Amyloid β-Protein Fibrillogenesis

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051

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

Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill

Hansen, M., Nielsen, S. E., & Berg, K. (1989) · Journal of Immunological Methods · doi:10.1016/0022-1759(89)90397-9 · Cited by 3,488

Candidate gene for the chromosome 1 familial Alzheimer’s disease locus

Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.

Pan, K. M., Baldwin, M. A., Nguyen, J. T., Gasset, M., Serban, A. V., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,281

The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780

Are there generic mechanisms governing interactions between nanoparticles and cells? Epitope mapping the outer layer of the protein–material interface

Lynch, I. (2006) · Physica A Statistical Mechanics and its Applications · doi:10.1016/j.physa.2006.06.008 · Cited by 65

Environment‐ and mutation‐dependent aggregation behavior of Alzheimer amyloid β‐protein

Yamamoto, N., Hasegawa, K., Matsuzaki, K., Naiki, H., & Yanagisawa, K. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02459.x · Cited by 67

Alzheimer’s disease: biological aspects, therapeutic perspectives and diagnostic tools

Carlo, M. D., Giacomazza, D., & Biagio, P. L. S. (2012) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/24/24/244102 · Cited by 67

Tauroursodeoxycholic acid prevents E22Q Alzheimer’s Aβ toxicity in human cerebral endothelial cells

Viana, R. J. S., Nunes, A. F., Castro, R. E., Ramalho, R. M., Meyerson, J. L., Fossati, S., Ghiso, J. A., Rostagno, A. A., & Rodrigues, C. M. P. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-8746-x · Cited by 64

A comparative molecular dynamics analysis of the amyloid β-peptide in a lipid bilayer

Lemkul, J. A., & Bevan, D. R. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.11.004 · Cited by 64

Strategic Design of Amyloid-β Species Fluorescent Probes for Alzheimer’s Disease

Su, D., Diao, W., Li, J., Pan, L., Zhang, X., Wu, X., & Mao, W. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00810 · Cited by 64

Anti-amyloidogenic, anti-oxidant and anti-apoptotic role of gelsolin in Alzheimer’s disease

Chauhan, V. P. S., Ji, L., & Chauhan, A. (2008) · Biogerontology · doi:10.1007/s10522-008-9169-z · Cited by 63

Binding, Conformational Transition and Dimerization of Amyloid-β Peptide on GM1-Containing Ternary Membrane: Insights from Molecular Dynamics Simulation

Manna, M., & Mukhopadhyay, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071308 · Cited by 63

Iron chelation as a potential therapy for neurodegenerative disease

Hider, R. C., Ma, Y., Molina‐Holgado, F., Gaeta, A., & Roy, S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361304 · Cited by 64

Promotion of formation of amyloid fibrils by aluminium adenosine triphosphate (AlATP)

Exley, C., & Korchazhkina, O. V. (2001) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00171-4 · Cited by 63

Modulation of Amyloid-β1–40 Transport by ApoA1 and ApoJ Across an in vitro Model of the Blood-Brain Barrier

Merino-Zamorano, C., Fernández-de Retana, S., Montañola, A., Batlle, A., Saint-Pol, J., Mysiorek, C., Gosselet, F., Montaner, J., & Hernández-Guillamon, M. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-150976 · Cited by 63

Amyloid-beta immunotherapy: the hope for Alzheimer disease?

Barrera-Ocampo, A. A., & Lopera, F. J. (2016) · Colombia medica · doi:10.25100/cm.v47i4.2640 · Cited by 64

Effects of sphingomyelin, cholesterol and zinc ions on the binding, insertion and aggregation of the amyloid Aβ1−40 peptide in solid‐supported lipid bilayers

Devanathan, S., Salamon, Z., Lindblom, G., Gröbner, G., & Tollin, G. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05162.x · Cited by 69

The Unique Alzheimer’s β-Amyloid Triangular Fibril Has a Cavity along the Fibril Axis under Physiological Conditions

Miller, Y., Ma, B., & Nussinov, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1100273 · Cited by 62

Potential Links between Impaired One-Carbon Metabolism Due to Polymorphisms, Inadequate B-Vitamin Status, and the Development of Alzheimer’s Disease

Troesch, B., Weber, P., & Mohajeri, M. H. (2016) · Nutrients · doi:10.3390/nu8120803 · Cited by 63

Amyloid β-Peptide Oligomerization in S ilico : Dimer and Trimer

Jang, S., & Shin, S. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp055568e · Cited by 62

Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target

Oakley, S. S., Maina, M. B., Marshall, K. E., Al‐Hilaly, Y. K., Harrington, C., Wischik, C. M., & Serpell, L. C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590754 · Cited by 59

Fibrillation in Human Serum Albumin Is Enhanced in the Presence of Copper(II)

PANDEY, N. K., Ghosh, S., & Dasgupta, S. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp103876p · Cited by 61

The Polyphenol Piceid Destabilizes Preformed Amyloid Fibrils and Oligomers In Vitro: Hypothesis on Possible Molecular Mechanisms

Rivière, C., Delaunay, J.-C., Immel, F., Cullin, C., & Monti, J. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9883-6 · Cited by 63

Role of water‐soluble amyloid‐β in the pathogenesis of Alzheimer's disease

Tabaton, M., & Piccini, A. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00428.x · Cited by 65

Amyloid-like Fibril Formation in an All β-Barrel Protein Involves the Formation of Partially Structured Intermediate(s)

Srisailam, S., Wang, H.-M., Kumar, T. K. S., Rajalingam, D., Vaithiyalingam, S., Sheu, H., Chang, Y., & Yu, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110762200 · Cited by 61

On the subject of rigor in the study of amyloid β-protein assembly

Teplow, D. B. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt203 · Cited by 60

Conformational Intermediate of the Amyloidogenic Protein β2-Microglobulin at Neutral pH

Heegaard, N. H. H., Sen, J. W., Kaarsholm, N. C., & Nissen, M. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104452200 · Cited by 61

Ubiquitous Amyloids

Puławski, W., Ghoshdastider, U., Andrisano, V., & Filipek, S. (2012) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-012-9549-3 · Cited by 60

p3 peptide, a truncated form of Aβ devoid of synaptotoxic effect, does not assemble into soluble oligomers

Dulin, F., Léveillé, F., Becerril-Ortega, J., Mornon, J., Buisson, A., Callebaut, I., & Colloc’h, N. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.05.002 · Cited by 73

Amyloid Fibril Formation by the Glaucoma-Associated Olfactomedin Domain of Myocilin

Orwig, S. D., Perry, C. W., Kim, L. Y., Turnage, K. C., Zhang, R., Vollrath, D., Schmidt‐Krey, I., & Lieberman, R. L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.016 · Cited by 59

Structural Differences between Aβ(1-40) Intermediate Oligomers and Fibrils Elucidated by Proteolytic Fragmentation and Hydrogen/Deuterium Exchange

Zhang, A., Qi, W., Good, T. A., & Fernández, E. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.10.022 · Cited by 60

Oligomerization of β-amyloid of the Alzheimer’s and the Dutch-cerebral-haemorrhage types

SIAN, A. K., Frears, E. R., El‐Agnaf, O. M. A., PATEL, B. P., Manca, M. F., Siligardi, G., Hussain, R., & Austen, B. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3490299 · Cited by 61

The Peculiar Role of the A2V Mutation in Amyloid-β (Aβ) 1–42 Molecular Assembly

Messa, M., Colombo, L., Favero, E. D., Cantú, L., Stoilova, T., Cagnotto, A., Rossi, A., Morbin, M., Fede, G. D., Tagliavini, F., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576256 · Cited by 59

Co‐incorporation of Aβ40 and Aβ42 to form mixed pre‐fibrillar aggregates

Frost, D., Gorman, P. M., Yip, C. M., & Chakrabartty, A. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03415.x · Cited by 59

Conformational Restriction via Cyclization in β-Amyloid Peptide Aβ(1-28) Leads to an Inhibitor of Aβ(1-28) Amyloidogenesis and Cytotoxicity

Kapurniotu, A., Buck, A. K., Weber, M., Schmauder, A., Hirsch, T., Bernhagen, J., & Tatarek‐Nossol, M. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00022-x · Cited by 59

Self-Assembly of β-Amyloid 42 Is Retarded by Small Molecular Ligands at the Stage of Structural Intermediates

Bohrmann, B., Adrian, M., Dubochet, J., Kuner, P., Müller, F., Huber, W., Nordstedt, C., & Döbeli, H. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4241 · Cited by 58

In vitro fibrillogenesis of the amyloid β1–42 peptide: cholesterol potentiation and aspirin inhibition

Harris, J. R. (2002) · Micron · doi:10.1016/s0968-4328(02)00029-x · Cited by 59

Inhibitor Discovery Targeting the Intermediate Structure of β-Amyloid Peptide on the Conformational Transition Pathway: Implications in the Aggregation Mechanism of β-Amyloid Peptide

