Meier BH - Search Results

1

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy.

Guerrero-Ferreira R, Taylor NM, Arteni AA, Kumari P, Mona D, Ringler P, Britschgi M, Lauer ME, Makky A, Verasdonck J, Riek R, Melki R, Meier BH, Böckmann A, Bousset L, Stahlberg H. Guerrero-Ferreira R, et al. Among authors: meier bh. Elife. 2019 Dec 9;8:e48907. doi: 10.7554/eLife.48907. Elife. 2019. PMID: 31815671 Free PMC article.

2

NMR spectra of a microcrystalline protein at 30 kHz MAS.

Ernst M, Detken A, Böckmann A, Meier BH. Ernst M, et al. Among authors: meier bh. J Am Chem Soc. 2003 Dec 24;125(51):15807-10. doi: 10.1021/ja0369966. J Am Chem Soc. 2003. PMID: 14677971

3

High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.

Siemer AB, Ritter C, Ernst M, Riek R, Meier BH. Siemer AB, et al. Among authors: meier bh. Angew Chem Int Ed Engl. 2005 Apr 15;44(16):2441-4. doi: 10.1002/anie.200462952. Angew Chem Int Ed Engl. 2005. PMID: 15770629 No abstract available.

4

Correlation of structural elements and infectivity of the HET-s prion.

Ritter C, Maddelein ML, Siemer AB, Lührs T, Ernst M, Meier BH, Saupe SJ, Riek R. Ritter C, et al. Among authors: meier bh. Nature. 2005 Jun 9;435(7043):844-8. doi: 10.1038/nature03793. Nature. 2005. PMID: 15944710 Free PMC article.

5

13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form.

Siemer AB, Ritter C, Steinmetz MO, Ernst M, Riek R, Meier BH. Siemer AB, et al. Among authors: meier bh. J Biomol NMR. 2006 Feb;34(2):75-87. doi: 10.1007/s10858-005-5582-7. J Biomol NMR. 2006. PMID: 16518695

6

Observation of highly flexible residues in amyloid fibrils of the HET-s prion.

Siemer AB, Arnold AA, Ritter C, Westfeld T, Ernst M, Riek R, Meier BH. Siemer AB, et al. Among authors: meier bh. J Am Chem Soc. 2006 Oct 11;128(40):13224-8. doi: 10.1021/ja063639x. J Am Chem Soc. 2006. PMID: 17017802

7

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.

Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. Wasmer C, et al. Among authors: meier bh. Science. 2008 Mar 14;319(5869):1523-6. doi: 10.1126/science.1151839. Science. 2008. PMID: 18339938

8

Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra.

Wasmer C, Soragni A, Sabaté R, Lange A, Riek R, Meier BH. Wasmer C, et al. Among authors: meier bh. Angew Chem Int Ed Engl. 2008;47(31):5839-41. doi: 10.1002/anie.200704896. Angew Chem Int Ed Engl. 2008. PMID: 18548467 No abstract available.

9

Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.

Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, Wang L, Riek R, Saupe SJ, Meier BH. Wasmer C, et al. Among authors: meier bh. Angew Chem Int Ed Engl. 2009;48(26):4858-60. doi: 10.1002/anie.200806100. Angew Chem Int Ed Engl. 2009. PMID: 19472238

10

The molecular organization of the fungal prion HET-s in its amyloid form.

Wasmer C, Schütz A, Loquet A, Buhtz C, Greenwald J, Riek R, Böckmann A, Meier BH. Wasmer C, et al. Among authors: meier bh. J Mol Biol. 2009 Nov 20;394(1):119-27. doi: 10.1016/j.jmb.2009.09.015. Epub 2009 Sep 11. J Mol Biol. 2009. PMID: 19748509

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