| Year |
Citation |
Score |
| 2024 |
Sridharan V, George T, Conroy DW, Shaffer Z, Surewicz WK, Jaroniec CP. Copper binding alters the core structure of amyloid fibrils formed by Y145Stop human prion protein. Physical Chemistry Chemical Physics : Pccp. PMID 39392708 DOI: 10.1039/d4cp03593c |
0.316 |
|
| 2022 |
Li Q, Jaroniec CP, Surewicz WK. Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers. Nature Structural & Molecular Biology. PMID 36097290 DOI: 10.1038/s41594-022-00833-4 |
0.366 |
|
| 2022 |
Qi Z, Surewicz K, Surewicz WK, Jaroniec CP. Influence of the Dynamically Disordered N-Terminal Tail Domain on the Amyloid Core Structure of Human Y145Stop Prion Protein Fibrils. Frontiers in Molecular Biosciences. 9: 841790. PMID 35237664 DOI: 10.3389/fmolb.2022.841790 |
0.324 |
|
| 2021 |
Li Q, Babinchak WM, Surewicz WK. Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43. Nature Communications. 12: 1620. PMID 33712624 DOI: 10.1038/s41467-021-21912-y |
0.345 |
|
| 2020 |
Dao HH, Hlaing MZ, Ma Y, Surewicz K, Surewicz WK, Jaroniec CP. C and N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils. Biomolecular Nmr Assignments. PMID 33123960 DOI: 10.1007/s12104-020-09981-4 |
0.395 |
|
| 2020 |
Nemani SK, Xiao X, Cali I, Cracco L, Puoti G, Nigro M, Lavrich J, Bharara Singh A, Appleby BS, Sim VL, Notari S, Surewicz WK, Gambetti P. A novel mechanism of phenotypic heterogeneity in Creutzfeldt-Jakob disease. Acta Neuropathologica Communications. 8: 85. PMID 32560672 DOI: 10.1186/S40478-020-00966-X |
0.384 |
|
| 2020 |
Singh V, Xu L, Boyko S, Surewicz K, Surewicz WK. Zinc promotes liquid-liquid phase separation of tau protein. The Journal of Biological Chemistry. PMID 32229582 DOI: 10.1074/Jbc.Ac120.013166 |
0.324 |
|
| 2020 |
Babinchak WM, Surewicz WK. Liquid-Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation. Journal of Molecular Biology. 432: 1910-1925. PMID 32169484 DOI: 10.1016/J.Jmb.2020.03.004 |
0.427 |
|
| 2019 |
Cracco L, Xiao X, Nemani SK, Lavrich J, Cali I, Ghetti B, Notari S, Surewicz WK, Gambetti P. Gerstmann-Sträussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments. Acta Neuropathologica Communications. 7: 1. PMID 31142381 DOI: 10.1186/S40478-019-0734-2 |
0.395 |
|
| 2019 |
Boyko S, Qi X, Chen TH, Surewicz K, Surewicz WK. Liquid-liquid phase separation of tau protein: The crucial role of electrostatic interactions. The Journal of Biological Chemistry. PMID 31097543 DOI: 10.1074/Jbc.Ac119.009198 |
0.33 |
|
| 2019 |
Babinchak WM, Haider R, Dumm BK, Sarkar P, Surewicz K, Choi JK, Surewicz WK. The role of liquid-liquid phase separation in aggregation of the TDP-43 low complexity domain. The Journal of Biological Chemistry. PMID 30814253 DOI: 10.1074/Jbc.Ra118.007222 |
0.346 |
|
| 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 |
0.375 |
|
| 2018 |
Peng Y, Cao S, Kiselar J, Xiao X, Du Z, Hsieh A, Ko S, Chen Y, Agrawal P, Zheng W, Shi W, Jiang W, Yang L, Chance MR, Surewicz WK, et al. A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain. Structure (London, England : 1993). PMID 30581045 DOI: 10.1016/J.Str.2018.10.026 |
0.351 |
|
| 2018 |
Theint T, Xia Y, Nadaud PS, Mukhopadhyay D, Schwieters CD, Surewicz K, Surewicz WK, Jaroniec CP. Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy. Journal of the American Chemical Society. PMID 30295029 DOI: 10.1021/Jacs.8B06758 |
0.436 |
|
| 2018 |
Shannon M, Theint T, Mukhopadhyay D, Surewicz K, Surewicz W, Marion D, Schanda P, Jaroniec CP. Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 30276945 DOI: 10.1002/Cphc.201800779 |
0.406 |
|
| 2018 |
Li Q, Wang F, Xiao X, Kim C, Bohon J, Kiselar J, Safar JG, Ma J, Surewicz WK. Structural attributes of mammalian prion infectivity: Insights from studies with synthetic prions. The Journal of Biological Chemistry. PMID 30275016 DOI: 10.1074/Jbc.Ra118.005622 |
0.462 |
|
| 2018 |
Kim C, Xiao X, Chen S, Haldiman T, Smirnovas V, Kofskey D, Warren M, Surewicz K, Maurer NR, Kong Q, Surewicz W, Safar JG. Artificial strain of human prions created in vitro. Nature Communications. 9: 2166. PMID 29867164 DOI: 10.1038/S41467-018-04584-Z |
0.405 |
|
| 2018 |
Aucoin D, Xia Y, Theint T, Nadaud PS, Surewicz K, Surewicz WK, Jaroniec CP. Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy. Journal of Structural Biology. PMID 29679649 DOI: 10.1016/J.Jsb.2018.04.002 |
0.476 |
|
| 2018 |
Nieznanska H, Bandyszewska M, Surewicz K, Zajkowski T, Surewicz WK, Nieznanski K. Identification of prion protein-derived peptides of potential use in Alzheimer's disease therapy. Biochimica Et Biophysica Acta. 1864: 2143-2153. PMID 29604335 DOI: 10.1016/J.Bbadis.2018.03.023 |
0.412 |
|
| 2017 |
Abskharon R, Dang J, Elfarash A, Wang Z, Shen P, Zou LS, Hassan S, Wang F, Fujioka H, Steyaert J, Mulaj M, Surewicz WK, Castilla J, Wohlkonig A, Zou WQ. Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors. Microbial Cell Factories. 16: 170. PMID 28978309 DOI: 10.1186/S12934-017-0782-X |
0.446 |
|
| 2017 |
Theint T, Nadaud PS, Aucoin D, Helmus JJ, Pondaven SP, Surewicz K, Surewicz WK, Jaroniec CP. Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy. Nature Communications. 8: 753. PMID 28963458 DOI: 10.1038/S41467-017-00794-Z |
0.484 |
|
| 2017 |
Wang F, Wang X, Orrú CD, Groveman BR, Surewicz K, Abskharon R, Imamura M, Yokoyama T, Kim YS, Vander Stel KJ, Sinniah K, Priola SA, Surewicz WK, Caughey B, Ma J. Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity. Plos Pathogens. 13: e1006491. PMID 28704563 DOI: 10.1371/Journal.Ppat.1006491 |
0.42 |
|
| 2017 |
Bett C, Lawrence J, Kurt TD, Orru C, Aguilar-Calvo P, Kincaid AE, Surewicz WK, Caughey B, Wu C, Sigurdson CJ. Enhanced neuroinvasion by smaller, soluble prions. Acta Neuropathologica Communications. 5: 32. PMID 28431576 DOI: 10.1186/S40478-017-0430-Z |
0.341 |
|
| 2017 |
Aguilar-Calvo P, Xiao X, Bett C, Eraña H, Soldau K, Castilla J, Nilsson KP, Surewicz WK, Sigurdson CJ. Post-translational modifications in PrP expand the conformational diversity of prions in vivo. Scientific Reports. 7: 43295. PMID 28272426 DOI: 10.1038/Srep43295 |
0.483 |
|
| 2017 |
Theint T, Nadaud P, Surewicz K, Surewicz W, Jaroniec C. 13C and 15N Chemical Shift Assignments for Syrian Hamster Y145Stop Prion Protein Amyloid Fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26926 |
0.406 |
|
| 2016 |
Theint T, Nadaud PS, Surewicz K, Surewicz WK, Jaroniec CP. (13)C and (15)N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils. Biomolecular Nmr Assignments. PMID 28004358 DOI: 10.1007/S12104-016-9723-6 |
0.446 |
|
| 2016 |
Choi JK, Cali I, Surewicz K, Kong Q, Gambetti P, Surewicz WK. Amyloid fibrils from the N-terminal prion protein fragment are infectious. Proceedings of the National Academy of Sciences of the United States of America. PMID 27849581 DOI: 10.1073/Pnas.1610716113 |
0.483 |
|
| 2016 |
Scott-McKean JJ, Surewicz K, Choi JK, Ruffin VA, Salameh AI, Nieznanski K, Costa AC, Surewicz WK. Soluble prion protein and its N-terminal fragment prevent impairment of synaptic plasticity by Aβ oligomers: Implications for novel therapeutic strategy in Alzheimer's disease. Neurobiology of Disease. PMID 26949218 DOI: 10.1016/J.Nbd.2016.03.001 |
0.392 |
|
| 2015 |
Williams TL, Choi JK, Surewicz K, Surewicz WK. Soluble Prion Protein Binds Isolated Low Molecular Weight Amyloid-β Oligomers Causing Cyto-toxicity Inhibition. Acs Chemical Neuroscience. PMID 26466138 DOI: 10.1021/Acschemneuro.5B00229 |
0.427 |
|
| 2015 |
Safar JG, Xiao X, Kabir ME, Chen S, Kim C, Haldiman T, Cohen Y, Chen W, Cohen ML, Surewicz WK. Structural determinants of phenotypic diversity and replication rate of human prions. Plos Pathogens. 11: e1004832. PMID 25875953 DOI: 10.1371/Journal.Ppat.1004832 |
0.459 |
|
| 2015 |
Cohen ML, Kim C, Haldiman T, ElHag M, Mehndiratta P, Pichet T, Lissemore F, Shea M, Cohen Y, Chen W, Blevins J, Appleby BS, Surewicz K, Surewicz WK, Sajatovic M, et al. Rapidly progressive Alzheimer's disease features distinct structures of amyloid-β. Brain : a Journal of Neurology. 138: 1009-22. PMID 25688081 DOI: 10.1093/Brain/Awv006 |
0.364 |
|
| 2014 |
Nieznanski K, Surewicz K, Chen S, Nieznanska H, Surewicz WK. Interaction between prion protein and Aβ amyloid fibrils revisited. Acs Chemical Neuroscience. 5: 340-5. PMID 24669873 DOI: 10.1021/Cn500019C |
0.418 |
|
| 2014 |
Cobb NJ, Apostol MI, Chen S, Smirnovas V, Surewicz WK. Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region. The Journal of Biological Chemistry. 289: 2643-50. PMID 24338015 DOI: 10.1074/Jbc.M113.520718 |
0.443 |
|
| 2013 |
