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Journal Abstract Search

101 related items for PubMed ID: 24751876

  • 21. Segmental Isotope Labeling of Insoluble Proteins for Solid-State NMR by Protein Trans-Splicing.
    Schubeis T, Nagaraj M, Ritter C.
    Methods Mol Biol; 2017; 1495():147-160. PubMed ID: 27714615
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  • 28. Isotopic labeling of recombinant proteins from the methylotrophic yeast Pichia pastoris.
    Pickford AR, O'Leary JM.
    Methods Mol Biol; 2004; 278():17-33. PubMed ID: 15317988
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  • 29. Structural polymorphism of human islet amyloid polypeptide (hIAPP) oligomers highlights the importance of interfacial residue interactions.
    Zhao J, Yu X, Liang G, Zheng J.
    Biomacromolecules; 2011 Jan 10; 12(1):210-20. PubMed ID: 21158384
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  • 30. A new structural model of Aβ40 fibrils.
    Bertini I, Gonnelli L, Luchinat C, Mao J, Nesi A.
    J Am Chem Soc; 2011 Oct 12; 133(40):16013-22. PubMed ID: 21882806
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  • 31. Recoupling of native homonuclear dipolar couplings in magic-angle-spinning solid-state NMR by the double-oscillating field technique.
    Straasø LA, Nielsen NC.
    J Chem Phys; 2010 Aug 14; 133(6):064501. PubMed ID: 20707569
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  • 32. High yield expression and purification of isotopically labelled human endothelin-1 for use in NMR studies.
    Mac TT, Beyermann M, Pires JR, Schmieder P, Oschkinat H.
    Protein Expr Purif; 2006 Aug 14; 48(2):253-60. PubMed ID: 16584890
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  • 33. Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
    Ippel JH, Olofsson A, Schleucher J, Lundgren E, Wijmenga SS.
    Proc Natl Acad Sci U S A; 2002 Jun 25; 99(13):8648-53. PubMed ID: 12072564
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  • 34. Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
    Meier BH, Riek R, Böckmann A.
    Trends Biochem Sci; 2017 Oct 25; 42(10):777-787. PubMed ID: 28916413
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  • 35. Absolute structural constraints on amyloid fibrils from solid-state NMR spectroscopy of partially oriented samples.
    Oyler NA, Tycko R.
    J Am Chem Soc; 2004 Apr 14; 126(14):4478-9. PubMed ID: 15070340
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  • 36. Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation.
    van Ham TJ, Esposito A, Kumita JR, Hsu ST, Kaminski Schierle GS, Kaminski CF, Dobson CM, Nollen EA, Bertoncini CW.
    J Mol Biol; 2010 Jan 22; 395(3):627-42. PubMed ID: 19891973
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  • 37. Optimal control based NCO and NCA experiments for spectral assignment in biological solid-state NMR spectroscopy.
    Kehlet C, Bjerring M, Sivertsen AC, Kristensen T, Enghild JJ, Glaser SJ, Khaneja N, Nielsen NC.
    J Magn Reson; 2007 Oct 22; 188(2):216-30. PubMed ID: 17681479
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  • 38. Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides.
    Rijkers DT, Höppener JW, Posthuma G, Lips CJ, Liskamp RM.
    Chemistry; 2002 Sep 16; 8(18):4285-91. PubMed ID: 12298020
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  • 39. Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form.
    Blanco FJ, Hess S, Pannell LK, Rizzo NW, Tycko R.
    J Mol Biol; 2001 Nov 02; 313(4):845-59. PubMed ID: 11697908
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  • 40. Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state.
    Yonemoto IT, Kroon GJ, Dyson HJ, Balch WE, Kelly JW.
    Biochemistry; 2008 Sep 16; 47(37):9900-10. PubMed ID: 18710262
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