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Das Gründungsteam hat umfangreich zum Thema Proteinaggregation und Proteinverhalten publiziert (1 - 14). Diese Arbeiten schließen sechs verschiedene Proteine ein, die faserartige Eiweißagglomerationen bilden können. Dazu gehören u. a. auch das Aβ-Peptid (Alzheimer-Demenz), das α-Synuclein (Parkinson-Krankheit) und das Prion-Protein (Creutzfeldt-Jakob-Demenz). Hinzu kommen weitere Arbeiten und Co-Autorenschaften, die in den erweiterten Themenkomplex des Verhaltens und der Struktur von Proteinen gehören (15 - 23).

  1. Schubeis T, Luhrs T, & Ritter C (2015) Unambiguous assignment of short- and long-range structural restraints by solid-state NMR spectroscopy with segmental isotope labeling. Chembiochem : a European journal of chemical biology 16(1):51-54. http://www.ncbi.nlm.nih.gov/pubmed/25394265
  2. He L, Luhrs T, & Ritter C (2014) Solid-state NMR resonance assignments of the filament-forming CARD domain of the innate immunity signaling protein MAVS. Biomolecular NMR assignments. http://www.ncbi.nlm.nih.gov/pubmed/25301530
  3. Vilar M, Chou HT, Luhrs T, Maji SK, Riek-Loher D, Verel R, Manning G, Stahlberg H, & Riek R (2008) The fold of alpha-synuclein fibrils. Proceedings of the National Academy of Sciences of the United States of America 105(25):8637-8642. http://www.ncbi.nlm.nih.gov/pubmed/18550842
  4. Luhrs T, Zahn R, & Wuthrich K (2006) Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions. Journal of molecular biology 357(3):833-841. http://www.ncbi.nlm.nih.gov/pubmed/16466741
  5. Ritter C, Maddelein ML, Siemer AB, Luhrs T, Ernst M, Meier BH, Saupe SJ, & Riek R (2005) Correlation of structural elements and infectivity of the HET-s prion. Nature 435(7043):844-848. http://www.ncbi.nlm.nih.gov/pubmed/15944710
  6. Luhrs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, Dobeli H, Schubert D, & Riek R (2005) 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proceedings of the National Academy of Sciences of the United States of America 102(48):17342-17347. http://www.ncbi.nlm.nih.gov/pubmed/16293696
  7. Luhrs T, Riek R, Guntert P, & Wuthrich K (2003) NMR structure of the human doppel protein. Journal of molecular biology 326(5):1549-1557. http://www.ncbi.nlm.nih.gov/pubmed/12595265
  8. Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, & Wuthrich K (2000) NMR solution structure of the human prion protein. Proceedings of the National Academy of Sciences of the United States of America 97(1):145-150. http://www.ncbi.nlm.nih.gov/pubmed/10618385
  9. Wasmer C, Zimmer A, Sabate R, Soragni A, Saupe SJ, Ritter C, & Meier BH (2010) Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity. Journal of molecular biology 402(2):311-325. http://www.ncbi.nlm.nih.gov/pubmed/20600104
  10. Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, & Riek R (2010) The mechanism of prion inhibition by HET-S. Molecular cell 38(6):889-899. http://www.ncbi.nlm.nih.gov/pubmed/20620958
  11. Siemer AB, Ritter C, Steinmetz MO, Ernst M, Riek R, & Meier BH (2006) 13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form. Journal of biomolecular NMR 34(2):75-87. http://www.ncbi.nlm.nih.gov/pubmed/16518695
  12. Siemer AB, Arnold AA, Ritter C, Westfeld T, Ernst M, Riek R, & Meier BH (2006) Observation of highly flexible residues in amyloid fibrils of the HET-s prion. Journal of the American Chemical Society 128(40):13224-13228. http://www.ncbi.nlm.nih.gov/pubmed/17017802
  13. Liu Y, Ritter C, Riek R, & Schubert D (2006) The formation of bioactive amyloid species by prion proteins in vitro and in cells. Neuroscience letters 406(3):200-204. http://www.ncbi.nlm.nih.gov/pubmed/16916580
  14. Siemer AB, Ritter C, Ernst M, Riek R, & Meier BH (2005) High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angewandte Chemie 44(16):2441-2444. http://www.ncbi.nlm.nih.gov/pubmed/15770629
  15. Hellert J, Krausze J, Schulz TF, & Luhrs T (2014) Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA. Acta crystallographica. Section F, Structural biology communications 70(Pt 11):1570-1574. http://www.ncbi.nlm.nih.gov/pubmed/25372834
  16. Hellert J, Weidner-Glunde M, Krausze J, Richter U, Adler H, Fedorov R, Pietrek M, Ruckert J, Ritter C, Schulz TF, & Luhrs T (2013) A structural basis for BRD2/4-mediated host chromatin interaction and oligomer assembly of Kaposi sarcoma-associated herpesvirus and murine gammaherpesvirus LANA proteins. PLoS pathogens 9(10):e1003640. http://www.ncbi.nlm.nih.gov/pubmed/24146614
  17. Wiesand U, Sorg I, Amstutz M, Wagner S, van den Heuvel J, Luhrs T, Cornelis GR, & Heinz DW (2009) Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica. Journal of molecular biology 385(3):854-866. http://www.ncbi.nlm.nih.gov/pubmed/18976663
  18. Nitschke C, Flechsig E, van den Brandt J, Lindner N, Luhrs T, Dittmer U, & Klein MA (2007) Immunisation strategies against prion diseases: prime-boost immunisation with a PrP DNA vaccine containing foreign helper T-cell epitopes does not prevent mouse scrapie. Veterinary microbiology 123(4):367-376. http://www.ncbi.nlm.nih.gov/pubmed/17499458
  19. Nishina KA, Deleault NR, Mahal SP, Baskakov I, Luhrs T, Riek R, & Supattapone S (2006) The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry 45(47):14129-14139. http://www.ncbi.nlm.nih.gov/pubmed/17115708
  20. Glatzel M, Stoeck K, Seeger H, Luhrs T, & Aguzzi A (2005) Human prion diseases: molecular and clinical aspects. Archives of neurology 62(4):545-552. http://www.ncbi.nlm.nih.gov/pubmed/15824251
  21. Glatzel M, Pekarik V, Luhrs T, Dittami J, & Aguzzi A (2002) Analysis of the prion protein in primates reveals a new polymorphism in codon 226 (Y226F). Biological chemistry 383(6):1021-1025. http://www.ncbi.nlm.nih.gov/pubmed/12222676
  22. Ritter C & Helenius A (2000) Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase. Nature structural biology 7(4):278-280. http://www.ncbi.nlm.nih.gov/pubmed/10742170
  23. Ritter C, Quirin K, Kowarik M, & Helenius A (2005) Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT. The EMBO journal 24(9):1730-1738. http://www.ncbi.nlm.nih.gov/pubmed/15861139

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