Al-Hilaly YK, Hurt V, Rickard JE, Harrington CR, Storey JMD, Wischik CM, Serpell LC, and Siemer AB (2022)Solid-state NMR of paired helical filaments formed by the core tau fragment tau(297-391) Front. Neurosci. 16:988074 [DOI]
Siemer AB (2022)What makes functional amyloids work? Crit. Rev. Biochem. Mol. Biol. 57(4) 399–411 [DOI]
Soria MA, Cervantes SA, and Siemer AB (2022)Calmodulin binds the N-terminus of the functional amyloid Orb2A inhibiting fibril formation Plos one 17, e0259872 [DOI]
Isas JM, Pandey NK, Xu H, Teranishi K, Okada AK, Fultz EK, Rawat A, Applebaum A, Meier F, Chen J, Langen R, and Siemer AB (2021)Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted Nat. Commun. 12, 4272 [DOI]
Ashami K, Falk AS, Hurd C, Garg G, Cervantes SA, Rawat A, Siemer AB (2021)Droplet and fibril formation of the functional amyloid Orb2. J. Biol. Chem. 297(1), 100804 [DOI]
Falk AS, Bravo-Arredondo JM, Varkey J, Pacheco S, Langen R, Siemer AS (2020)Structural Model of the Proline-Rich Domain of Huntingtin Exon-1 Fibrils. Biophys. J. 119(10), 2019–2028 [DOI]
Siemer AB (2020)Advances in studying protein disorder with solid-state NMR. Solid State Nucl. Magn. Reson. 106,101643 [DOI]
Caulkins BG, Cervantes SA, Isas JM, Siemer AB (2018)Dynamics of the Proline-Rich C-Terminus of Huntingtin Exon-1 Fibrils. J. Phys. Chem. B. 122(41),9507–9515 [DOI]
Mompeán M, Li W, Li J, Laage S, Siemer AB, Bozkurt G, Wu H, McDermott AE.(2018)The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell 173(5) 1244–1253 [DOI]
Bajakian TH, Cervantes SA, Soria MA, Beaugrand M, Kim JY, Service RJ, Siemer AB (2017)Metal Binding Properties of the N‐Terminus of the Functional Amyloid Orb2. Biomolecules 7(3),57 [DOI]
Soria MA, Cervantes SA, Bajakian TH, Siemer AB (2017)The Functional Amyloid Orb2A Binds to Lipid Membranes Biophys. J. 113(1),37–47 [DOI]
Isas JM, Langen A, Isas MC, Pandey NK, Siemer AB (2017)Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils. Biochemistry 56(28), 3579–3586 [DOI]
Cervantes SA, Bajakian TH, Soria MA, Falk AS, Service RJ, Langen R, Siemer AB (2016)Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A. Sci. Rep. 6(25), 38265 [DOI]
Falk AS,Siemer AB (2016)Dynamic Domains of Amyloid Fibrils can be Site-specifically Assigned with Proton Detected 3D NMR Spectroscopy. J. Biomol. NMR 66(3), 159–162 [DOI]
Isas JM, Langen R, Siemer AB (2015)Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils. Biochemistry 54(25), 3942–3949 [DOI]
Siemer AB (2014)Antifreeze Proteins by Solid-state NMR: Methods and Applications. eMagRes, 3, 153–160 [DOI]
Siemer AB (2013)Magic Angle Spinning Solid-State NMR on Proteins. Encyclopedia of Biophysics [URL]
Raveendra BL, Siemer AB, Puthanveettil SV, Hendrickson WA,
Kandel ER, McDermott AE (2013)Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEB. Nat. Struct. Mol. Biol. 20(4), 495–501 [DOI]
Siemer AB, Huang KY, McDermott AE (2012)Protein linewidth and solvent dynamics in frozen solution NMR. PLoS One 7(10): e47242. [DOI]
Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H (2012)The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis. Cell 150(2), 339–350 [DOI]
Huang KY, Siemer AB, McDermott AE (2011)Homonuclear mixing sequences for perdeuterated proteins. J. Magn. Reson. 208(1), 122–127 [DOI]
Siemer AB, Huang KY, McDermott AE (2010)Protein–ice interaction of an antifreeze protein observed with solid-state NMR. Proc. Natl. Ac. Sci. 107(41), 17580–17585 [DOI]
Eichelbaum M, Siemer AB, Farrauto RJ, Castaldi MJ (2010)The impact of urea on the performance of metal
exchanged zeolites for the selective catalytic reduction of NOx - part II. catalytic, FTIR, and NMR studies. Appl. Catal. B 97(1–2), 98–107[DOI]
Siemer AB, McDermott AE (2008)Solid-state NMR on a type III antifreeze protein in the presence of ice. J. Am. Chem. Soc. 130(51), 17394–17399 [DOI]
Wasmer C, Lange A, Van Melckebeke H, Siemer AB , Riek R, Meier BH (2008) Amyloid fibrils of the HET-s(218–289) prion form a beta-solenoid with a triangular hydrophobic core. Science 319(5869), 1523–1526. [DOI]
Verel R, Manolikas T, Siemer AB, Meier BH (2007)Improved resolution in 13C solid-state spectra through spin-state-selection techniques.
J. Magn. Reson. 184(2), 322–329. [DOI]
Siemer AB, Arnold A, Westfeld T, Ritter C, Ernst M, Riek R, Meier BH (2006) Structural and dynamical heterogeneity of the HET-s prion protein observed by liquid- and solid-state NMR. J. Am. Chem. Soc. 128(40), 13224–13228. [DOI]
Siemer AB, Ritter C, Steinmetz M, Ernst M, Riek R, Meier BH (2006) 13C, 15N
Resonance assignment of parts of the HET-s prion protein in its amyloid
form. J. Biomol. NMR. 34, 75–87. [DOI]
Ritter C, Maddelein ML, Siemer AB, Lührs 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. [DOI]
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. Angew. Chem. Int. Ed. Engl. 44(16), 2441–2444. [DOI]
Siemer A, Masip M, Carreras N,
García-Ortega L, Onaderra M, Bruix M, Del Pozo AM, Gavilanes JG (2004)Conserved asparagine residue 54 of alpha-sarcin plays a role in protein stability and enzyme activity.
Biol. Chem. 385(12), 1165–1170. [DOI]
Gast K, Siemer A, Zirwer D, Damaschun G (2001)Fluoroalcohol-induced structural
changes of proteins: some aspects of cosolvent-protein interactions. Eur. Biophys. J. 30(4), 273–283. [DOI]
