Publications

34 publications, newest first.

2026

  1. Fang A,Tang X, Fleming M, Tancowny B, Wang X, Wang YL, Daude N, Dorosh L, Fleck SC, Rathod V, Coustou V, Cervantes SA, Velásquez CD, Westaway D, Aiken J, McKenzie D,Telling G, Stepanova M, Saupe SJ, Siemer AB, Wille H model-based prion vaccine protects a transgenic mouse line carrying a Gerstmann–Sträussler–Scheinker disease mutation Acta Neuropathologica doi:10.1007/s00401-026-03015-4

2025

  1. Pacheco S, Reselammal DS, Li S, Zhang Q, Velloor G, Chen J, and Siemer AB Phosphorylation of α-Synuclein Fibrils at S129 Changes DNAJB1 Binding as Probed by Solid-State NMR JACS Au doi:10.1021/jacsau.5c01266

2022

  1. Al-Hilaly YK, Hurt V, Rickard JE, Harrington CR, Storey JMD, Wischik CM, Serpell LC, and Siemer AB Solid-state NMR of paired helical filaments formed by the core tau fragment tau(297-391) Front. Neurosci. 16:988074 doi:10.3389/fnins.2022.988074
  2. Siemer AB What makes functional amyloids work? Crit. Rev. Biochem. Mol. Biol. 57(4) 399–411 doi:10.1080/10409238.2022.2113030
  3. Soria MA, Cervantes SA, and Siemer AB Calmodulin binds the N-terminus of the functional amyloid Orb2A inhibiting fibril formation Plos one 17, e0259872 doi:10.1371/journal.pone.0259872

2021

  1. 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 Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted Nat. Commun. 12, 4272 doi:10.1038/s41467-021-24411-2
  2. Ashami K, Falk AS, Hurd C, Garg G, Cervantes SA, Rawat A, Siemer AB Droplet and fibril formation of the functional amyloid Orb2 J. Biol. Chem. 297(1), 100804 doi:10.1016/j.jbc.2021.100804

2020

  1. Falk AS, Bravo-Arredondo JM, Varkey J, Pacheco S, Langen R, Siemer AB Structural Model of the Proline-Rich Domain of Huntingtin Exon-1 Fibrils Biophys. J. 119(10), 2019–2028 doi:10.1016/j.bpj.2020.10.010
  2. Siemer AB Advances in studying protein disorder with solid-state NMR Solid State Nucl. Magn. Reson. 106,101643 doi:10.1016/j.ssnmr.2020.101643

2018

  1. Caulkins BG, Cervantes SA, Isas JM, Siemer AB Dynamics of the Proline-Rich C-Terminus of Huntingtin Exon-1 Fibrils J. Phys. Chem. B. 122(41),9507–9515 doi:10.1021/acs.jpcb.8b09213
  2. Mompeán M, Li W, Li J, Laage S, Siemer AB, Bozkurt G, Wu H, McDermott AE The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex Cell 173(5) 1244–1253 doi:10.1016/j.cell.2018.03.032

2017

  1. Bajakian TH, Cervantes SA, Soria MA, Beaugrand M, Kim JY, Service RJ, Siemer AB Metal Binding Properties of the N‐Terminus of the Functional Amyloid Orb2 Biomolecules 7(3),57 doi:10.3390/biom7030057
  2. Soria MA, Cervantes SA, Bajakian TH, Siemer AB The Functional Amyloid Orb2A Binds to Lipid Membranes Biophys. J. 113(1),37–47 doi:10.1016/j.bpj.2017.05.039
  3. Isas JM, Langen A, Isas MC, Pandey NK, Siemer AB Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils Biochemistry 56(28), 3579–3586 doi:10.1021/acs.biochem.7b00138

2016

  1. Cervantes SA, Bajakian TH, Soria MA, Falk AS, Service RJ, Langen R, Siemer AB Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A Sci. Rep. 6(25), 38265 doi:10.1038/srep38265
  2. Falk AS,Siemer AB Dynamic Domains of Amyloid Fibrils can be Site-specifically Assigned with Proton Detected 3D NMR Spectroscopy J. Biomol. NMR 66(3), 159–162 doi:10.1007/s10858-016-0069-2

2015

  1. Isas JM, Langen R, Siemer AB Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils Biochemistry 54(25), 3942–3949 doi:10.1021/acs.biochem.5b00281

2014

  1. Siemer AB Antifreeze Proteins by Solid-state NMR: Methods and Applications eMagRes, 3, 153–160 doi:10.1002/9780470034590.emrstm1355

2013

  1. Siemer AB Magic Angle Spinning Solid-State NMR on Proteins Encyclopedia of Biophysics Link
  2. Raveendra BL, Siemer AB, Puthanveettil SV, Hendrickson WA, Kandel ER, McDermott AE Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEB Nat. Struct. Mol. Biol. 20(4), 495–501 doi:10.1038/nsmb.2503

2012

  1. Siemer AB, Huang KY, McDermott AE Protein linewidth and solvent dynamics in frozen solution NMR PLoS One 7(10): e47242 doi:10.1371/journal.pone.0047242
  2. Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis Cell 150(2), 339–350 doi:10.1016/j.cell.2012.06.019

2011

  1. Huang KY, Siemer AB, McDermott AE Homonuclear mixing sequences for perdeuterated proteins J. Magn. Reson. 208(1), 122–127 doi:10.1016/j.jmr.2010.10.015

2010

  1. Siemer AB, Huang KY, McDermott AE Protein–ice interaction of an antifreeze protein observed with solid-state NMR Proc. Natl. Ac. Sci. 107(41), 17580–17585 doi:10.1073/pnas.1009369107
  2. Eichelbaum M, Siemer AB, Farrauto RJ, Castaldi MJ 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:10.1016/j.apcatb.2010.03.028

2008

  1. Siemer AB, McDermott AE Solid-state NMR on a type III antifreeze protein in the presence of ice J. Am. Chem. Soc. 130(51), 17394–17399 doi:10.1021/ja8047893
  2. Wasmer C, Lange A, Van Melckebeke H, Siemer AB , Riek R, Meier BH Amyloid fibrils of the HET-s(218–289) prion form a beta-solenoid with a triangular hydrophobic core Science 319(5869), 1523–1526 doi:10.1126/science.1151839

2007

  1. Verel R, Manolikas T, Siemer AB, Meier BH Improved resolution in 13C solid-state spectra through spin-state-selection techniques J. Magn. Reson. 184(2), 322–329 doi:10.1016/j.jmr.2006.09.024

2006

  1. Siemer AB, Arnold A, Westfeld T, Ritter C, Ernst M, Riek R, Meier BH 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:10.1021/ja063639x
  2. Siemer AB, Ritter C, Steinmetz M, Ernst M, Riek R, Meier BH 13C, 15N Resonance assignment of parts of the HET-s prion protein in its amyloid form J. Biomol. NMR. 34, 75–87 doi:10.1007/s10858-005-5582-7

2005

  1. Ritter C, Maddelein ML, Siemer AB, Lührs T, Ernst M, Meier BH, Saupe SJ, Riek R Correlation of structural elements and infectivity of the HET-s prion Nature. 435(7043), 844–848 doi:10.1038/nature03793
  2. Siemer AB, Ritter C, Ernst M, Riek R, Meier BH 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:10.1002/anie.200462952

2004

  1. Siemer A, Masip M, Carreras N, García-Ortega L, Onaderra M, Bruix M, Del Pozo AM, Gavilanes JG Conserved asparagine residue 54 of alpha-sarcin plays a role in protein stability and enzyme activity Biol. Chem. 385(12), 1165–1170 doi:10.1515/BC.2004.150

2001

  1. Gast K, Siemer A, Zirwer D, Damaschun G Fluoroalcohol-induced structural changes of proteins: some aspects of cosolvent-protein interactions Eur. Biophys. J. 30(4), 273–283 doi:10.1007/s002490100148