| Year |
Citation |
Score |
| 2022 |
Makarava N, Baskakov IV. Role of sialylation of N-linked glycans in prion pathogenesis. Cell and Tissue Research. PMID 35088180 DOI: 10.1007/s00441-022-03584-2 |
0.327 |
|
| 2020 |
Baskakov IV. Role of sialylation in prion disease pathogenesis and prion structure. Progress in Molecular Biology and Translational Science. 175: 31-52. PMID 32958238 DOI: 10.1016/Bs.Pmbts.2020.07.004 |
0.43 |
|
| 2020 |
Makarava N, Chang JC, Molesworth K, Baskakov IV. Posttranslational modifications define course of prion strain adaptation and disease phenotype. The Journal of Clinical Investigation. PMID 32484800 DOI: 10.1172/Jci138677 |
0.382 |
|
| 2020 |
Makarava N, Chang JC, Baskakov IV. Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism. International Journal of Molecular Sciences. 21. PMID 32012886 DOI: 10.3390/Ijms21030828 |
0.395 |
|
| 2020 |
Makarava N, Chang JC, Molesworth K, Baskakov IV. Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different cell tropism. Neurobiology of Disease. 104783. PMID 32001329 DOI: 10.1016/J.Nbd.2020.104783 |
0.35 |
|
| 2019 |
Makarava N, Chang JC, Kushwaha R, Baskakov IV. Region-Specific Response of Astrocytes to Prion Infection. Frontiers in Neuroscience. 13: 1048. PMID 31649496 DOI: 10.3389/Fnins.2019.01048 |
0.355 |
|
| 2019 |
Baskakov IV, Caughey B, Requena JR, Sevillano AM, Surewicz WK, Wille H. The Prion 2018 round tables (I): The structure of PrP. Prion. PMID 30646817 DOI: 10.1080/19336896.2019.1569450 |
0.377 |
|
| 2018 |
Baskakov IV, Katorcha E, Makarava N. Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology. Viruses. 10. PMID 30567302 DOI: 10.3390/V10120723 |
0.402 |
|
| 2018 |
Makarava N, Savtchenko R, Lasch P, Beekes M, Baskakov IV. Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein. Acta Neuropathologica Communications. 6: 92. PMID 30208966 DOI: 10.1186/S40478-018-0597-Y |
0.435 |
|
| 2018 |
Srivastava S, Katorcha E, Makarava N, Barrett JP, Loane DJ, Baskakov IV. Inflammatory response of microglia to prions is controlled by sialylation of PrP. Scientific Reports. 8: 11326. PMID 30054538 DOI: 10.1038/S41598-018-29720-Z |
0.381 |
|
| 2018 |
Katorcha E, Gonzalez-Montalban N, Makarava N, Kovacs GG, Baskakov IV. Prion replication environment defines the fate of prion strain adaptation. Plos Pathogens. 14: e1007093. PMID 29928047 DOI: 10.1371/Journal.Ppat.1007093 |
0.366 |
|
| 2018 |
Katorcha E, Baskakov IV. Analysis of Covalent Modifications of Amyloidogenic Proteins Using Two-Dimensional Electrophoresis: Prion Protein and Its Sialylation. Methods in Molecular Biology (Clifton, N.J.). 1779: 241-255. PMID 29886537 DOI: 10.1007/978-1-4939-7816-8_15 |
0.452 |
|
| 2017 |
Katorcha E, Baskakov IV. Analyses of N-linked glycans of PrP revealed predominantly 2,6-linked sialic acid residues. The Febs Journal. 284: 3727-3738. PMID 28898525 DOI: 10.1111/Febs.14268 |
0.38 |
|
| 2017 |
Makarava N, Savtchenko R, Baskakov IV. Methods of Protein Misfolding Cyclic Amplification. Methods in Molecular Biology (Clifton, N.J.). 1658: 169-183. PMID 28861790 DOI: 10.1007/978-1-4939-7244-9_13 |
0.385 |
|
| 2017 |
Makarava N, Savtchenko R, Baskakov IV. Purification and Fibrillation of Full-Length Recombinant PrP. Methods in Molecular Biology (Clifton, N.J.). 1658: 3-22. PMID 28861778 DOI: 10.1007/978-1-4939-7244-9_1 |
0.352 |
|
| 2017 |
Katorcha E, Makarava N, Lee YJ, Lindberg I, Monteiro MJ, Kovacs GG, Baskakov IV. Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy. Plos Pathogens. 13: e1006563. PMID 28797122 DOI: 10.1371/Journal.Ppat.1006563 |
