Jan Bieschke, Ph.D. - Publications

Affiliations: 
Biomedical Engineering Washington University, Saint Louis, St. Louis, MO 
Area:
Protein folding and misfolding
Website:
http://engineering.wustl.edu/facultybio.aspx?faculty=569

40 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 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: 10.1073/pnas.1908263116  1
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  1
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: 10.1002/cbic.201800352  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2013 Drey LL, Graber MC, Bieschke J. Counting unstained, confluent cells by modified bright-field microscopy. Biotechniques. 55: 28-33. PMID 23834382 DOI: 10.2144/000114056  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2010 Bieschke J, Paul F. Plant ingredients: Green tea - New insights on an old drug | Pflanzeiminhaltsstoffe: Grüner Tee - Neue Einsichten für einen alten Wirkstoff Chemie in Unserer Zeit. 44: 306-307. DOI: 10.1002/ciuz.201090055  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2000 Dürig J, Giese A, Schulz-Schaeffer W, Rosenthal C, Schmücker U, Bieschke J, Dührsen U, Kretzschmar HA. Differential constitutive and activation-dependent expression of prion protein in human peripheral blood leucocytes. British Journal of Haematology. 108: 488-95. PMID 10759704 DOI: 10.1046/j.1365-2141.2000.01881.x  1
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  1
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  1
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