Liu, D., Xu, Y., Yu, F., Liu, H., Shen, X., Chen, K., Ma, J., & Jiang, H. (2006) · Biochemistry · doi:10.1021/bi060955f · Cited by 59

Linker Histone H1 Binds to Disease Associated Amyloid-like Fibrils

Duce, J. A., Smith, D. P., Blake, R. E., Crouch, P. J., Li, Q., Masters, C. L., & Trounce, I. A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.038 · Cited by 62

Fluorescence Anisotropy: A Method for Early Detection of Alzheimer β-Peptide (Aβ) Aggregation

Allsop, D., Swanson, L., Moore, S., Davies, Y., York, A., El‐Agnaf, O. M. A., & Soutar, I. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5123 · Cited by 59

Neurodegenerative pathways as targets for acquired epilepsy therapy development

Casillas-Espinosa, P. M., Ali, I. Y., & O'Brien, T. J. (2020) · Epilepsia Open · doi:10.1002/epi4.12386 · Cited by 59

Misfolding of the amyloid β‐protein: A molecular dynamics study

Flöck, D., Colacino, S., Colombo, G., & Nola, A. D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20683 · Cited by 58

Synergistic Inhibitory Effect of GQDs–Tramiprosate Covalent Binding on Amyloid Aggregation

Liu, Y., Xu, L.-P., Wang, Q., Yang, B., & Zhang, X. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00439 · Cited by 58

Neuron Specific Toxicity of Oligomeric Amyloid-β: Role for JUN-Kinase and Oxidative Stress

Ebenezer, P. J., Weidner, A. M., LeVine, H., Markesbery, W. R., Murphy, M. P., Zhang, L., Dasuri, K., Fernandez-Kim, S. O., Bruce-Keller, A. J., Gavilán, E., et al. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-101161 · Cited by 58

Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation

Österlund, N., Lundqvist, M., Ilag, L. L., Gräslund, A., & Emanuelsson, C. S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013459 · Cited by 57

Pharmacotherapeutic targets in Alzheimer's disease

Biran, Y., Masters, C. L., Barnham, K. J., Bush, A. I., & Adlard, P. A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00595.x · Cited by 59

Tissue transglutaminase: A novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases

Wilhelmus, M. M. M., van Dam, A., & Drukarch, B. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.01.059 · Cited by 56

Interaction of human stefin B in the prefibrillar oligomeric form with membranes

Anderluh, G., Gutiérrez‐Aguirre, I., Rabzelj, S., Čeru, S., Kopitar‐Jerala, N., Maček, P., Türk, V., & Žerovnik, E. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04717.x · Cited by 57

Pressure-jump NMR Study of Dissociation and Association of Amyloid Protofibrils

Kamatari, Y. O., Yokoyama, S., Tachibana, H., & Akasaka, K. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.010 · Cited by 57

Mutant Presenilin 1 Increases the Expression and Activity of BACE1

Giliberto, L., Borghi, R., Piccini, A., Mangerini, R., Sorbi, S., Cirmena, G., Garuti, A., Ghetti, B. F., Tagliavini, F., Mughal, M. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805685200 · Cited by 56

Computational Study on the Structural Diversity of Amyloid Beta Peptide (Aβ10-35) Oligomers

Jang, S., & Shin, S. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp076450w · Cited by 56

Stable Size Distribution of Amyloid Plaques Over the Course of Alzheimer Disease

Serrano‐Pozo, A., Mielke, M. L., Muzitansky, A., Gómez‐Isla, T., Growdon, J. H., Bacskai, B. J., Betensky, R. A., Frosch, M. P., & Hyman, B. T. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825e77de · Cited by 57

Neurodegeneration and Alzheimer’s disease: the lesson from tauopathies

Sorrentino, G., & Bonavita, V. (2007) · Neurological Sciences · doi:10.1007/s10072-007-0789-x · Cited by 56

6-Shogaol has anti-amyloidogenic activity and ameliorates Alzheimer’s disease via CysLT1R-mediated inhibition of cathepsin B

Na, J., Song, K., Lee, J.-W., Kim, S., & Kwon, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.06.026 · Cited by 56

Toxicity mediated by soluble oligomers of β‐amyloid(1–42) on cholinergic SN56.B5.G4 cells

Heinitz, K., Beck, M., Schliebs, R., & Perez-Polo, J. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04015.x · Cited by 58

Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases

Bigi, A., Cascella, R., Chiti, F., & Cecchi, C. (2022) · BioEssays · doi:10.1002/bies.202200086 · Cited by 56

Mechanical manipulation of Alzheimer’s amyloid β1–42 fibrils

Karsai, Á., Mártonfalvi, Z., Nagy, A., Grama, L., Penke, B., & Kellermayer, M. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.12.015 · Cited by 55

Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease

Dickerson, T. J., & Janda, K. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332847100 · Cited by 55

The Effect of Aβ Conformation on the Metal Affinity and Aggregation Mechanism Studied by Circular Dichroism Spectroscopy

Chen, Y. R., Huang, H., Chyan, C. L., Shiao, M. S., Lin, T. H., & Chen, Y. C. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj083 · Cited by 54

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Johansson, A., Bergquist, J., Volbracht, C., Päiviö, A., Leist, M., Lannfelt, L., & Westlind‐Danielsson, A. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3280b07c21 · Cited by 53

The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP

Gao, M., & Winter, R. (2015) · Journal of Diabetes Research · doi:10.1155/2015/849017 · Cited by 54

Prevention of Alzheimer's Disease-associated Aβ Aggregation by Rationally Designed Nonpeptidic β-Sheet Ligands

Rzepecki, P., Nagel‐Steger, L., Feuerstein, S., Linne, U., Molt, O., Zadmard, R., Aschermann, K., Wehner, M., Schrader, T. H., & Riesner, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405914200 · Cited by 54

Amyloid fibril formation by human stefin B: influence of pH and TFE on fibril growth and morphology

Žerovnik, E., Škarabot, M., Škerget, K., Giannini, S., Žerovnik, E., Škarabot, M., Škerget, K., Giannini, S., Stoka, V., Kokalj, S. J., et al. (2007) · Amyloid · doi:10.1080/13506120701461137 · Cited by 54

The relationship between the aggregational state of the amyloid‐β peptides and free radical generation by the peptides

Monji, A., Utsumi, H., Ueda, T., Imoto, T., Yoshida, I., Hashioka, S., Tashiro, K., & Tashiro, N. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00392.x · Cited by 53

Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease

Murakami, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.940275 · Cited by 53

Mitochondria in Aging and Alzheimer's Disease

Crouch, P. J., Cimdins, K., Duce, J. A., Bush, A. I., & Trounce, I. A. (2007) · Rejuvenation Research · doi:10.1089/rej.2007.0592 · Cited by 54

Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry

Ly, T., & Julian, R. R. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.07.006 · Cited by 53

New evidence that the Alzheimer β-amyloid peptide does not spontaneously form free radicals: An ESR study using a series of spin-traps

Turnbull, S., Tabner, B. J., El‐Agnaf, O. M. A., Twyman, L. J., & Allsop, D. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00510-x · Cited by 54

Expansion of Polyglutamine Induces the Formation of Quasi-aggregate in the Early Stage of Protein Fibrillization

Tanaka, M., Machida, Y., Nishikawa, Y., Akagi, T., Hashikawa, T., Fujisawa, T., & Nukina, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209852200 · Cited by 53

Iowa Variant of Familial Alzheimer’s Disease

Tomidokoro, Y., Rostagno, A. A., Neubert, T. A., Lu, Y., Rebeck, G. W., Frangione, B., Greenberg, S. M., & Ghiso, J. A. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090636 · Cited by 54

Two Disaccharides and Trimethylamine N-Oxide Affect Aβ Aggregation Differently, but All Attenuate Oligomer-Induced Membrane Permeability

Qi, W., Zhang, A., Good, T. A., & Fernández, E. (2009) · Biochemistry · doi:10.1021/bi9006397 · Cited by 52

Simultaneous Single-Molecule Fluorescence and Conductivity Studies Reveal Distinct Classes of Aβ Species on Lipid Bilayers

Schauerte, J. A., Wong, P., Wisser, K. C., Ding, H., Steel, D. G., & Gafni, A. (2010) · Biochemistry · doi:10.1021/bi901444w · Cited by 52

Proinsulin Is Refractory to Protein Fibrillation

Huang, K., Dong, J., Phillips, N. B., CAREY, P. R., & Weiss, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507110200 · Cited by 53

Differential toxicity, conformation and morphology of typical initial aggregation states of Aβ1-42 and Aβpy3-42 beta-amyloids

Galante, D., Corsaro, A., Florio, T., Vella, S., Pagano, A., Sbrana, F., Vassalli, M., Perico, A., & D’Arrigo, C. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.08.010 · