Year |
Citation |
Score |
2023 |
Sun Y, Jack K, Ercolani T, Sangar D, Hosszu L, Collinge J, Bieschke J. Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics. Acs Nano. PMID 36802500 DOI: 10.1021/acsnano.2c12009 |
0.334 |
|
2022 |
Jack K, Jackson GS, Bieschke J. Essential Components of Synthetic Infectious Prion Formation De Novo. Biomolecules. 12. PMID 36421708 DOI: 10.3390/biom12111694 |
0.302 |
|
2021 |
Nahass GR, Sun Y, Xu Y, Batchelor M, Reilly M, Benilova I, Kedia N, Spehar K, Sobott F, Sessions RB, Caughey BW, Radford SE, Jat P, Collinge J, Bieschke J. Brazilin Removes Toxic alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium. Journal of Molecular Biology. 166878. PMID 33610557 DOI: 10.1016/j.jmb.2021.166878 |
0.746 |
|
2020 |
Verzini S, Shah M, Theillet FX, Belsom A, Bieschke J, Wanker EE, Rappsilber J, Binolfi A, Selenko P. Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal Dynamics. Journal of Molecular Biology. 432: 166689. PMID 33211011 DOI: 10.1016/j.jmb.2020.10.023 |
0.414 |
|
2020 |
Sun Y, Batchelor M, Collinge J, Bieschke J. Direct Observation of Prion Protein Fibril Elongation Kinetics Biophysical Journal. 118: 484a. DOI: 10.1016/J.Bpj.2019.11.2681 |
0.395 |
|
2019 |
Kedia N, Arhzaouy K, Pittman SK, Sun Y, Batchelor M, Weihl CC, Bieschke J. Desmin forms toxic, seeding-competent amyloid aggregates that persist in muscle fibers. Proceedings of the National Academy of Sciences of the United States of America. PMID 31371504 DOI: 10.1016/J.Bpj.2019.11.1201 |
0.808 |
|
2019 |
French RL, Grese ZR, Aligireddy H, Dhavale DD, Reeb AN, Kedia N, Kotzbauer PT, Bieschke J, Ayala YM. Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation. The Journal of Biological Chemistry. PMID 30824544 DOI: 10.1074/Jbc.Ra118.005889 |
0.775 |
|
2018 |
Spehar K, Ding T, Sun Y, Kedia N, Lu J, Nahass GR, Lew MD, Bieschke J. Super-Resolution Imaging of Amyloid Structures over Extended Times Using Transient Binding of Single Thioflavin T Molecules. Chembiochem : a European Journal of Chemical Biology. PMID 29953718 DOI: 10.1016/J.Bpj.2018.11.2471 |
0.792 |
|
2018 |
Spehar K, Ding T, Sun Y, Lu J, Nahass GR, Lew MD, Bieschke J. Long-Term Super-Resolution Imaging of Amyloid Structures using Transient Binding of Standard Amyloid Probes Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.1934 |
0.43 |
|
2018 |
Spehar K, Ding T, Sun Y, Kedia N, Lu J, Nahass GR, Lew MD, Bieschke J. Cover Feature: Super-resolution Imaging of Amyloid Structures over Extended Times by Using Transient Binding of Single Thioflavin T Molecules (ChemBioChem 18/2018) Chembiochem. 19: 1897-1897. DOI: 10.1002/Cbic.201800489 |
0.728 |
|
2017 |
Kedia N, Almisry M, Bieschke J. Glucose directs amyloid-beta into membrane-active oligomers. Physical Chemistry Chemical Physics : Pccp. PMID 28671211 DOI: 10.1039/C7Cp02849K |
0.788 |
|
2017 |
Weihl C, Bieschke J. Prion-like protein aggregation of desmin myofibrillar myopathies Neuromuscular Disorders. 27: S247-S248. DOI: 10.1016/j.nmd.2017.06.548 |
0.354 |
|
2016 |
Andrich K, Hegenbart U, Kimmich C, Kedia N, Bergen HR, Schönland S, Wanker EE, Bieschke J. Aggregation of Full Length Immunoglobulin Light Chains from AL Amyloidosis Patients Is Remodeled by Epigallocatechin-3-gallate. The Journal of Biological Chemistry. PMID 28031465 DOI: 10.1074/Jbc.M116.750323 |
0.788 |
|
2016 |
Jin S, Kedia N, Illes-Toth E, Haralampiev I, Prisner S, Herrmann A, Wanker EE, Bieschke J. Amyloid-β 1-42 Aggregation Initiates Its Cellular Uptake and Cytotoxicity. The Journal of Biological Chemistry. PMID 27458018 DOI: 10.1074/Jbc.M115.691840 |
0.808 |
|
2016 |
Lam HT, Graber MC, Gentry KA, Bieschke J. Stabilization of α-Synuclein Fibril Clusters Prevents Fragmentation and Reduces Seeding Activity and Toxicity. Biochemistry. PMID 26799377 DOI: 10.1021/Acs.Biochem.5B01168 |
0.525 |
|
2016 |
Eva I, Maliha S, Nelson W, Silvia V, Philipp S, Erich WE, Bieschke J. Unconventional Chaperone Inhibits Amyloid Formation by Promoting off-Pathway Aggregation Biophysical Journal. 110: 551a-552a. DOI: 10.1016/J.Bpj.2015.11.2950 |
0.54 |
|
2015 |
Andrich K, Bieschke J. The Effect of (-)-Epigallo-catechin-(3)-gallate on Amyloidogenic Proteins Suggests a Common Mechanism. Advances in Experimental Medicine and Biology. 863: 139-61. PMID 26092630 DOI: 10.1007/978-3-319-18365-7_7 |
0.545 |
|
2015 |
Mirbaha H, Holmes BB, Sanders DW, Bieschke J, Diamond MI. Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation. The Journal of Biological Chemistry. 290: 14893-903. PMID 25887395 DOI: 10.1074/Jbc.M115.652693 |
0.47 |
|
2015 |
Wobst HJ, Sharma A, Diamond MI, Wanker EE, Bieschke J. The green tea polyphenol (-)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios. Febs Letters. 589: 77-83. PMID 25436420 DOI: 10.1016/J.Febslet.2014.11.026 |
0.586 |
|
2015 |
Andrich K, Hegenbart U, Schönland S, Wanker E, Bieschke J. Amyloidogenicity of Immunoglobulin Light Chains Biophysical Journal. 108: 386a. DOI: 10.1016/J.Bpj.2014.11.2117 |
0.478 |
|
2015 |
Jin S, Nikolaus J, Herrmann A, Bieschke J. Membrane Interaction of Amyloid-Beta Peptide Induces Spontaneous Membrane Invagination Biophysical Journal. 108: 256a. DOI: 10.1016/J.Bpj.2014.11.1415 |
0.485 |
|
2014 |
Andrich K, Bieschke J. Aggregation in AL Amyloidosis Biophysical Journal. 106: 58a. DOI: 10.1016/J.Bpj.2013.11.401 |
0.504 |
|
2014 |
Jin S, Herrmann A, Bieschke J. Amyloid-β42 Aggregation on Cellular Membranes Facilitates its Cellular Uptake Biophysical Journal. 106: 471a. DOI: 10.1016/J.Bpj.2013.11.2665 |
0.596 |
|
2013 |
Murray AN, Palhano FL, Bieschke J, Kelly JW. Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes. Protein Science : a Publication of the Protein Society. 22: 1531-41. PMID 23963844 DOI: 10.1002/Pro.2339 |
0.747 |
|
2013 |
Bieschke J. Natural compounds may open new routes to treatment of amyloid diseases. Neurotherapeutics : the Journal of the American Society For Experimental Neurotherapeutics. 10: 429-39. PMID 23670234 DOI: 10.1007/S13311-013-0192-7 |
0.586 |
|
2012 |
Lopez del Amo JM, Fink U, Dasari M, Grelle G, Wanker EE, Bieschke J, Reif B. Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers. Journal of Molecular Biology. 421: 517-24. PMID 22300765 DOI: 10.1016/J.Jmb.2012.01.013 |
0.502 |
|
2012 |
Bieschke J, Herbst M, Wiglenda T, Friedrich RP, Boeddrich A, Schiele F, Kleckers D, Lopez del Amo JM, Grüning BA, Wang Q, Schmidt MR, Lurz R, Anwyl R, Schnoegl S, Fändrich M, et al. Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils. Nature Chemical Biology. 8: 93-101. PMID 22101602 DOI: 10.1038/Nchembio.719 |
0.573 |
|
2012 |
Sommer AP, Bieschke J, Friedrich RP, Zhu D, Wanker EE, Fecht HJ, Mereles D, Hunstein W. 670 nm laser light and EGCG complementarily reduce amyloid-β aggregates in human neuroblastoma cells: basis for treatment of Alzheimer's disease? Photomedicine and Laser Surgery. 30: 54-60. PMID 22029866 DOI: 10.1089/Pho.2011.3073 |
0.421 |
|
2012 |
Priller J, Nicoletti C, Bounab Y, Grohmann M, Foulle R, Bieschke J, Zabel C, Lalowski M, Wanker E. B16 Collapsin response mediator protein 4 downregulates aggregation and toxicity of mutant huntingtin Journal of Neurology, Neurosurgery & Psychiatry. 83: A10.3-A10. DOI: 10.1136/jnnp-2012-303524.32 |
0.315 |
|
2012 |
Bieschke J. Small Molecule Induced Conversion of Toxic Oligomers to Non-Toxic Beta-Sheet-Rich Amyloid Fibrils Biophysical Journal. 102: 454a-455a. DOI: 10.1016/J.Bpj.2011.11.2494 |
0.593 |
|
2012 |
Jin S, Bieschke J. Cellular Internalization of Monomeric and Oligomeric Amyloid-Beta 42 Peptide Biophysical Journal. 102: 442a-443a. DOI: 10.1016/J.Bpj.2011.11.2424 |
0.588 |
|
2011 |
Grelle G, Otto A, Lorenz M, Frank RF, Wanker EE, Bieschke J. Black tea theaflavins inhibit formation of toxic amyloid-β and α-synuclein fibrils. Biochemistry. 50: 10624-36. PMID 22054421 DOI: 10.1021/Bi2012383 |
0.595 |
|
2011 |
Dasari M, Espargaro A, Sabate R, Lopez del Amo JM, Fink U, Grelle G, Bieschke J, Ventura S, Reif B. Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states. Chembiochem : a European Journal of Chemical Biology. 12: 407-23. PMID 21290543 DOI: 10.1002/Cbic.201000602 |
0.564 |
|
2010 |
Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, Wanker EE. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. Proceedings of the National Academy of Sciences of the United States of America. 107: 7710-5. PMID 20385841 DOI: 10.1073/Pnas.0910723107 |
0.542 |
|
2009 |
Bieschke J, Cohen E, Murray A, Dillin A, Kelly JW. A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis. Protein Science : a Publication of the Protein Society. 18: 2231-41. PMID 19701939 DOI: 10.1002/Pro.234 |
0.622 |
|
2008 |
Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, Engemann S, Pastore A, Wanker EE. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature Structural & Molecular Biology. 15: 558-66. PMID 18511942 DOI: 10.1038/Nsmb.1437 |
0.566 |
|
2008 |
Bieschke J, Siegel SJ, Fu Y, Kelly JW. Alzheimer's Abeta peptides containing an isostructural backbone mutation afford distinct aggregate morphologies but analogous cytotoxicity. Evidence for a common low-abundance toxic structure(s)? Biochemistry. 47: 50-9. PMID 18078350 DOI: 10.1021/Bi701757V |
0.761 |
|
2007 |
Siegel SJ, Bieschke J, Powers ET, Kelly JW. The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation. Biochemistry. 46: 1503-10. PMID 17279615 DOI: 10.1021/Bi061853S |
0.796 |
|
2007 |
Herbst M, Bieschke J, Wang Q, Lurz R, Boeddrich A, Otto A, Anwyl R, Walsh D, Wanker E. Induction of fibril-like beta-amyloid aggregates by a natural substance decreases soluble oligomers and protects from neurotoxicity Aktuelle Neurologie. 34. DOI: 10.1055/s-2007-987948 |
0.413 |
|
2006 |
Fu Y, Gao J, Bieschke J, Dendle MA, Kelly JW. Amide-to-E-olefin versus amide-to-ester backbone H-bond perturbations: Evaluating the O-O repulsion for extracting H-bond energies. Journal of the American Chemical Society. 128: 15948-9. PMID 17165703 DOI: 10.1021/Ja065303T |
0.59 |
|
2006 |
Bieschke J, Zhang Q, Bosco DA, Lerner RA, Powers ET, Wentworth P, Kelly JW. Small molecule oxidation products trigger disease-associated protein misfolding. Accounts of Chemical Research. 39: 611-9. PMID 16981677 DOI: 10.1021/Ar0500766 |
0.772 |
|
2006 |
Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A. Opposing activities protect against age-onset proteotoxicity. Science (New York, N.Y.). 313: 1604-10. PMID 16902091 DOI: 10.1126/Science.1124646 |
0.614 |
|
2006 |
Jäger M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW. Structure-function-folding relationship in a WW domain. Proceedings of the National Academy of Sciences of the United States of America. 103: 10648-53. PMID 16807295 DOI: 10.1073/Pnas.0600511103 |
0.497 |
|
2005 |
Fu Y, Bieschke J, Kelly JW. E-olefin dipeptide isostere incorporation into a polypeptide backbone enables hydrogen bond perturbation: probing the requirements for Alzheimer's amyloidogenesis. Journal of the American Chemical Society. 127: 15366-7. PMID 16262389 DOI: 10.1021/Ja0551382 |
0.604 |
|
2005 |
Giese A, Bader B, Bieschke J, Schaffar G, Odoy S, Kahle PJ, Haass C, Kretzschmar H. Single particle detection and characterization of synuclein co-aggregation. Biochemical and Biophysical Research Communications. 333: 1202-10. PMID 15978545 DOI: 10.1016/J.Bbrc.2005.06.025 |
0.532 |
|
2005 |
Sarafoff NI, Bieschke J, Giese A, Weber P, Bertsch U, Kretzschmar HA. Automated PrPres amplification using indirect sonication. Journal of Biochemical and Biophysical Methods. 63: 213-21. PMID 15967508 DOI: 10.1016/J.Jbbm.2005.05.004 |
0.313 |
|
2005 |
Bertsch U, Winklhofer KF, Hirschberger T, Bieschke J, Weber P, Hartl FU, Tavan P, Tatzelt J, Kretzschmar HA, Giese A. Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets. Journal of Virology. 79: 7785-91. PMID 15919931 DOI: 10.1128/Jvi.79.12.7785-7791.2005 |
0.432 |
|
2005 |
Bieschke J, Zhang Q, Powers ET, Lerner RA, Kelly JW. Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a two-step mechanism, eliminating the requirement for nucleation. Biochemistry. 44: 4977-83. PMID 15794636 DOI: 10.1021/Bi0501030 |
0.812 |
|
2004 |
Bieschke J, Weber P, Sarafoff N, Beekes M, Giese A, Kretzschmar H. Autocatalytic self-propagation of misfolded prion protein. Proceedings of the National Academy of Sciences of the United States of America. 101: 12207-11. PMID 15297610 DOI: 10.1073/Pnas.0404650101 |
0.351 |
|
2004 |
Zhang Q, Powers ET, Nieva J, Huff ME, Dendle MA, Bieschke J, Glabe CG, Eschenmoser A, Wentworth P, Lerner RA, Kelly JW. Metabolite-initiated protein misfolding may trigger Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. 101: 4752-7. PMID 15034169 DOI: 10.1073/Pnas.0400924101 |
0.776 |
|
2000 |
Giese A, Bieschke J, Eigen M, Kretzschmar HA. Putting prions into focus: application of single molecule detection to the diagnosis of prion diseases. Archives of Virology. Supplementum. 161-71. PMID 11214919 DOI: 10.1007/978-3-7091-6308-5_15 |
0.599 |
|
2000 |
Bieschke J, Giese A, Schulz-Schaeffer W, Zerr I, Poser S, Eigen M, Kretzschmar H. Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets. Proceedings of the National Academy of Sciences of the United States of America. 97: 5468-73. PMID 10805803 DOI: 10.1073/Pnas.97.10.5468 |
0.635 |
|
1998 |
Koltermann A, Kettling U, Bieschke J, Winkler T, Eigen M. Rapid assay processing by integration of dual-color fluorescence cross-correlation spectroscopy: high throughput screening for enzyme activity. Proceedings of the National Academy of Sciences of the United States of America. 95: 1421-6. PMID 9465030 DOI: 10.1073/Pnas.95.4.1421 |
0.531 |
|
1997 |
Schwille P, Bieschke J, Oehlenschläger F. Kinetic investigations by fluorescence correlation spectroscopy: the analytical and diagnostic potential of diffusion studies. Biophysical Chemistry. 66: 211-28. PMID 9362560 DOI: 10.1016/S0301-4622(97)00061-6 |
0.466 |
|
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