. Macromolecular crowders and osmolytes modulate the structural and catalytic properties of alkaline molten globular 5-aminolevulinate synthase Rsc Advances. 6: 114541-114552. DOI: 10.1039/C6Ra22533K  0.432
2016 Sales AE, Breydo L, Porto TS, Porto ALF, Uversky VN. Hydrophobicity-dependent effects of polymers on different protein conformations Rsc Advances. 6: 42971-42983. DOI: 10.1039/C6Ra07910E  0.471
2015 Breydo L, Newland B, Zhang H, Rosser A, Werner C, Uversky VN, Wang W. A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation. Biochemical and Biophysical Research Communications. PMID 26707645 DOI: 10.1016/J.Bbrc.2015.12.060  0.461
2015 Fratz EJ, Clayton J, Hunter GA, Ducamp S, Breydo L, Uversky VN, Deybach JC, Gouya L, Puy H, Ferreira GC. Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release. Biochemistry. 54: 5617-31. PMID 26300302 DOI: 10.1021/Acs.Biochem.5B00407  0.465
2015 Breydo L, Uversky VN. Structural, morphological, and functional diversity of amyloid oligomers. Febs Letters. 589: 2640-8. PMID 26188543 DOI: 10.1016/J.Febslet.2015.07.013  0.509
2015 Breydo L, Sales AE, Frege T, Howell MC, Zaslavsky BY, Uversky VN. Effects of Polymer Hydrophobicity on Protein Structure and Aggregation Kinetics in Crowded Milieu. Biochemistry. 54: 2957-66. PMID 25919930 DOI: 10.1021/Acs.Biochem.5B00116  0.519
2015 Breydo L, Morgan D, Uversky VN. Pseudocatalytic Antiaggregation Activity of Antibodies: Immunoglobulins can Influence α-Synuclein Aggregation at Substoichiometric Concentrations. Molecular Neurobiology. PMID 25833100 DOI: 10.1007/S12035-015-9148-8  0.465
2015 Breydo L, Sales AE, Ferreira L, Fedotoff O, Shevelyova MP, Permyakov SE, Kroeck KG, Permyakov EA, Zaslavsky BY, Uversky VN. Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions. Archives of Biochemistry and Biophysics. 570: 66-74. PMID 25712220 DOI: 10.1016/J.Abb.2015.02.021  0.5
2015 Ferreira LA, Madeira PP, Breydo L, Reichardt C, Uversky VN, Zaslavsky BY. Role of solvent properties of aqueous media in macromolecular crowding effects. Journal of Biomolecular Structure & Dynamics. 1-12. PMID 25616385 DOI: 10.1080/07391102.2015.1011235  0.441
2015 Kuznetsova IM, Zaslavsky BY, Breydo L, Turoverov KK, Uversky VN. Beyond the excluded volume effects: mechanistic complexity of the crowded milieu. Molecules (Basel, Switzerland). 20: 1377-409. PMID 25594347 DOI: 10.3390/Molecules20011377  0.503
2014 Portillo A, Hashemi M, Zhang Y, Breydo L, Uversky VN, Lyubchenko YL. Role of monomer arrangement in the amyloid self-assembly. Biochimica Et Biophysica Acta. 1854: 218-28. PMID 25542374 DOI: 10.1016/J.Bbapap.2014.12.009  0.491
2014 Stojanovski BM, Breydo L, Hunter GA, Uversky VN, Ferreira GC. Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase. Biochimica Et Biophysica Acta. 1844: 2145-2154. PMID 25240868 DOI: 10.1016/J.Bbapap.2014.09.013  0.423
2014 Kovacs GG, Breydo L, Green R, Kis V, Puska G, LÅ‘rincz P, Perju-Dumbrava L, Giera R, Pirker W, Lutz M, Lachmann I, Budka H, Uversky VN, Molnár K, László L. Intracellular processing of disease-associated α-synuclein in the human brain suggests prion-like cell-to-cell spread. Neurobiology of Disease. 69: 76-92. PMID 24878508 DOI: 10.1016/J.Nbd.2014.05.020  0.453
2014 Na I, Reddy KD, Breydo L, Xue B, Uversky VN. A putative role of the Sup35p C-terminal domain in the cytoskeleton organization during yeast mitosis. Molecular Biosystems. 10: 925-40. PMID 24549315 DOI: 10.1039/C3Mb70515C  0.742
2013 Breydo L, Reddy KD, Piai A, Felli IC, Pierattelli R, Uversky VN. The crowd you're in with: effects of different types of crowding agents on protein aggregation. Biochimica Et Biophysica Acta. 1844: 346-57. PMID 24252314 DOI: 10.1016/J.Bbapap.2013.11.004  0.641
2013 Breydo L, Mikheeva LM, Madeira PP, Zaslavsky BY, Uversky VN. Solvent interaction analysis of intrinsically disordered proteins in aqueous two-phase systems. Molecular Biosystems. 9: 3068-79. PMID 24072065 DOI: 10.1039/C3Mb70329K  0.479
