Cited by 1,044

The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.

Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils

Open access

Petkova, Aneta T., Yau, Wai-Ming, Tycko, Robert·2006·Biochemistry

DOI 10.1021/bi051952q

Open this paper in CoChat — free account

Abstract

We describe solid-state nuclear magnetic resonance (NMR) measurements on fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)) that place constraints on the identity and symmetry of contacts between in-register, parallel beta-sheets in the fibrils. We refer to these contacts as internal and external quaternary contacts, depending on whether they are within a single molecular layer or between molecular layers. The data include (1) two-dimensional 13C-13C NMR spectra that indicate internal quaternary contacts between side chains of L17 and F19 and side chains of I32, L34, and V36, as well as external quaternary contacts between side chains of I31 and G37; (2) two-dimensional 15N-13C NMR spectra that indicate external quaternary contacts between the side chain of M35 and the peptide backbone at G33; (3) measurements of magnetic dipole-dipole couplings between the side chain carboxylate group of D23 and the side chain amine group of K28 that indicate salt bridge interactions. Isotopic dilution experiments allow us to make distinctions between intramolecular and intermolecular contacts. On the basis of these data and previously determined structural constraints from solid-state NMR and electron microscopy, we construct full molecular models using restrained molecular dynamics simulations and restrained energy minimization. These models apply to Abeta(1-40) fibrils grown with gentle agitation. We also present evidence for different internal quaternary contacts in Abeta(1-40) fibrils grown without agitation, which are morphologically distinct.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1021/bi051952q