Yuan J, Zhan YA, Abskharon R, Xiao X, Martinez MC, Zhou X, Kneale G, Mikol J, Lehmann S, Surewicz WK, Castilla J, Steyaert J, Zhang S, Kong Q, Petersen RB, et al. Recombinant human prion protein inhibits prion propagation in vitro. Scientific Reports. 3: 2911. PMID 24105336 DOI: 10.1038/Srep02911 |
0.431 |
|
| 2013 |
Dutta A, Chen S, Surewicz WK. The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein. Febs Letters. 587: 2918-23. PMID 23892077 DOI: 10.1016/J.Febslet.2013.07.023 |
0.421 |
|
| 2013 |
Kong Q, Mills JL, Kundu B, Li X, Qing L, Surewicz K, Cali I, Huang S, Zheng M, Swietnicki W, Sönnichsen FD, Gambetti P, Surewicz WK. Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo. Cell Reports. 4: 248-54. PMID 23871665 DOI: 10.1016/J.Celrep.2013.06.030 |
0.476 |
|
| 2013 |
Apostol MI, Perry K, Surewicz WK. Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. Journal of the American Chemical Society. 135: 10202-5. PMID 23808589 DOI: 10.1021/Ja403001Q |
0.452 |
|
| 2013 |
Mills JL, Surewicz K, Surewicz W, Soennichsen FD. Solution Nmr Structure Of The V209M Variant Of The Human Prion Protein (Residues 90-231) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2M8T/Pdb |
0.401 |
|
| 2012 |
Nieznanski K, Choi JK, Chen S, Surewicz K, Surewicz WK. Soluble prion protein inhibits amyloid-β (Aβ) fibrillization and toxicity. The Journal of Biological Chemistry. 287: 33104-8. PMID 22915585 DOI: 10.1074/Jbc.C112.400614 |
0.434 |
|
| 2012 |
Kim C, Haldiman T, Surewicz K, Cohen Y, Chen W, Blevins J, Sy MS, Cohen M, Kong Q, Telling GC, Surewicz WK, Safar JG. Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C). Plos Pathogens. 8: e1002835. PMID 22876179 DOI: 10.1371/Journal.Ppat.1002835 |
0.434 |
|
| 2012 |
Liang J, Wang W, Sorensen D, Medina S, Ilchenko S, Kiselar J, Surewicz WK, Booth SA, Kong Q. Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle. The Journal of Biological Chemistry. 287: 16510-20. PMID 22447932 DOI: 10.1074/Jbc.M112.360891 |
0.346 |
|
| 2011 |
Jones EM, Wu B, Surewicz K, Nadaud PS, Helmus JJ, Chen S, Jaroniec CP, Surewicz WK. Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils. The Journal of Biological Chemistry. 286: 42777-84. PMID 22002245 DOI: 10.1074/Jbc.M111.302539 |
0.48 |
|
| 2011 |
Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP. Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy. Journal of the American Chemical Society. 133: 13934-7. PMID 21827207 DOI: 10.1021/Ja206469Q |
0.43 |
|
| 2011 |
Surewicz WK, Apostol MI. Prion protein and its conformational conversion: a structural perspective. Topics in Current Chemistry. 305: 135-67. PMID 21630136 DOI: 10.1007/128_2011_165 |
0.486 |
|
| 2011 |
Apostol MI, Surewicz WK. Structural underpinnings of prion protein conversion. The Journal of Biological Chemistry. 286: le7; author reply Ie. PMID 21602283 DOI: 10.1074/Jbc.L110.213926 |
0.446 |
|
| 2011 |
Smirnovas V, Baron GS, Offerdahl DK, Raymond GJ, Caughey B, Surewicz WK. Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nature Structural & Molecular Biology. 18: 504-6. PMID 21441913 DOI: 10.1038/Nsmb.2035 |
0.428 |
|
| 2011 |
Gambetti P, Cali I, Notari S, Kong Q, Zou WQ, Surewicz WK. Molecular biology and pathology of prion strains in sporadic human prion diseases. Acta Neuropathologica. 121: 79-90. PMID 21058033 DOI: 10.1007/S00401-010-0761-3 |
0.386 |
|
| 2010 |
Chen S, Yadav SP, Surewicz WK. Interaction between human prion protein and amyloid-beta (Abeta) oligomers: role OF N-terminal residues. The Journal of Biological Chemistry. 285: 26377-83. PMID 20576610 DOI: 10.1074/Jbc.M110.145516 |
0.426 |
|
| 2010 |
Kim JI, Cali I, Surewicz K, Kong Q, Raymond GJ, Atarashi R, Race B, Qing L, Gambetti P, Caughey B, Surewicz WK. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. The Journal of Biological Chemistry. 285: 14083-7. PMID 20304915 DOI: 10.1074/Jbc.C110.113464 |
0.477 |
|
| 2010 |
Zou WQ, Langeveld J, Xiao X, Chen S, McGeer PL, Yuan J, Payne MC, Kang HE, McGeehan J, Sy MS, Greenspan NS, Kaplan D, Wang GX, Parchi P, Hoover E, ... ... Surewicz WK, et al. PrP conformational transitions alter species preference of a PrP-specific antibody. The Journal of Biological Chemistry. 285: 13874-84. PMID 20194495 DOI: 10.1074/Jbc.M109.088831 |
0.345 |
|
| 2010 |