2013 Blair LJ, Nordhues BA, Hill SE, Scaglione KM, O'Leary JC, Fontaine SN, Breydo L, Zhang B, Li P, Wang L, Cotman C, Paulson HL, Muschol M, Uversky VN, Klengel T, et al. Accelerated neurodegeneration through chaperone-mediated oligomerization of tau. The Journal of Clinical Investigation. 123: 4158-69. PMID 23999428 DOI: 10.1172/Jci69003  0.451
2013 Zaslavsky A, Madeira P, Breydo L, Uversky VN, Chait A, Zaslavsky B. High throughput characterization of structural differences between closely related proteins in solution. Biochimica Et Biophysica Acta. 1834: 583-92. PMID 23174655 DOI: 10.1016/J.Bbapap.2012.11.004  0.481
2013 Silva BA, Breydo L, Uversky VN. Targeting the chameleon: a focused look at α-synuclein and its roles in neurodegeneration. Molecular Neurobiology. 47: 446-59. PMID 22940885 DOI: 10.1007/S12035-012-8334-1  0.39
2013 Silva BA, Breydo L, Fink AL, Uversky VN. Agrochemicals, α-synuclein, and Parkinson's disease. Molecular Neurobiology. 47: 598-612. PMID 22933040 DOI: 10.1007/S12035-012-8333-2  0.47
2013 Blair L, Nordhues B, Hill S, Scaglione KM, O'Leary J, Breydo L, Bo Z, Li P, Wang L, Cotman C, Paulson H, Muschol M, Uversky V, Klengel T, Binder E, et al. The Hsp90 co-chaperone FKBP51 produces neurotoxic tau oligomers: Implication for aging and Alzheimer's disease Alzheimers & Dementia. 9: 173. DOI: 10.1016/J.Jalz.2013.05.279  0.424
2012 Sivaramakrishnan S, Breydo L, Sun D, Gates KS. The macrocycle of leinamycin imparts hydrolytic stability to the thiol-sensing 1,2-dithiolan-3-one 1-oxide unit of the natural product. Bioorganic & Medicinal Chemistry Letters. 22: 3791-4. PMID 22560586 DOI: 10.1016/J.Bmcl.2012.04.003  0.733
2012 Breydo L, Wu JW, Uversky VN. Α-synuclein misfolding and Parkinson's disease. Biochimica Et Biophysica Acta. 1822: 261-85. PMID 22024360 DOI: 10.1016/J.Bbadis.2011.10.002  0.476
2011 Fekry MI, Szekely J, Dutta S, Breydo L, Zang H, Gates KS. Noncovalent DNA binding drives DNA alkylation by leinamycin: evidence that the Z,E-5-(thiazol-4-yl)-penta-2,4-dienone moiety of the natural product serves as an atypical DNA intercalator. Journal of the American Chemical Society. 133: 17641-51. PMID 21954957 DOI: 10.1021/Ja2046149  0.739
2011 Breydo L, Uversky VN. Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics : Integrated Biometal Science. 3: 1163-80. PMID 21869995 DOI: 10.1039/C1Mt00106J  0.482
2010 Kayed R, Canto I, Breydo L, Rasool S, Lukacsovich T, Wu J, Albay R, Pensalfini A, Yeung S, Head E, Marsh JL, Glabe C. Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Aβ oligomers. Molecular Neurodegeneration. 5: 57. PMID 21144050 DOI: 10.1186/1750-1326-5-57  0.351
2010 Wu JW, Breydo L, Isas JM, Lee J, Kuznetsov YG, Langen R, Glabe C. Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation. The Journal of Biological Chemistry. 285: 6071-9. PMID 20018889 DOI: 10.1074/Jbc.M109.069542  0.332
2008 Breydo L, Makarava N, Baskakov IV. Methods for conversion of prion protein into amyloid fibrils. Methods in Molecular Biology (Clifton, N.J.). 459: 105-15. PMID 18576151 DOI: 10.1007/978-1-59745-234-2_8  0.335
2007 Necula M, Breydo L, Milton S, Kayed R, van der Veer WE, Tone P, Glabe CG. Methylene blue inhibits amyloid Abeta oligomerization by promoting fibrillization. Biochemistry. 46: 8850-60. PMID 17595112 DOI: 10.1021/Bi700411K  0.306
2007 Sun Y, Breydo L, Makarava N, Yang Q, Bocharova OV, Baskakov IV. Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure. The Journal of Biological Chemistry. 282: 9090-7. PMID 17244617 DOI: 10.1074/Jbc.M608623200  0.365
2007 Breydo L, Sun Y, Makarava N, Lee CI, Novitskaia V, Bocharova O, Kao JP, Baskakov IV. Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation. Biochemistry. 46: 852-61. PMID 17223707 DOI: 10.1021/Bi061923V  0.361
2007 Baskakov IV, Breydo L. Converting the prion protein: what makes the protein infectious. Biochimica Et Biophysica Acta. 1772: 692-703. PMID 16935473 DOI: 10.1016/J.Bbadis.2006.07.007  0.345
2006 Dong C, Muriel JM, Ramirez S, Hutter H, Hedgecock EM, Breydo L, Baskakov IV, Vogel BE. Hemicentin assembly in the extracellular matrix is mediated by distinct structural modules. The Journal of Biological Chemistry. 281: 23606-10. PMID 16798744 DOI: 10.1074/Jbc.M513589200  0.301
2006 Makarava N, Bocharova OV, Salnikov VV, Breydo L, Anderson M, Baskakov IV. Dichotomous versus palm-type mechanisms of lateral assembly of amyloid fibrils. Protein Science : a Publication of the Protein Society. 15: 1334-41. PMID 16731968 DOI: 10.1110/Ps.052013106  0.348
2006 Anderson M, Bocharova OV, Makarava N, Breydo L, Salnikov VV, Baskakov IV. Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. Journal of Molecular Biology. 358: 580-96. PMID 16519898 DOI: 10.1016/J.Jmb.2006.02.007  0.314
2006 Bocharova OV, Makarava N, Breydo L, Anderson M, Salnikov VV, Baskakov IV. Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core. The Journal of Biological Chemistry. 281: 2373-9. PMID 16314415 DOI: 10.1074/Jbc.M510840200  0.34
2005 Breydo L, Bocharova OV, Makarava N, Salnikov VV, Anderson M, Baskakov IV. Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. Biochemistry. 44: 15534-43. PMID 16300402 DOI: 10.1021/Bi051369+  0.342
2005 Baskakov I, Disterer P, Breydo L, Shaw M, Gill A, James W, Tahiri-Alaoui A. The presence of valine at residue 129 in human prion protein accelerates amyloid formation. Febs Letters. 579: 2589-96. PMID 15862295 DOI: 10.1016/J.Febslet.2005.03.075  0.375
2005 Bocharova OV, Breydo L, Salnikov VV, Gill AC, Baskakov IV. Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease. Protein Science : a Publication of the Protein Society. 14: 1222-32. PMID 15802644 DOI: 10.1110/Ps.041186605  0.351
2005 Breydo L, Bocharova OV, Baskakov IV. Semiautomated cell-free conversion of prion protein: applications for high-throughput screening of potential antiprion drugs. Analytical Biochemistry. 339: 165-73. PMID 15766724 DOI: 10.1016/J.Ab.2005.01.003  0.343
2005 Bocharova OV, Breydo L, Parfenov AS, Salnikov VV, Baskakov IV. In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). Journal of Molecular Biology. 346: 645-59. PMID 15670611 DOI: 10.1016/J.Jmb.2004.11.068  0.366
2004 Breydo L, Zang H, Gates KS. Synthesis and noncovalent DNA-binding properties of thiazole derivatives related to leinamycin Tetrahedron Letters. 45: 5711-5716. DOI: 10.1016/J.Tetlet.2004.05.093  0.732
2002 Breydo L, Gates KS. Activation of leinamycin by thiols: a theoretical study. The Journal of Organic Chemistry. 67: 9054-60. PMID 12467428 DOI: 10.1021/Jo020568L  0.566
2002 Breydo L, Barnes CL, Gates KS. Two (E,E)- and (Z,E)-thiazol-5-ylpenta-2,4-dienones. Acta Crystallographica. Section C, Crystal Structure Communications. 58: o447-9. PMID 12154296 DOI: 10.1107/S0108270102007503  0.535
2001 Breydo L, Zang H, Mitra K, Gates KS. Thiol-independent DNA alkylation by leinamycin. Journal of the American Chemical Society. 123: 2060-1. PMID 11456831 DOI: 10.1021/Ja003309R  0.744
2001 Zang H, Breydo L, Mitra K, Dannaldson J, Gates KS. DNA alkylation by leinamycin can be triggered by cyanide and phosphines. Bioorganic & Medicinal Chemistry Letters. 11: 1511-5. PMID 11412971 DOI: 10.1016/S0960-894X(01)00196-2  0.749
2000 Breydo L, Gates KS. Thiol-dependent DNA cleavage by 3H-1,2-benzodithiol-3-one 1,1-dioxide. Bioorganic & Medicinal Chemistry Letters. 10: 885-9. PMID 10853652 DOI: 10.1016/S0960-894X(00)00125-6  0.608
1997 Breydo LP, Shevchenko AA, Kost OA. Study of ionization of tyrosine residues in proteins by second-derivative UV spectroscopy Russian Chemical Bulletin. 46: 1339-1343. DOI: 10.1007/Bf02495938  0.31
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