0.439 |
|
| 2017 |
Baskakov IV. Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology. Prion. 11: 82-88. PMID 28324664 DOI: 10.1080/19336896.2017.1301338 |
0.378 |
|
| 2016 |
Srivastava S, Katorcha E, Daus ML, Lasch P, Beekes M, Baskakov IV. Sialylation controls prion fate in vivo. The Journal of Biological Chemistry. PMID 27998976 DOI: 10.1074/Jbc.M116.768010 |
0.416 |
|
| 2016 |
Katorcha E, Daus ML, Gonzalez-Montalban N, Makarava N, Lasch P, Beekes M, Baskakov IV. Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation. Scientific Reports. 6: 33119. PMID 27609323 DOI: 10.1038/Srep33119 |
0.353 |
|
| 2016 |
Baskakov IV, Katorcha E. Multifaceted Role of Sialylation in Prion Diseases. Frontiers in Neuroscience. 10: 358. PMID 27551257 DOI: 10.3389/Fnins.2016.00358 |
0.45 |
|
| 2016 |
Katorcha E, Srivastava S, Klimova N, Baskakov IV. Sialylation of GPI Anchors of Mammalian Prions is Regulated in a Host-, Tissue- and Cell-Specific Manner. The Journal of Biological Chemistry. PMID 27317661 DOI: 10.1074/Jbc.M116.732040 |
0.408 |
|
| 2016 |
Morales R, Hu PP, Duran-Aniotz C, Moda F, Diaz-Espinoza R, Chen B, Bravo-Alegria J, Makarava N, Baskakov IV, Soto C. Strain-dependent profile of misfolded prion protein aggregates. Scientific Reports. 6: 20526. PMID 26877167 DOI: 10.1038/Srep20526 |
0.431 |
|
| 2016 |
Makarava N, Savtchenko R, Alexeeva I, Rohwer RG, Baskakov IV. New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions. The American Journal of Pathology. 186: 1006-14. PMID 26873446 DOI: 10.1016/J.Ajpath.2015.11.013 |
0.452 |
|
| 2015 |
Srivastava S, Makarava N, Katorcha E, Savtchenko R, Brossmer R, Baskakov IV. Post-conversion sialylation of prions in lymphoid tissues. Proceedings of the National Academy of Sciences of the United States of America. 112: E6654-62. PMID 26627256 DOI: 10.1073/Pnas.1517993112 |
0.363 |
|
| 2015 |
Katorcha E, Makarava N, Savtchenko R, Baskakov IV. Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio. Scientific Reports. 5: 16912. PMID 26576925 DOI: 10.1038/Srep16912 |
0.419 |
|
| 2015 |
Katorcha E, Klimova N, Makarava N, Savtchenko R, Pan X, Annunziata I, Takahashi K, Miyagi T, Pshezhetsky AV, d'Azzo A, Baskakov IV. Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1. Plos One. 10: e0143218. PMID 26569607 DOI: 10.1371/Journal.Pone.0143218 |
0.394 |
|
| 2015 |
Makarava N, Savtchenko R, Baskakov IV. Two alternative pathways for generating transmissible prion disease de novo. Acta Neuropathologica Communications. 3: 69. PMID 26556038 DOI: 10.1186/S40478-015-0248-5 |
0.428 |
|
| 2015 |
Martínez J, Sánchez R, Castellanos M, Makarava N, Aguzzi A, Baskakov IV, Gasset M. PrP charge structure encodes interdomain interactions. Scientific Reports. 5: 13623. PMID 26323476 DOI: 10.1038/Srep13623 |
0.364 |
|
| 2015 |
Srivastava S, Baskakov IV. Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein. Plos One. 10: e0130283. PMID 26090881 DOI: 10.1371/Journal.Pone.0130283 |
0.429 |
|
| 2015 |
Klimova N, Makarava N, Baskakov IV. The diversity and relationship of prion protein self-replicating states. Virus Research. 207: 113-9. PMID 25312451 DOI: 10.1016/J.Virusres.2014.10.002 |
0.364 |
|
| 2014 |
Katorcha E, Makarava N, Savtchenko R, D'Azzo A, Baskakov IV. Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. Plos Pathogens. 10: e1004366. PMID 25211026 DOI: 10.1371/Journal.Ppat.1004366 |
0.43 |
|
| 2014 |
Baskakov IV. The many shades of prion strain adaptation. Prion. 8. PMID 24518385 DOI: 10.4161/Pri.27836 |
0.386 |
|
| 2014 |