Helmus JJ, Surewicz K, Surewicz WK, Jaroniec CP. Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. Journal of the American Chemical Society. 132: 2393-403. PMID 20121096 DOI: 10.1021/Ja909827V |
0.432 |
|
| 2010 |
Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC. Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. The Embo Journal. 29: 251-62. PMID 19927125 DOI: 10.1038/Emboj.2009.333 |
0.448 |
|
| 2009 |
Kim JI, Surewicz K, Gambetti P, Surewicz WK. The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro. Febs Letters. 583: 3671-5. PMID 19854187 DOI: 10.1016/J.Febslet.2009.10.049 |
0.442 |
|
| 2009 |
Pasupuleti M, Roupe M, Rydengård V, Surewicz K, Surewicz WK, Chalupka A, Malmsten M, Sörensen OE, Schmidtchen A. Antimicrobial activity of human prion protein is mediated by its N-terminal region. Plos One. 4: e7358. PMID 19809501 DOI: 10.1371/Journal.Pone.0007358 |
0.42 |
|
| 2009 |
Smirnovas V, Kim JI, Lu X, Atarashi R, Caughey B, Surewicz WK. Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange. The Journal of Biological Chemistry. 284: 24233-41. PMID 19596861 DOI: 10.1074/Jbc.M109.036558 |
0.472 |
|
| 2009 |
Cobb NJ, Surewicz WK. Prion diseases and their biochemical mechanisms. Biochemistry. 48: 2574-85. PMID 19239250 DOI: 10.1021/Bi900108V |
0.425 |
|
| 2008 |
Cobb NJ, Apetri AC, Surewicz WK. Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal alpha-helical domain. The Journal of Biological Chemistry. 283: 34704-11. PMID 18930924 DOI: 10.1074/Jbc.M806701200 |
0.475 |
|
| 2008 |
Ganchev DN, Cobb NJ, Surewicz K, Surewicz WK. Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy. Biophysical Journal. 95: 2909-15. PMID 18539633 DOI: 10.1529/Biophysj.108.133108 |
0.417 |
|
| 2008 |
Helmus JJ, Surewicz K, Nadaud PS, Surewicz WK, Jaroniec CP. Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 105: 6284-9. PMID 18436646 DOI: 10.1073/Pnas.0711716105 |
0.471 |
|
| 2008 |
Yuan J, Dong Z, Guo JP, McGeehan J, Xiao X, Wang J, Cali I, McGeer PL, Cashman NR, Bessen R, Surewicz WK, Kneale G, Petersen RB, Gambetti P, Zou WQ. Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions. Cellular and Molecular Life Sciences : Cmls. 65: 631-43. PMID 18193391 DOI: 10.1007/S00018-007-7478-Z |
0.364 |
|
| 2007 |
Cobb NJ, Sönnichsen FD, McHaourab H, Surewicz WK. Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proceedings of the National Academy of Sciences of the United States of America. 104: 18946-51. PMID 18025469 DOI: 10.1073/Pnas.0706522104 |
0.475 |
|
| 2007 |
Cobb NJ, Surewicz WK. Prion strains under the magnifying glass. Nature Structural & Molecular Biology. 14: 882-4. PMID 17912257 DOI: 10.1038/Nsmb1007-882 |
0.381 |
|
| 2007 |
Surewicz WK. Protein science: discriminating taste of prions. Nature. 447: 541-2. PMID 17538609 DOI: 10.1038/447541B |
0.388 |
|
| 2007 |
Lu X, Wintrode PL, Surewicz WK. Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proceedings of the National Academy of Sciences of the United States of America. 104: 1510-5. PMID 17242357 DOI: 10.1073/Pnas.0608447104 |
0.458 |
|
| 2007 |
Davoodi J, Wakarchuk WW, Carey PR, Surewicz WK. Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds. Biophysical Chemistry. 125: 453-61. PMID 17141401 DOI: 10.1016/J.Bpc.2006.10.006 |
0.31 |
|
| 2006 |
Surewicz WK, Jones EM, Apetri AC. The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro. Accounts of Chemical Research. 39: 654-62. PMID 16981682 DOI: 10.1021/Ar050226C |
0.468 |
|
| 2006 |
Apetri AC, Maki K, Roder H, Surewicz WK. Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. Journal of the American Chemical Society. 128: 11673-8. PMID 16939293 DOI: 10.1021/Ja063880B |
0.443 |
|
| 2006 |
Jones EM, Surewicz K, Surewicz WK. Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro. The Journal of Biological Chemistry. 281: 8190-6. PMID 16443601 DOI: 10.1074/Jbc.M513417200 |
0.479 |
|
| 2005 |
Apetri AC, Vanik DL, Surewicz WK. Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231. Biochemistry. 44: 15880-8. PMID 16313190 DOI: 10.1021/Bi051455+ |
0.445 |
|
| 2005 |
Jones EM, Surewicz WK. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell. 121: 63-72. PMID 15820679 DOI: 10.1016/J.Cell.2005.01.034 |
0.447 |
|
| 2004 |