Cites

84 of 84 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,163
1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211777 · Cited by 2,359
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
Heteronuclear decoupling in rotating solids
Bennett, A. E., Rienstra, C. M., Auger, M., Lakshmi, K. V., & Griffin, R. G. (1995) · The Journal of Chemical Physics · doi:10.1063/1.470372 · Cited by 2,124
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., & Tycko, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262663499 · Cited by 1,845
Self-citation
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
Self-citation
P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., & Dobson, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3590 · Cited by 1,039
– dipolar-assisted rotational resonance in magic-angle spinning NMR
Takegoshi, K., Nakamura, S., & Terao, T. (2001) · Chemical Physics Letters · doi:10.1016/s0009-2614(01)00791-6 · Cited by 1,012
The protofilament structure of insulin amyloid fibrils
Jiménez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., & Saibil, H. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142459399 · Cited by 834
X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
EANES, E. D., & GLENNER, G. G. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.11.673 · Cited by 823
Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.
Roher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799
Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR
Balbach, J. J., Ishii, Y., Antzutkin, O. N., Leapman, R. D., Rizzo, N. W., Dyda, F., Reed, J., & Tycko, R. (2000) · Biochemistry · doi:10.1021/bi0011330 · Cited by 703
Self-citation
Molecular basis for amyloid fibril formation and stability
Makin, O. S., Atkins, E., Sikorski, P., Johansson, J., & Serpell, L. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406847102 · Cited by 657
The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into Amyloid
Lai, Z., Colón, W., & Kelly, J. W. (1996) · Biochemistry · doi:10.1021/bi952501g · Cited by 574
Metal Binding and Oxidation of Amyloid-β within Isolated Senile Plaque Cores: Raman Microscopic Evidence
Dong, J., Atwood, C. S., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G., & Carey, P. R. (2003) · Biochemistry · doi:10.1021/bi0272151 · Cited by 562
Rotational-echo double-resonance NMR
Gullion, T., & Schaefer, J. (2011) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2011.09.003 · Cited by 548
Evidence for assembly of prions with left-handed β-helices into trimers
Govaerts, C., Wille, H., Prusiner, S. B., & Cohen, F. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402254101 · Cited by 539
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
Jaroniec, C. P., MacPhee, C. E., Bajaj, V. S., McMahon, M. T., Dobson, C. M., & Griffin, R. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0304849101 · Cited by 515
Amyloid fibers are water-filled nanotubes
Perutz, M. F., Finch, J. T., Berriman, J., & Lesk, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042681399 · Cited by 506
Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
Jiménez, J. L., Guijarro, J. I., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M., & Saibil, H. R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.815 · Cited by 503
From the globular to the fibrous state: protein structure and structural conversion in amyloid formation
SUNDE, M., & BLAKE, C. C. F. (1998) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583598003400 · Cited by 457
The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
Coustou, V., Deleu, C., Saupe, S., & Begueret, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9773 · Cited by 456
Correlation of structural elements and infectivity of the HET-s prion
Ritter, C., Maddelein, M.-L., Siemer, A. B., Lührs, T., Ernst, M., Meier, B. H., Saupe, S. J., & Riek, R. (2005) · Nature · doi:10.1038/nature03793 · Cited by 437
Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ 16 – 22 , Aβ 16–35 , and Aβ 10 – 35 ): Sequence effects
Ma, B., & Nussinov, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212206899 · Cited by 403
Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
Lansbury, P. T., Costa, P. R., Griffiths, J. M., Simon, E. J., Auger, M., Halverson, K. J., Kocisko, D. A., Hendsch, Z. S., Ashburn, T. T., Spencer, R. G. S., et al. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb1195-990 · Cited by 396
Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register
Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13407 · Cited by 389
The X-ray interpretation of denaturation and the structure of the seed globulins
Astbury, W. T., Dickinson, S., & Bailey, K. (1935) · Biochemical Journal · doi:10.1042/bj0292351 · Cited by 386
Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils
Antzutkin, O. N., Balbach, J. J., Leapman, R. D., Rizzo, N. W., Reed, J., & Tycko, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.230315097 · Cited by 383
Self-citation
Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline Mutagenesis
Williams, A. D., Portelius, E., Kheterpal, I., Guo, J.-T., Cook, K. D., Xu, Y., & Wetzel, R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.008 · Cited by 378
Progress towards a molecular-level structural understanding of amyloid fibrils
Tycko, R. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.12.002 · Cited by 373
Self-citation
Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling
Török, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., & Langen, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205659200 · Cited by 373
A Molecular Model of Alzheimer Amyloid β-Peptide Fibril Formation
Tjernberg, L. O., Callaway, D. J. E., Tjernberg, A., Hahne, S., Lilliehöök, C., Terenius, L., Thyberg, J., & Nordstedt, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12619 · Cited by 360
Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling
Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305266200 · Cited by 329
Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange
Hoshino, M., Katou, H., Hagihara, Y., Hasegawa, K., Naiki, H., & Goto, Y. (2002) · Nature Structural Biology · doi:10.1038/nsb792 · Cited by 315
Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide
Petkova, A. T., Buntkowsky, G., Dyda, F., Leapman, R. D., Yau, W.-M., & Tycko, R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.044 · Cited by 314
Self-citation
Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance
Balbach, J. J., Petkova, A. T., Oyler, N. A., Antzutkin, O. N., Gordon, D. J., Meredith, S. C., & Tycko, R. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75244-2 · Cited by 314
Self-citation
3D TEDOR NMR Experiments for the Simultaneous Measurement of Multiple Carbon−Nitrogen Distances in Uniformly13C,15N-Labeled Solids
Jaroniec, C. P., Filip, C., & Griffin, R. G. (2002) · Journal of the American Chemical Society · doi:10.1021/ja026385y · Cited by 288
Template-assisted filament growth by parallel stacking of tau
Margittai, M., & Langen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401911101 · Cited by 274
Supramolecular Structural Constraints on Alzheimer's β-Amyloid Fibrils from Electron Microscopy and Solid-State Nuclear Magnetic Resonance
Antzutkin, O. N., Leapman, R. D., Balbach, J. J., & Tycko, R. (2002) · Biochemistry · doi:10.1021/bi0204185 · Cited by 263
Self-citation
Molecular Dynamics Simulations of Alzheimer's β-Amyloid Protofilaments
Buchete, N.-V., Tycko, R., & Hummer, G. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.066 · Cited by 256
Self-citation
Frequency Selective Heteronuclear Dipolar Recoupling in Rotating Solids: Accurate13C−15N Distance Measurements in Uniformly13C,15N-labeled Peptides
Jaroniec, C. P., Tounge, B. A., Herzfeld, J., & Griffin, R. G. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003266e · Cited by 255
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril
Jaroniec, C. P., MacPhee, C. E., Astrof, N. S., Dobson, C. M., & Griffin, R. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625999 · Cited by 253
Fibril formation by primate, rodent, and Dutch-hemorrhagic analogs of Alzheimer amyloid .beta.-protein
Fraser, P. E., Nguyen, J. T., Inouye, H., Surewicz, W. K., Selkoe, D. J., Podlisny, M. B., & Kirschner, D. A. (1992) · Biochemistry · doi:10.1021/bi00159a011 · Cited by 248
Aβ40-Lactam(D23/K28) Models a Conformation Highly Favorable for Nucleation of Amyloid
Sciarretta, K. L., Gordon, D. J., Petkova, A. T., Tycko, R., & Meredith, S. C. (2005) · Biochemistry · doi:10.1021/bi0474867 · Cited by 244
Self-citation
The architecture of parallel β-helices and related folds
Jenkins, J., & Pickersgill, R. (2001) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(01)00013-x · Cited by 235
Structure of the β-Amyloid(10-35) Fibril
Burkoth, T. S., Benzinger, T. L. S., Urban, V., Morgan, D. M., Gregory, D. M., Thiyagarajan, P., Botto, R. E., Meredith, S. C., & Lynn, D. G. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000645z · Cited by 224
Diluting Abundant Spins by Isotope Edited Radio Frequency Field Assisted Diffusion
Morcombe, C. R., Gaponenko, V., Byrd, R. A., & Zilm, K. W. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047919t · Cited by 223
NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque‐competence, Aβ(1–40)ox and Aβ(1–42)ox
Riek, R., Güntert, P., Döbeli, H., Wipf, B., & Wüthrich, K. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02537.x · Cited by 221
Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Aβ-(1–42) Peptide of Alzheimer's Disease
Hou, L., Kang, I., Marchant, R. E., & Zagorski, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200338200 · Cited by 218
Insights into the Amyloid Folding Problem from Solid-State NMR
Tycko, R. (2003) · Biochemistry · doi:10.1021/bi027378p · Cited by 216
Self-citation
Mutational analysis of the structural organization of polyglutamine aggregates
Thakur, A. K., & Wetzel, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252523899 · Cited by 209
Structural Features of the Aβ Amyloid Fibril Elucidated by Limited Proteolysis
Kheterpal, I., Williams, A., Murphy, C., Bledsoe, B., & Wetzel, R. (2001) · Biochemistry · doi:10.1021/bi010805z · Cited by 200
The Parallel Superpleated Beta-structure as a Model for Amyloid Fibrils of Human Amylin
Kajava, A. V., Aebi, U., & Steven, A. C. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.029 · Cited by 191
Two-Dimensional Structure of β-Amyloid(10−35) Fibrils
Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C. (2000) · Biochemistry · doi:10.1021/bi991527v · Cited by 189
Direct visualisation of the β-sheet structure of synthetic Alzheimer’s amyloid 1 1Edited by F. E. Cohen
Serpell, L. C., & Smith, J. M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3650 · Cited by 176
Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange
Kheterpal, I., Zhou, S., Cook, K. D., & Wetzel, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250288897 · Cited by 170
A model for Ure2p prion filaments and other amyloids: The parallel superpleated β-structure
Kajava, A. V., Baxa, U., Wickner, R. B., & Steven, A. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402427101 · Cited by 167
Exploring amyloid formation by a de novo design
Kammerer, R. A., Kostrewa, D., Zurdo, J., Detken, A., García-Echeverría, C., Green, J. D., Müller, S. A., Meier, B. H., Winkler, F. K., Dobson, C. M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306786101 · Cited by 164
A Molecular Switch in Amyloid Assembly: Met35and Amyloid β-Protein Oligomerization
Bitan, G., Tarus, B., Vollers, S. S., Lashuel, H. A., Condron, M. M., Straub, J. E., & Teplow, D. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0349296 · Cited by 161
Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling
Jayasinghe, S. A., & Langen, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406853200 · Cited by 153
Determination of Solid-State NMR Structures of Proteins by Means of Three-Dimensional 15 N− 13 C− 13 C Dipolar Correlation Spectroscopy and Chemical Shift Analysis