Jeffrey M, Mcgovern G, Makarava N, González L, Kim YS, Rohwer RG, Baskakov IV. Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies Neuropathology and Applied Neurobiology. 40: 296-310. PMID 23578208 DOI: 10.1111/Nan.12053 |
0.4 |
|
| 2013 |
Kovacs GG, Makarava N, Savtchenko R, Baskakov IV. Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles. The American Journal of Pathology. 183: 1539-47. PMID 24012784 DOI: 10.1016/J.Ajpath.2013.07.024 |
0.37 |
|
| 2013 |
Gonzalez-Montalban N, Lee YJ, Makarava N, Savtchenko R, Baskakov IV. Changes in prion replication environment cause prion strain mutation. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 27: 3702-10. PMID 23729586 DOI: 10.1096/Fj.13-230466 |
0.347 |
|
| 2013 |
Makarava N, Savtchenko R, Baskakov IV. Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. The Journal of Biological Chemistry. 288: 33-41. PMID 23168413 DOI: 10.1074/Jbc.M112.419531 |
0.394 |
|
| 2012 |
Gonzalez-Montalban N, Baskakov IV. Assessment of strain-specific PrP(Sc) elongation rates revealed a transformation of PrP(Sc) properties during protein misfolding cyclic amplification. Plos One. 7: e41210. PMID 22815972 DOI: 10.1371/Journal.Pone.0041210 |
0.385 |
|
| 2012 |
Makarava N, Kovacs GG, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV. Stabilization of a prion strain of synthetic origin requires multiple serial passages. The Journal of Biological Chemistry. 287: 30205-14. PMID 22807452 DOI: 10.1074/Jbc.M112.392985 |
0.367 |
|
| 2012 |
Shashilov V, Xu M, Makarava N, Savtchenko R, Baskakov IV, Lednev IK. Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy. The Journal of Physical Chemistry. B. 116: 7926-30. PMID 22681559 DOI: 10.1021/Jp2122455 |
0.364 |
|
| 2012 |
Makarava N, Kovacs GG, Savtchenko R, Alexeeva I, Ostapchenko VG, Budka H, Rohwer RG, Baskakov IV. A new mechanism for transmissible prion diseases. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 7345-55. PMID 22623680 DOI: 10.1523/Jneurosci.6351-11.2012 |
0.469 |
|
| 2012 |
Makarava N, Baskakov IV. Genesis of tramsmissible protein states via deformed templating. Prion. 6: 252-5. PMID 22561163 DOI: 10.4161/Pri.19930 |
0.45 |
|
| 2012 |
Ostapchenko V, Gasset M, Baskakov IV. Atomic force fluorescence microscopy in the characterization of amyloid fibril assembly and oligomeric intermediates. Methods in Molecular Biology (Clifton, N.J.). 849: 157-67. PMID 22528089 DOI: 10.1007/978-1-61779-551-0_11 |
0.367 |
|
| 2012 |
Makarava N, Baskakov IV. Purification and fibrillation of full-length recombinant PrP. Methods in Molecular Biology (Clifton, N.J.). 849: 33-52. PMID 22528082 DOI: 10.1007/978-1-61779-551-0_4 |
0.438 |
|
| 2012 |
Makarava N, Savtchenko R, Alexeeva I, Rohwer RG, Baskakov IV. Fast and ultrasensitive method for quantitating prion infectivity titre. Nature Communications. 3: 741. PMID 22415832 DOI: 10.1038/Ncomms1730 |
0.364 |
|
| 2011 |
Makarava N, Kovacs GG, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV. Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. Plos Pathogens. 7: e1002419. PMID 22144901 DOI: 10.1371/Journal.Ppat.1002419 |
0.441 |
|
| 2011 |
Ayrolles-Torro A, Imberdis T, Torrent J, Toupet K, Baskakov IV, Poncet-Montange G, Grégoire C, Roquet-Baneres F, Lehmann S, Rognan D, Pugnière M, Verdier JM, Perrier V. Oligomeric-induced activity by thienyl pyrimidine compounds traps prion infectivity. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 31: 14882-92. PMID 22016521 DOI: 10.1523/Jneurosci.0547-11.2011 |
0.424 |
|
| 2011 |
Gonzalez-Montalban N, Makarava N, Savtchenko R, Baskakov IV. Relationship between conformational stability and amplification efficiency of prions. Biochemistry. 50: 7933-40. PMID 21848309 DOI: 10.1021/Bi200950V |
0.356 |
|
| 2011 |
Lee YJ, Savtchenko R, Ostapchenko VG, Makarava N, Baskakov IV. Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity. Plos One. 6: e20244. PMID 21625461 DOI: 10.1371/Journal.Pone.0020244 |
0.408 |
|
| 2011 |
El Moustaine D, Perrier V, Acquatella-Tran Van Ba I, Meersman F, Ostapchenko VG, Baskakov IV, Lange R, Torrent J. Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure. The Journal of Biological Chemistry. 286: 13448-59. PMID 21357423 DOI: 10.1074/Jbc.M110.192872 |
0.393 |
|
| 2011 |
Gonzalez-Montalban N, Makarava N, Ostapchenko VG, Savtchenk R, Alexeeva I, Rohwer RG, Baskakov IV. Highly efficient protein misfolding cyclic amplification. Plos Pathogens. 7: e1001277. PMID 21347353 DOI: 10.1371/Journal.Ppat.1001277 |
0.419 |
|
| 2010 |
Tycko R, Savtchenko R, Ostapchenko VG, Makarava N, Baskakov IV. The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry. 49: 9488-97. PMID 20925423 DOI: 10.1021/Bi1013134 |
0.385 |
|
| 2010 |
Ostapchenko VG, Sawaya MR, Makarava N, Savtchenko R, Nilsson KP, Eisenberg D, Baskakov IV. Two amyloid States of the prion protein display significantly different folding patterns. Journal of Molecular Biology. 400: 908-21. PMID 20553730 DOI: 10.1016/J.Jmb.2010.05.051 |
0.402 |
|
| 2010 |
Colby DW, Wain R, Baskakov IV, Legname G, Palmer CG, Nguyen HO, Lemus A, Cohen FE, DeArmond SJ, Prusiner SB. Protease-sensitive synthetic prions. Plos Pathogens. 6: e1000736. PMID 20107515 DOI: 10.1371/Journal.Ppat.1000736 |
0.533 |
|
| 2010 |
Lee YJ, Baskakov IV. Treatment with normal prion protein delays differentiation and helps to maintain high proliferation activity in human embryonic stem cells. Journal of Neurochemistry. 114: 362-73. PMID 20089130 DOI: 10.1111/J.1471-4159.2010.06601.X |
0.35 |
|
| 2010 |
Makarava N, Kovacs GG, Bocharova O, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV. Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathologica. 119: 177-87. PMID 20052481 DOI: 10.1007/S00401-009-0633-X |
0.405 |
|
| 2009 |
Colby DW, Giles K, Legname G, Wille H, Baskakov IV, DeArmond SJ, Prusiner SB. Design and construction of diverse mammalian prion strains. Proceedings of the National Academy of Sciences of the United States of America. 106: 20417-22. PMID 19915150 DOI: 10.1073/Pnas.0910350106 |
0.568 |
|
| 2009 |
Baskakov IV. Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classification. Febs Letters. 583: 2618-22. PMID 19482025 DOI: 10.1016/J.Febslet.2009.05.044 |
0.382 |
|
| 2009 |
Makarava N, Ostapchenko VG, Savtchenko R, Baskakov IV. Conformational switching within individual amyloid fibrils. The Journal of Biological Chemistry. 284: 14386-95. PMID 19329794 DOI: 10.1074/Jbc.M900533200 |
0.419 |
|
| 2008 |
Ostapchenko VG, Makarava N, Savtchenko R, Baskakov IV. The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP. Journal of Molecular Biology. 383: 1210-24. PMID 18789949 DOI: 10.1016/J.Jmb.2008.08.073 |
0.471 |
|
| 2008 |
Makarava N, Baskakov IV. Expression and purification of full-length recombinant PrP of high purity. Methods in Molecular Biology (Clifton, N.J.). 459: 131-43. PMID 18576153 DOI: 10.1007/978-1-59745-234-2_10 |
0.39 |
|
| 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 |
0.441 |
|
| 2008 |
Makarava N, Baskakov IV. The same primary structure of the prion protein yields two distinct self-propagating states. The Journal of Biological Chemistry. 283: 15988-96. PMID 18400757 DOI: 10.1074/Jbc.M800562200 |