Vanik DL, Surewicz KA, Surewicz WK. Molecular basis of barriers for interspecies transmissibility of mammalian prions. Molecular Cell. 14: 139-45. PMID 15068810 DOI: 10.1016/S1097-2765(04)00155-8 |
0.408 |
|
| 2004 |
Apetri AC, Surewicz K, Surewicz WK. The effect of disease-associated mutations on the folding pathway of human prion protein. The Journal of Biological Chemistry. 279: 18008-14. PMID 14761942 DOI: 10.1074/Jbc.M313581200 |
0.468 |
|
| 2003 |
Kundu B, Maiti NR, Jones EM, Surewicz KA, Vanik DL, Surewicz WK. Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proceedings of the National Academy of Sciences of the United States of America. 100: 12069-74. PMID 14519851 DOI: 10.1073/Pnas.2033281100 |
0.488 |
|
| 2003 |
Apetri AC, Surewicz WK. Atypical effect of salts on the thermodynamic stability of human prion protein. The Journal of Biological Chemistry. 278: 22187-92. PMID 12676939 DOI: 10.1074/Jbc.M302130200 |
0.444 |
|
| 2002 |
Vanik DL, Surewicz WK. Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form. The Journal of Biological Chemistry. 277: 49065-70. PMID 12372829 DOI: 10.1074/Jbc.M207511200 |
0.495 |
|
| 2002 |
Apetri AC, Surewicz WK. Kinetic intermediate in the folding of human prion protein. The Journal of Biological Chemistry. 277: 44589-92. PMID 12356762 DOI: 10.1074/Jbc.C200507200 |
0.466 |
|
| 2002 |
Moscardini M, Pistello M, Bendinelli M, Ficheux D, Miller JT, Gabus C, Le Grice SF, Surewicz WK, Darlix JL. Functional interactions of nucleocapsid protein of feline immunodeficiency virus and cellular prion protein with the viral RNA. Journal of Molecular Biology. 318: 149-59. PMID 12054775 DOI: 10.1016/S0022-2836(02)00092-X |
0.353 |
|
| 2001 |
Knaus KJ, Morillas M, Swietnicki W, Malone M, Surewicz WK, Yee VC. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nature Structural Biology. 8: 770-4. PMID 11524679 DOI: 10.1038/Nsb0901-770 |
0.462 |
|
| 2001 |
Morillas M, Vanik DL, Surewicz WK. On the Mechanism of α-Helix to β-Sheet Transition in the Recombinant Prion Protein† Biochemistry. 40: 6982-6987. PMID 11389614 DOI: 10.1021/Bi010232Q |
0.413 |
|
| 2001 |
Gabus C, Auxilien S, Péchoux C, Dormont D, Swietnicki W, Morillas M, Surewicz W, Nandi P, Darlix JL. The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. Journal of Molecular Biology. 307: 1011-21. PMID 11286552 DOI: 10.1006/Jmbi.2001.4544 |
0.389 |
|
| 2001 |
Gabus C, Derrington E, Leblanc P, Chnaiderman J, Dormont D, Swietnicki W, Morillas M, Surewicz WK, Marc D, Nandi P, Darlix JL. The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. The Journal of Biological Chemistry. 276: 19301-9. PMID 11278562 DOI: 10.1074/Jbc.M009754200 |
0.347 |
|
| 2001 |
Maiti NR, Surewicz WK. The role of disulfide bridge in the folding and stability of the recombinant human prion protein. Journal of Biological Chemistry. 276: 2427-2431. PMID 11069909 DOI: 10.1074/Jbc.M007862200 |
0.494 |
|
| 2000 |
Li R, Liu T, Wong BS, Pan T, Morillas M, Swietnicki W, O'Rourke K, Gambetti P, Surewicz WK, Sy MS. Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. Journal of Molecular Biology. 301: 567-73. PMID 10966770 DOI: 10.1006/Jmbi.2000.3986 |
0.373 |
|
| 2000 |
Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sönnichsen FD. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. The Journal of Biological Chemistry. 275: 33650-4. PMID 10954699 DOI: 10.1074/Jbc.C000483200 |
0.486 |
|
| 2000 |
Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins. The Journal of Biological Chemistry. 275: 4565-70. PMID 10671481 DOI: 10.1074/Jbc.275.7.4565 |
0.306 |
|
| 2000 |
Swietnicki W, Morillas M, Chen SG, Gambetti P, Surewicz WK. Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry. 39: 424-31. PMID 10631004 DOI: 10.1021/Bi991967M |
0.492 |
|
| 2000 |
Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Soennichsen FD. Human Prion Protein Mutant E200K Fragment 90-231 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Fkc/Pdb |
0.389 |
|
| 1999 |
Morillas M, Swietnicki W, Gambetti P, Surewicz WK. Membrane environment alters the conformational structure of the recombinant human prion protein. Journal of Biological Chemistry. 274: 36859-36865. PMID 10601237 DOI: 10.1074/Jbc.274.52.36859 |
0.437 |
|
| 1999 |
Das KP, Choo-Smith LP, Petrash JM, Surewicz WK. Insight into the secondary structure of non-native proteins bound to a molecular chaperone alpha-crystallin. An isotope-edited infrared spectroscopic study. The Journal of Biological Chemistry. 274: 33209-12. PMID 10559193 DOI: 10.1074/Jbc.274.47.33209 |
0.408 |
|
| 1998 |
Swietnicki W, Petersen RB, Gambetti P, Surewicz WK. Familial mutations and the thermodynamic stability of the recombinant human prion protein. The Journal of Biological Chemistry. 273: 31048-52. PMID 9813003 DOI: 10.1074/Jbc.273.47.31048 |
0.393 |
|
| 1998 |
Davoodi J, Wakarchuk WW, Surewicz WK, Carey PR. Scan-rate dependence in protein calorimetry: The reversible transitions of Bacillus circulans xylanase and a disulfide-bridge mutant Protein Science. 7: 1538-1544. PMID 9684886 DOI: 10.1002/Pro.5560070707 |
0.352 |
|
| 1998 |
Perrier V, Burlacu-Miron S, Bourgeois S, Surewicz WK, Gilles AM. Genetically engineered zinc-chelating adenylate kinase from Escherichia coli with enhanced thermal stability. Journal of Biological Chemistry. 273: 19097-19101. PMID 9668094 DOI: 10.1074/Jbc.273.30.19097 |
0.319 |
|
| 1997 |
Swietnicki W, Petersen R, Gambetti P, Surewicz WK. pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231) Journal of Biological Chemistry. 272: 27517-27520. PMID 9346881 DOI: 10.1074/Jbc.272.44.27517 |
0.448 |
|
| 1997 |
Butko P, Huang F, Pusztai-Carey M, Surewicz WK. Interaction of the δ-endotoxin CytA from Bacillus thuringiensis var. israelensis with lipid membranes Biochemistry. 36: 12862-12868. PMID 9335544 DOI: 10.1021/Bi9702389 |
0.307 |
|
| 1997 |
Choo-Smith LP, Garzon-Rodriguez W, Glabe CG, Surewicz WK. Acceleration of amyloid fibril formation by specific binding of Abeta-(1-40) peptide to ganglioside-containing membrane vesicles. The Journal of Biological Chemistry. 272: 22987-90. PMID 9287293 DOI: 10.1074/Jbc.272.37.22987 |
0.337 |
|
| 1997 |
Sayre LM, Zagorski MG, Surewicz WK, Krafft GA, Perry G. Mechanisms of neurotoxicity associated with amyloid beta deposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal. Chemical Research in Toxicology. 10: 518-26. PMID 9168248 DOI: 10.1021/Tx970009N |
0.316 |
|
| 1997 |
Choo-Smith LPI, Surewicz WK. The interaction between Alzheimer amyloid β(1–40) peptide and ganglioside GM1‐containing membranes Febs Letters. 402: 95-98. PMID 9037173 DOI: 10.1016/S0014-5793(96)01504-9 |
0.388 |
|
| 1996 |
Serina L, Bucurenci N, Gilles AM, Surewicz WK, Fabian H, Mantsch HH, Takahashi M, Petrescu I, Batelier G, Bârzu O. Structural Properties of UMP-Kinase from Escherichia coli: Modulation of Protein Solubility by pH and UTP† Biochemistry. 35: 7003-7011. PMID 8679525 DOI: 10.1021/Bi960062V |
0.36 |
|
| 1996 |
Das KP, Petrash JM, Surewicz WK. Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin. The Journal of Biological Chemistry. 271: 10449-52. PMID 8631839 DOI: 10.1074/Jbc.271.18.10449 |
0.377 |
|
| 1995 |
Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. Febs Letters. 369: 321-5. PMID 7649280 DOI: 10.1016/0014-5793(95)00775-5 |
0.361 |
|
| 1995 |
Surewicz WK, Olesen PR. On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy Biochemistry. 34: 9655-9660. PMID 7626634 DOI: 10.1021/Bi00030A001 |
0.384 |
|
| 1995 |
Das KP, Surewicz WK. On the substrate specificity of alpha-crystallin as a molecular chaperone. The Biochemical Journal. 311: 367-70. PMID 7487869 DOI: 10.1042/Bj3110367 |
0.361 |
|
| 1995 |
Davoodi J, Wakarchuk WW, Campbell RL, Carey PR, Surewicz WK. Abnormally High pK a of an Active-Site Glutamic Acid Residue in Bacillus Circulans Xylanase. The Role of Electrostatic Interactions European Journal of Biochemistry. 232: 839-843. DOI: 10.1111/J.1432-1033.1995.Tb20881.X |
0.336 |
|
| 1995 |
Davoodi J, Wakarchuk WW, Campbell RL, Carey PR, Surewicz WK. Abnormally High pKa of an Active‐Site Glutamic Acid Residue in Bacillus Circulans Xylanase Febs Journal. 232: 839-843. DOI: 10.1111/J.1432-1033.1995.0839A.X |
0.333 |
|
| 1994 |
Muga A, Neugebauer W, Hirama T, Surewicz WK. Membrane Interaction and Conformational Properties of the Putative Fusion Peptide of PH-30, a Protein Active in Sperm-Egg Fusion Biochemistry. 33: 4444-4448. PMID 8161498 DOI: 10.1021/Bi00181A002 |
0.373 |
|
| 1994 |
Perrier V, Surewicz WK, Glaser P, Martineau L, Craescu CT, Fabian H, Mantsch HH, Barzu O, Gilles A. Zinc chelation and structural stability of adenylate kinase from Bacillus subtilis Biochemistry. 33: 9960-9967. PMID 8061005 DOI: 10.1021/Bi00199A019 |