Castellani, F., van Rossum, B., Diehl, A., Rehbein, K., & Oschkinat, H. (2003) · Biochemistry · doi:10.1021/bi034903r · Cited by 141
Parallel β-Sheets and Polar Zippers in Amyloid Fibrils Formed by Residues 10−39 of the Yeast Prion Protein Ure2p
Chan, J. C. C., Oyler, N. A., Yau, W., & Tycko, R. (2005) · Biochemistry · doi:10.1021/bi050724t · Cited by 141
Self-citation
NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106–126
Kuwata, K., Matumoto, T., Cheng, H., Nagayama, K., James, T. L., & Röder, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2433563100 · Cited by 135
Hydrogen−Deuterium (H/D) Exchange Mapping of Aβ1-40 Amyloid Fibril Secondary Structure Using Nuclear Magnetic Resonance Spectroscopy
Whittemore, N. A., Mishra, R., Kheterpal, I., Williams, A. D., Wetzel, R. B., & SERPERSU, E. H. (2005) · Biochemistry · doi:10.1021/bi048292u · Cited by 124
High‐Resolution Solid‐State NMR Spectroscopy of the Prion Protein HET‐s in Its Amyloid Conformation
Siemer, A. B., Ritter, C., Ernst, M., Riek, R., & Meier, B. H. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200462952 · Cited by 120
Arrangement of subunits and ordering of β-strands in an amyloid sheet
Serag, A. A., Altenbach, C., Gingery, M., Hubbell, W. L., & Yeates, T. O. (2002) · Nature Structural Biology · doi:10.1038/nsb838 · Cited by 117
Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy
Olofsson, A., Ippel, H., Wijmenga, S. S., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310605200 · Cited by 115
Constraints on Supramolecular Structure in Amyloid Fibrils from Two-Dimensional Solid-State NMR Spectroscopy with Uniform Isotopic Labeling
Tycko, R., & Ishii, Y. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0342042 · Cited by 114
Self-citation
An Atomic Model for the Pleated β-Sheet Structure of Aβ Amyloid Protofilaments
Li, L., Darden, T. A., Bartolotti, L. J., Kominos, D., & Pedersen, L. G. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77442-4 · Cited by 113
Core and Heterogeneity of β2-Microglobulin Amyloid Fibrils as Revealed by H/D Exchange
Yamaguchi, K., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H., & Goto, Y. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.067 · Cited by 102
Amyloid Fibrils May Be Assembled from β-Helical Protofibrils
Lazo, N. D., & Downing, D. T. (1998) · Biochemistry · doi:10.1021/bi971016d · Cited by 98
Structural diversity of amyloid fibril formed in human calcitonin as revealed by site‐directed 13C solid‐state NMR spectroscopy
Naito, A., Kamihira, M., Inoue, R., & Saitô, H. (2004) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1323 · Cited by 94
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy
Ippel, H., Olofsson, A., Schleucher, J., Lundgren, E., & Wijmenga, S. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132098999 · Cited by 86
Molecular modeling of the Abeta1-42 peptide from Alzheimer's disease
Chaney, M. O., Webster, S. D., Kuo, Y., & Roher, A. E. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.9.761 · Cited by 81
Prion Genetics: New Rules for a New Kind of Gene
Wickner, R. B., Edskes, H. K., Ross, E. D., Pierce, M. M., Baxa, U., Brachmann, A., & Shewmaker, F. P. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.092200 · Cited by 79
Dipolar recoupling NMR of biomolecular self-assemblies: determining inter- and intrastrand distances in fibrilized Alzheimer's β-amyloid peptide
Gregory, D. M., Benzinger, T. L. S., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Meredith, S. C., & Botto, R. E. (1998) · Solid State Nuclear Magnetic Resonance · doi:10.1016/s0926-2040(98)00086-1 · Cited by 75
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration
Laws, D. D., Bitter, H. L., Liu, K., Ball, H. L., Kaneko, K., Wille, H., Cohen, F. E., Prusiner, S. B., Pines, A., & Wemmer, D. E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201404298 · Cited by 73
Site-Specific Identification of Non-β-Strand Conformations in Alzheimer's β-Amyloid Fibrils by Solid-State NMR
Antzutkin, O. N., Balbach, J. J., & Tycko, R. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)70057-5 · Cited by 72
Self-citation
Molecular modeling of the core of Aβ amyloid fibrils
Guo, J., Wetzel, R. B., & Xu, Y. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20222 · Cited by 62
An Intersheet Packing Interaction in Aβ Fibrils Mapped by Disulfide Cross-Linking
Shivaprasad, S., & Wetzel, R. B. (2004) · Biochemistry · doi:10.1021/bi048019s · Cited by 59
Hydrogen Exchange-Mass Spectrometry Analysis of β-Amyloid Peptide Structure
Wang, S. S. ‐., Tobler, S. A., Good, T. A., & Fernández, E. (2003) · Biochemistry · doi:10.1021/bi0342766 · Cited by 53
Hydrogen-Deuterium Exchange in the Free and Immunoglobulin G-Bound Protein G B-Domain
Orban, J. P., Alexander, P., & Bryan, P. N. (1994) · Biochemistry · doi:10.1021/bi00185a006 · Cited by 37
The effect of vicinal polar and charged groups on hydrophobic hydration
Cheng, Y., & Rossky, P. J. (1999) · Biopolymers · doi:10.1002/(sici)1097-0282(199912)50:7<733::aid-bip6>3.0.co;2-7 · Cited by 34

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Paravastu, A. K., Leapman, R. D., Yau, W.-M., & Tycko, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806270105 · Cited by 1,160
Self-citation
Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., & Ishii, Y. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2991 · Cited by 818
Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide
Cerf, E., Sarroukh, R., Tamamizu-Kato, S., Breydo, L., Derclaye, S., Dufrêne, Y. F., Narayanaswami, V., Goormaghtigh, E., Ruysschaert, J.-M., & Raussens, V. (2009) · Biochemical Journal · doi:10.1042/bj20090379 · Cited by 494

See all 1,044

Authors: Petkova, A. T., Yau, W.-M., & Tycko, R.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2005-12-17
Volume: 45
Issue: 2
Pages: 498-512
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi051952q
OpenAlex: W2118280241
Cited by: 1,044
References: 84
FWCI: 24.63
Type: journal article
Language: en
Open access: green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources