Structural Characterization of a Soluble Amyloid β-Peptide Oligomer

Molecular cloning: A laboratory manual

Deininger, P. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,682

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment

Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506

Pathways towards and Away from Alzheimer’s Disease

Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 1,996

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

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530

Folding proteins in fatal ways

Selkoe, D. J. (2003) · Nature · doi:10.1038/nature02264 · Cited by 1,417

Amyloid pores from pathogenic mutations

Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., & Lansbury, P. T. (2002) · Nature · doi:10.1038/418291a · Cited by 1,289

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

Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044

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

Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?

Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989

Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum.

Arispe, N., Rojas, E., & Pollard, H. B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.567 · Cited by 926

Structural Classification of Toxic Amyloid Oligomers

Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783

Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculations

Nilges, M., Clore, G. M., & Gronenborn, A. M. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)81148-7 · Cited by 770

Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains

Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618

X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

Kirschner, D. A., Abraham, C., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.2.503 · Cited by 565

Globular amyloid β‐peptide 1−42 oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559

Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid

Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B., & Ishii, Y. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1345 · Cited by 544

A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins

Goto, N. K., Gardner, K. H., Mueller, G. A., Willis, R. C., & Kay, L. E. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008393201236 · Cited by 512

A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity

Yamazaki, T., Lee, W., Arrowsmith, C. H., Muhandiram, D. R., & Kay, L. E. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00105a005 · Cited by 499

Structures for amyloid fibrils

Makin, O. S., & Serpell, L. C. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.05025.x · Cited by 461

Correlations of synaptic and pathological markers with cognition of the elderly

Dickson, D. W., Crystal, H. A., Bevona, C., Honer, W., Vincent, I., & Davies, P. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00013-5 · Cited by 410

On the nucleation of amyloid β‐protein monomer folding

Lazo, N. D., Grant, M. A., Condron, M. C., Rigby, A. C., & Teplow, D. B. (2005) · Protein Science · doi:10.1110/ps.041292205 · Cited by 331

Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice

Martins, I. C., Kuperstein, I., Wilkinson, H., Maes, E., Vanbrabant, M., Jonckheere, W., Van Gelder, P., Hartmann, D., D'Hooge, R., De Strooper, B., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601953 · Cited by 311

[11] Multidimensional heteronuclear nuclear magnetic resonance of proteins

Marius Clore, G., & Gronenborn, A. M. (1994) · Methods in Enzymology · doi:10.1016/s0076-6879(94)39013-4 · Cited by 272

Isotope-filtered 2D NMR of a protein-peptide complex: study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin

Ikura, M., & Bax, A. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00033a019 · Cited by 271

Simulations as analytical tools to understand protein aggregation and predict amyloid conformation

Ma, B., & Nussinov, R. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.08.018 · Cited by 222

The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers

Eisenberg, D., Nelson, R., Sawaya, M. R., Balbirnie, M., Sambashivan, S., Ivanova, M. I., Madsen, A. Ø., & Riekel, C. (2006) · Accounts of Chemical Research · doi:10.1021/ar0500618 · Cited by 179

General structural motifs of amyloid protofilaments

Ferguson, N., Becker, J., Tidow, H., Tremmel, S., Sharpe, T. D., Krause, G., Flinders, J., Petrovich, M., Berriman, J., Oschkinat, H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607815103 · Cited by 177

The Solvent Protection of Alzheimer Amyloid-β-(1–42) Fibrils as Determined by Solution NMR Spectroscopy

Olofsson, A., Sauer-Eriksson, A. E., & Öhman, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508962200 · Cited by 123

Familial Alzheimer's disease mutations alter the stability of the amyloid β-protein monomer folding nucleus

Grant, M. A., Lazo, N. D., Lomakin, A., Condron, M. M., Arai, H., Yamin, G., Rigby, A. C., & Teplow, D. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705197104 · Cited by 121

Aβ-globulomers are formed independently of the fibril pathway

Gellermann, G. P., Byrnes, H., Striebinger, A., Ullrich, K., Mueller, R., Hillen, H., & Barghorn, S. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.01.010 · Cited by 117

Untitled work

(1999) · doi:10.1002/1531-8249(199912)46:6<860::aid-ana8>3.0.co;2-m

Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development

Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111

Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies

Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 584

Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease

Masters, C. L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006262 · Cited by 542

Alzheimer's disease: synaptic dysfunction and Aβ

Shankar, G. M., & Walsh, D. M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-48 · Cited by 486