0.322 |
|
| 1994 |
Fraser PE, McLachlan DR, Surewicz WK, Mizzen CA, Snow AD, Nguyen JT, Kirschner DA. Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues. Journal of Molecular Biology. 244: 64-73. PMID 7966323 DOI: 10.1006/Jmbi.1994.1704 |
0.38 |
|
| 1993 |
Surewicz WK, Mantsch HH, Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment Biochemistry. 32: 389-394. PMID 8422346 DOI: 10.1021/Bi00053A001 |
0.352 |
|
| 1993 |
Gilles A, Sismeiro O, Munier H, Fabian H, Mantsch HH, Surewicz WK, Craescu CC, Barzu O, Danchin A. Structural and physico-chemical characteristics of Bordetella pertussis adenylate kinase, a tryptophan-containing enzyme Febs Journal. 218: 921-927. PMID 8281944 DOI: 10.1111/J.1432-1033.1993.Tb18448.X |
0.308 |
|
| 1993 |
Kallwass HK, Surewicz WK, Parris W, Macfarlane EL, Luyten MA, Kay CM, Gold M, Jones JB. Single amino acid substitutions can further increase the stability of a thermophilic L-lactate dehydrogenase. Protein Engineering. 5: 769-74. PMID 1287656 DOI: 10.1093/Protein/5.8.769 |
0.344 |
|
| 1992 |
Epand RM, Gabel B, Epand RF, Sen A, Hui SW, Muga A, Surewicz WK. Formation of a new stable phase of phosphatidylglycerols. Biophysical Journal. 63: 327-32. PMID 1420881 DOI: 10.1016/S0006-3495(92)81618-1 |
0.307 |
|
| 1992 |
Fraser PE, Nguyen JT, Inouye H, Surewicz WK, Selkoe DJ, Podlisny MB, Kirschner DA. Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein. Biochemistry. 31: 10716-23. PMID 1420187 DOI: 10.1021/Bi00159A011 |
0.397 |
|
| 1992 |
Neugebauer W, Surewicz WK, Gordon HL, Somorjai RL, Sung W, Willick GE. Structural elements of human parathyroid hormone and their possible relation to biological activities. Biochemistry. 31: 2056-63. PMID 1311201 DOI: 10.1021/Bi00122A023 |
0.387 |
|
| 1991 |
Labruyere E, Mock M, Surewicz WK, Mantsch HH, Rose T, Munier H, Sarfati RS, Barzu O. Structural and ligand-binding properties of a truncated form of Bacillus anthracis adenylate cyclase and of a catalytically inactive variant in which glutamine substitutes for lysine-346. Biochemistry. 30: 2619-2624. PMID 1900429 DOI: 10.1021/Bi00224A008 |
0.4 |
|
| 1991 |
Choma CT, Surewicz WK, Kaplan H. The toxic moiety of the Bacillus thuringiensis protoxin undergoes a conformational change upon activation. Biochemical and Biophysical Research Communications. 179: 933-8. PMID 1898414 DOI: 10.1016/0006-291X(91)91908-U |
0.37 |
|
| 1991 |
Muga A, Mantsch HH, Surewicz WK. Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy. Biochemistry. 30: 2629-2635. PMID 1848092 DOI: 10.1021/Bi00224A010 |
0.416 |
|
| 1991 |
Fraser PE, Nguyen JT, Surewicz WK, Kirschner DA. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophysical Journal. 60: 1190-201. PMID 1760507 DOI: 10.1016/S0006-3495(91)82154-3 |
0.399 |
|
| 1991 |
Muga A, Mantsch HH, Surewicz WK. Membrane binding induces destabilization of cytochrome c structure. Biochemistry. 30: 7219-7224. PMID 1649625 DOI: 10.1021/Bi00243A025 |
0.389 |
|
| 1990 |
Choma CT, Surewicz WK, Carey PR, Pozsgay M, Kaplan H. Secondary structure of the entomocidal toxin from Bacillus thuringiensis subsp. kurstaki HD-73 Journal of Protein Chemistry. 9: 87-94. PMID 2340079 DOI: 10.1007/Bf01024989 |
0.329 |
|
| 1990 |
Muga A, Surewicz WK, Wong PTT, Mantsch HH. Structural studies with the uveopathogenic peptide M derived from retinal S-antigen. Biochemistry. 29: 2925-2930. PMID 2337574 DOI: 10.1021/Bi00464A006 |
0.362 |
|
| 1990 |
Surewicz WK, Leddy JJ, Mantsch HH. Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy. Biochemistry. 29: 8106-11. PMID 2261465 DOI: 10.1021/Bi00487A017 |
0.322 |
|
| 1990 |
Choma CT, Surewicz WK, Carey PR, Pozsgay M, Raynor T, Kaplan H. Unusual proteolysis of the protoxin and toxin from Bacillus thuringiensis. Structural implications European Journal of Biochemistry. 189: 523-527. PMID 2190826 DOI: 10.1111/J.1432-1033.1990.Tb15518.X |
0.336 |
|
| 1990 |
Surewicz WK, Mantsch HH. The conformation of proteins and peptides in a membrane environment: an infrared spectroscopic approach. Biotechnology(Faisalabad). 14: 131-157. PMID 2183896 DOI: 10.1016/B978-0-409-90116-0.50015-7 |
0.368 |
|
| 1990 |
Whitaker JN, Moscarello MA, Herman PK, Epand RM, Surewicz WK. Conformational correlates of the epitopes of human myelin basic protein peptide 80-89. Journal of Neurochemistry. 55: 568-76. PMID 1695239 DOI: 10.1111/J.1471-4159.1990.Tb04171.X |
0.365 |
|
| 1989 |
Surewicz WK, Surewicz K, Mantsch HH, Auclair F. Interaction of Shigella toxin with globotriaosyl ceramide receptor-containing membranes: a fluorescence study. Biochemical and Biophysical Research Communications. 160: 126-132. PMID 2653314 DOI: 10.1016/0006-291X(89)91630-6 |
0.302 |
|
| 1988 |
Surewicz WK, Mantsch HH. Solution and membrane structure of enkephalins as studied by infrared spectroscopy Biochemical and Biophysical Research Communications. 150: 245-251. PMID 3337714 DOI: 10.1016/0006-291X(88)90512-8 |
0.351 |
|
| 1988 |
Surewicz WK, Mantsch HH. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochimica Et Biophysica Acta. 952: 115-130. PMID 3276352 DOI: 10.1016/0167-4838(88)90107-0 |
0.372 |
|
| 1988 |
Epand RM, Surewicz WK, Yeagle P. Role of peptide structure in lipid-peptide interactions: nuclear magnetic resonance study of the interaction of pentagastrin and [Arg4]pentagastrin with dimyristoylphosphatidylcholine. Chemistry and Physics of Lipids. 49: 105-10. PMID 3233705 DOI: 10.1016/0009-3084(88)90071-0 |
0.322 |
|
| 1987 |
Surewicz WK, Epand RM, Orlowski RC, Mantsch HH. Structural properties of acidic phospholipids in complexes with calcitonin: a Fourier transform infrared spectroscopic investigation. Biochimica Et Biophysica Acta. 899: 307-310. PMID 3580371 DOI: 10.1016/0005-2736(87)90413-5 |
0.326 |
|
| 1987 |
Surewicz WK, Szabo AG, Mantsch HH. Conformational properties of azurin in solution as determined from resolution-enhanced Fourier-transform infrared spectra European Journal of Biochemistry. 167: 519-523. PMID 3115776 DOI: 10.1111/J.1432-1033.1987.Tb13368.X |
0.395 |
|
| 1987 |
Surewicz WK, Mantsch HH, Stahl GL, Epand RM. Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide. Proceedings of the National Academy of Sciences of the United States of America. 84: 7028-7030. PMID 2959955 DOI: 10.1073/Pnas.84.20.7028 |
0.385 |
|
| 1987 |
Surewicz WK, Moscarello MA, Mantsch HH. Fourier transform infrared spectroscopic investigation of the interaction between myelin basic protein and dimyristoylphosphatidylglycerol bilayers. Biochemistry. 26: 3881-6. PMID 2443163 DOI: 10.1021/Bi00387A021 |
0.441 |
|
| 1986 |
Surewicz WK, Epand RM. Phospholipid structure determines the effects of peptides on membranes. Differential scanning calorimetry studies with pentagastrin-related peptides. Biochimica Et Biophysica Acta. 856: 290-300. PMID 3955044 DOI: 10.1016/0005-2736(86)90039-8 |
0.328 |
|
| 1986 |
Surewicz WK, Epand RM, Epand RF, Hallett FR, Moscarello MA. Modulation of myelin basic protein-induced aggregation and fusion of liposomes by cholesterol, aliphatic aldehydes and alkanes. Biochimica Et Biophysica Acta. 863: 45-52. PMID 2430621 DOI: 10.1016/0005-2736(86)90385-8 |
0.356 |
|
| 1985 |
Surewicz WK, Epand RM. Role of peptide structure in lipid-peptide interactions: high-sensitivity differential scanning calorimetry and electron spin resonance studies of the structural properties of dimyristoylphosphatidylcholine membranes interacting with pentagastrin-related pentapeptides. Biochemistry. 24: 3135-3144. PMID 2992577 DOI: 10.1021/Bi00334A010 |
0.328 |
|
| 1985 |
Surewicz WK, Epand RM, Vail WJ, Moscarello MA. Aliphatic aldehydes promote myelin basic protein-induced fusion of phospholipid vesicles. Biochimica Et Biophysica Acta. 820: 319-23. PMID 2413893 DOI: 10.1016/0005-2736(85)90127-0 |
0.334 |
|
| 1984 |
Surewicz WK, Epand RM. Role of peptide structure in lipid-peptide interactions: a fluorescence study of the binding of pentagastrin-related pentapeptides to phospholipid vesicles. Biochemistry. 23: 6072-6077. PMID 6525344 DOI: 10.1021/Bi00320A026 |
0.358 |
|
| 1984 |
Epand RM, Dell K, Surewicz WK, Moscarello MA. Effect of lipid structure on the capacity of myelin basic protein to alter vesicle properties: potent effects of aliphatic aldehydes in promoting basic protein-induced vesicle aggregation. Journal of Neurochemistry. 43: 1550-5. PMID 6208335 DOI: 10.1111/J.1471-4159.1984.Tb06077.X |
0.392 |
|
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