0.396 |
|
| 2008 |
Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, Baskakov IV. Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. Journal of Molecular Biology. 376: 1155-67. PMID 18206163 DOI: 10.1016/J.Jmb.2007.12.053 |
0.429 |
|
| 2007 |
Makarava N, Lee CI, Ostapchenko VG, Baskakov IV. Highly promiscuous nature of prion polymerization. The Journal of Biological Chemistry. 282: 36704-13. PMID 17940285 DOI: 10.1074/Jbc.M704926200 |
0.465 |
|
| 2007 |
Lee CI, Yang Q, Perrier V, Baskakov IV. The dominant-negative effect of the Q218K variant of the prion protein does not require protein X. Protein Science : a Publication of the Protein Society. 16: 2166-73. PMID 17766375 DOI: 10.1110/Ps.072954607 |
0.43 |
|
| 2007 |
Baskakov IV. Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils. The Febs Journal. 274: 3756-65. PMID 17617227 DOI: 10.1111/J.1742-4658.2007.05916.X |
0.447 |
|
| 2007 |
Novitskaya V, Makarava N, Sylvester I, Bronstein IB, Baskakov IV. Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2-derived terminally differentiated neurons. Journal of Neurochemistry. 102: 398-407. PMID 17472702 DOI: 10.1111/J.1471-4159.2007.04537.X |
0.373 |
|
| 2007 |
Baskakov IV. The reconstitution of mammalian prion infectivity de novo. The Febs Journal. 274: 576-87. PMID 17288547 DOI: 10.1111/J.1742-4658.2007.05630.X |
0.439 |
|
| 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 |
0.456 |
|
| 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 |
0.459 |
|
| 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 |
0.439 |
|
| 2006 |
Nishina KA, Deleault NR, Mahal SP, Baskakov I, Luhrs T, Riek R, Supattapone S. The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry. 45: 14129-39. PMID 17115708 DOI: 10.1021/Bi061526K |
0.651 |
|
| 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 |
0.307 |
|
| 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 |
0.438 |
|
| 2006 |
Novitskaya V, Makarava N, Bellon A, Bocharova OV, Bronstein IB, Williamson RA, Baskakov IV. Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. The Journal of Biological Chemistry. 281: 15536-45. PMID 16569635 DOI: 10.1074/Jbc.M601349200 |
0.423 |
|
| 2006 |
Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. The Journal of Biological Chemistry. 281: 13828-36. PMID 16554307 DOI: 10.1074/Jbc.M511174200 |
0.418 |
|
| 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 |
0.387 |
|
| 2006 |
Ter-Avanesyan M, Derkatch I, Baskakov I, Kushnirov V. Unraveling prion structures and biological functions. Genome Biology. 6: 366. PMID 16420684 DOI: 10.1186/Gb-2005-6-13-366 |
0.312 |
|
| 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 |
0.428 |
|
| 2006 |
Legname G, Nguyen HB, Baskakov IV, DeArmond SJ, Prusiner SB. S1-03-04: Transmission studies of mouse synthetic prions Alzheimer's & Dementia. 2: S5-S5. DOI: 10.1016/J.Jalz.2006.05.022 |
0.459 |
|
| 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+ |
0.403 |
|
| 2005 |
Bocharova OV, Breydo L, Salnikov VV, Baskakov IV. Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils. Biochemistry. 44: 6776-87. PMID 15865423 DOI: 10.1021/Bi050251Q |
0.348 |
|
| 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 |
0.433 |
|
| 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 |
0.452 |
|
| 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 |
0.459 |
|
| 2005 |
Baskakov IV, Bocharova OV. In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features. Biochemistry. 44: 2339-48. PMID 15709746 DOI: 10.1021/Bi048322T |
0.441 |
|
| 2005 |
Legname G, Nguyen HO, Baskakov IV, Cohen FE, Dearmond SJ, Prusiner SB. Strain-specified characteristics of mouse synthetic prions. Proceedings of the National Academy of Sciences of the United States of America. 102: 2168-73. PMID 15671162 DOI: 10.1073/Pnas.0409079102 |
0.495 |
|
| 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 |
0.446 |
|
| 2004 |
Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, DeArmond SJ, Prusiner SB. Synthetic mammalian prions. Science (New York, N.Y.). 305: 673-6. PMID 15286374 DOI: 10.1126/Science.1100195 |
0.543 |
|
| 2004 |
Baskakov IV, Legname G, Gryczynski Z, Prusiner SB. The peculiar nature of unfolding of the human prion protein. Protein Science : a Publication of the Protein Society. 13: 586-95. PMID 14767078 DOI: 10.1110/Ps.03457204 |
0.574 |
|
| 2004 |
Baskakov IV. Autocatalytic conversion of recombinant prion proteins displays a species barrier. The Journal of Biological Chemistry. 279: 7671-7. PMID 14668351 DOI: 10.1074/Jbc.M310594200 |
0.425 |
|
| 2002 |
Baskakov IV, Legname G, Baldwin MA, Prusiner SB, Cohen FE. Pathway complexity of prion protein assembly into amyloid. The Journal of Biological Chemistry. 277: 21140-8. PMID 11912192 DOI: 10.1074/Jbc.M111402200 |
0.538 |
|
| 2001 |
Bolen DW, Baskakov IV. The osmophobic effect: natural selection of a thermodynamic force in protein folding. Journal of Molecular Biology. 310: 955-63. PMID 11502004 DOI: 10.1006/Jmbi.2001.4819 |
0.633 |
|
| 2001 |
Baskakov IV, Legname G, Prusiner SB, Cohen FE. Folding of prion protein to its native alpha-helical conformation is under kinetic control. The Journal of Biological Chemistry. 276: 19687-90. PMID 11306559 DOI: 10.1074/Jbc.C100180200 |
0.502 |
|
| 2000 |
Baskakov IV, Aagaard C, Mehlhorn I, Wille H, Groth D, Baldwin MA, Prusiner SB, Cohen FE. Self-assembly of recombinant prion protein of 106 residues. Biochemistry. 39: 2792-804. PMID 10704232 DOI: 10.1021/Bi9923353 |
0.559 |
|
| 1999 |
Kumar R, Baskakov IV, Srinivasan G, Bolen DW, Lee JC, Thompson EB. Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor. The Journal of Biological Chemistry. 274: 24737-41. PMID 10455143 DOI: 10.1074/Jbc.274.35.24737 |
0.614 |
|
| 1999 |
Baskakov IV, Bolen DW. The paradox between m values and deltaCp's for denaturation of ribonuclease T1 with disulfide bonds intact and broken. Protein Science : a Publication of the Protein Society. 8: 1314-9. PMID 10386881 DOI: 10.1110/Ps.8.6.1314 |
0.589 |
|
| 1999 |
Baskakov IV, Kumar R, Srinivasan G, Ji YS, Bolen DW, Thompson EB. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. The Journal of Biological Chemistry. 274: 10693-6. PMID 10196139 DOI: 10.1074/Jbc.274.16.10693 |
0.666 |
|
| 1998 |
Baskakov IV, Bolen DW. Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: implications regarding m values, intermediates, and thermodynamics. Biochemistry. 37: 18010-7. PMID 9922169 DOI: 10.1021/Bi981849J |
0.648 |
|
| 1998 |
Baskakov I, Wang A, Bolen DW. Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis. Biophysical Journal. 74: 2666-73. PMID 9591690 DOI: 10.1016/S0006-3495(98)77972-X |
0.625 |
|
| 1998 |
Baskakov I, Bolen DW. Time-dependent effects of trimethylamine-N-oxide/urea on lactate dehydrogenase activity: an unexplored dimension of the adaptation paradigm. Biophysical Journal. 74: 2658-65. PMID 9591689 DOI: 10.1016/S0006-3495(98)77971-8 |
0.621 |
|
| 1998 |
Baskakov I, Bolen DW. Forcing thermodynamically unfolded proteins to fold. The Journal of Biological Chemistry. 273: 4831-4. PMID 9478922 DOI: 10.1074/jbc.273.9.4831 |
0.645 |
|
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