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Items: 39

1.

Desmin forms toxic, seeding-competent amyloid aggregates that persist in muscle fibers.

Kedia N, Arhzaouy K, Pittman SK, Sun Y, Batchelor M, Weihl CC, Bieschke J.

Proc Natl Acad Sci U S A. 2019 Aug 20;116(34):16835-16840. doi: 10.1073/pnas.1908263116. Epub 2019 Aug 1.

2.

Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation.

French RL, Grese ZR, Aligireddy H, Dhavale DD, Reeb AN, Kedia N, Kotzbauer PT, Bieschke J, Ayala YM.

J Biol Chem. 2019 Apr 26;294(17):6696-6709. doi: 10.1074/jbc.RA118.005889. Epub 2019 Mar 1.

PMID:
30824544
3.

Super-resolution Imaging of Amyloid Structures over Extended Times by Using Transient Binding of Single Thioflavin T Molecules.

Spehar K, Ding T, Sun Y, Kedia N, Lu J, Nahass GR, Lew MD, Bieschke J.

Chembiochem. 2018 Sep 17;19(18):1944-1948. doi: 10.1002/cbic.201800352. Epub 2018 Aug 8.

4.

Glucose directs amyloid-beta into membrane-active oligomers.

Kedia N, Almisry M, Bieschke J.

Phys Chem Chem Phys. 2017 Jul 21;19(27):18036-18046. doi: 10.1039/c7cp02849k. Epub 2017 Jul 3.

5.

Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.

Andrich K, Hegenbart U, Kimmich C, Kedia N, Bergen HR 3rd, Schönland S, Wanker E, Bieschke J.

J Biol Chem. 2017 Feb 10;292(6):2328-2344. doi: 10.1074/jbc.M116.750323. Epub 2016 Dec 28.

6.

Amyloid-β(1-42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity.

Jin S, Kedia N, Illes-Toth E, Haralampiev I, Prisner S, Herrmann A, Wanker EE, Bieschke J.

J Biol Chem. 2016 Sep 9;291(37):19590-606. doi: 10.1074/jbc.M115.691840. Epub 2016 Jul 25.

7.

Stabilization of α-Synuclein Fibril Clusters Prevents Fragmentation and Reduces Seeding Activity and Toxicity.

Lam HT, Graber MC, Gentry KA, Bieschke J.

Biochemistry. 2016 Feb 2;55(4):675-85. doi: 10.1021/acs.biochem.5b01168. Epub 2016 Jan 22.

8.

The Effect of (-)-Epigallo-catechin-(3)-gallate on Amyloidogenic Proteins Suggests a Common Mechanism.

Andrich K, Bieschke J.

Adv Exp Med Biol. 2015;863:139-61. doi: 10.1007/978-3-319-18365-7_7.

9.

Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation.

Mirbaha H, Holmes BB, Sanders DW, Bieschke J, Diamond MI.

J Biol Chem. 2015 Jun 12;290(24):14893-903. doi: 10.1074/jbc.M115.652693. Epub 2015 Apr 17.

10.

The green tea polyphenol (-)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios.

Wobst HJ, Sharma A, Diamond MI, Wanker EE, Bieschke J.

FEBS Lett. 2015 Jan 2;589(1):77-83. doi: 10.1016/j.febslet.2014.11.026. Epub 2014 Nov 29.

11.

Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes.

Murray AN, Palhano FL, Bieschke J, Kelly JW.

Protein Sci. 2013 Nov;22(11):1531-41. doi: 10.1002/pro.2339. Epub 2013 Sep 30. Erratum in: Protein Sci. 2013 Nov;22(11):1689.

12.

Counting unstained, confluent cells by modified bright-field microscopy.

Drey LL, Graber MC, Bieschke J.

Biotechniques. 2013 Jul;55(1):28-33. doi: 10.2144/000114056.

13.

Natural compounds may open new routes to treatment of amyloid diseases.

Bieschke J.

Neurotherapeutics. 2013 Jul;10(3):429-39. doi: 10.1007/s13311-013-0192-7. Review.

14.

Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers.

Lopez del Amo JM, Fink U, Dasari M, Grelle G, Wanker EE, Bieschke J, Reif B.

J Mol Biol. 2012 Aug 24;421(4-5):517-24. doi: 10.1016/j.jmb.2012.01.013. Epub 2012 Jan 28.

PMID:
22300765
15.

Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils.

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, Frank RF, Reif B, Günther S, Walsh DM, Wanker EE.

Nat Chem Biol. 2011 Nov 20;8(1):93-101. doi: 10.1038/nchembio.719.

PMID:
22101602
16.

Black tea theaflavins inhibit formation of toxic amyloid-β and α-synuclein fibrils.

Grelle G, Otto A, Lorenz M, Frank RF, Wanker EE, Bieschke J.

Biochemistry. 2011 Dec 13;50(49):10624-36. doi: 10.1021/bi2012383. Epub 2011 Nov 16.

PMID:
22054421
17.

670 nm laser light and EGCG complementarily reduce amyloid-β aggregates in human neuroblastoma cells: basis for treatment of Alzheimer's disease?

Sommer AP, Bieschke J, Friedrich RP, Zhu D, Wanker EE, Fecht HJ, Mereles D, Hunstein W.

Photomed Laser Surg. 2012 Jan;30(1):54-60. doi: 10.1089/pho.2011.3073. Epub 2011 Oct 26.

PMID:
22029866
18.

Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states.

Dasari M, Espargaro A, Sabate R, Lopez del Amo JM, Fink U, Grelle G, Bieschke J, Ventura S, Reif B.

Chembiochem. 2011 Feb 11;12(3):407-23. doi: 10.1002/cbic.201000602. Epub 2011 Jan 10.

PMID:
21290543
19.

EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.

Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, Wanker EE.

Proc Natl Acad Sci U S A. 2010 Apr 27;107(17):7710-5. doi: 10.1073/pnas.0910723107. Epub 2010 Apr 12.

20.

A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis.

Bieschke J, Cohen E, Murray A, Dillin A, Kelly JW.

Protein Sci. 2009 Nov;18(11):2231-41. doi: 10.1002/pro.234. Erratum in: Protein Sci. 2013 Nov;22(11):1688.

21.

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers.

Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, Engemann S, Pastore A, Wanker EE.

Nat Struct Mol Biol. 2008 Jun;15(6):558-66. doi: 10.1038/nsmb.1437. Epub 2008 May 30.

PMID:
18511942
23.

The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation.

Siegel SJ, Bieschke J, Powers ET, Kelly JW.

Biochemistry. 2007 Feb 13;46(6):1503-10.

24.
25.

Small molecule oxidation products trigger disease-associated protein misfolding.

Bieschke J, Zhang Q, Bosco DA, Lerner RA, Powers ET, Wentworth P Jr, Kelly JW.

Acc Chem Res. 2006 Sep;39(9):611-9. Review.

PMID:
16981677
26.

Opposing activities protect against age-onset proteotoxicity.

Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A.

Science. 2006 Sep 15;313(5793):1604-10. Epub 2006 Aug 10.

27.

Structure-function-folding relationship in a WW domain.

Jäger M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW.

Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10648-53. Epub 2006 Jun 28.

29.

Single particle detection and characterization of synuclein co-aggregation.

Giese A, Bader B, Bieschke J, Schaffar G, Odoy S, Kahle PJ, Haass C, Kretzschmar H.

Biochem Biophys Res Commun. 2005 Aug 12;333(4):1202-10.

PMID:
15978545
30.

Automated PrPres amplification using indirect sonication.

Sarafoff NI, Bieschke J, Giese A, Weber P, Bertsch U, Kretzschmar HA.

J Biochem Biophys Methods. 2005 Jun 30;63(3):213-21.

PMID:
15967508
31.

Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets.

Bertsch U, Winklhofer KF, Hirschberger T, Bieschke J, Weber P, Hartl FU, Tavan P, Tatzelt J, Kretzschmar HA, Giese A.

J Virol. 2005 Jun;79(12):7785-91.

32.

Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a two-step mechanism, eliminating the requirement for nucleation.

Bieschke J, Zhang Q, Powers ET, Lerner RA, Kelly JW.

Biochemistry. 2005 Apr 5;44(13):4977-83.

PMID:
15794636
33.

Autocatalytic self-propagation of misfolded prion protein.

Bieschke J, Weber P, Sarafoff N, Beekes M, Giese A, Kretzschmar H.

Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12207-11. Epub 2004 Aug 5.

34.

Metabolite-initiated protein misfolding may trigger Alzheimer's disease.

Zhang Q, Powers ET, Nieva J, Huff ME, Dendle MA, Bieschke J, Glabe CG, Eschenmoser A, Wentworth P Jr, Lerner RA, Kelly JW.

Proc Natl Acad Sci U S A. 2004 Apr 6;101(14):4752-7. Epub 2004 Mar 19.

35.

Putting prions into focus: application of single molecule detection to the diagnosis of prion diseases.

Giese A, Bieschke J, Eigen M, Kretzschmar HA.

Arch Virol Suppl. 2000;(16):161-71.

PMID:
11214919
36.

Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets.

Bieschke J, Giese A, Schulz-Schaeffer W, Zerr I, Poser S, Eigen M, Kretzschmar H.

Proc Natl Acad Sci U S A. 2000 May 9;97(10):5468-73.

37.

Differential constitutive and activation-dependent expression of prion protein in human peripheral blood leucocytes.

Dürig J, Giese A, Schulz-Schaeffer W, Rosenthal C, Schmücker U, Bieschke J, Dührsen U, Kretzschmar HA.

Br J Haematol. 2000 Mar;108(3):488-95.

PMID:
10759704
38.

Rapid assay processing by integration of dual-color fluorescence cross-correlation spectroscopy: high throughput screening for enzyme activity.

Koltermann A, Kettling U, Bieschke J, Winkler T, Eigen M.

Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1421-6.

39.

Kinetic investigations by fluorescence correlation spectroscopy: the analytical and diagnostic potential of diffusion studies.

Schwille P, Bieschke J, Oehlenschläger F.

Biophys Chem. 1997 Jun 30;66(2-3):211-28. Review.

PMID:
9362560

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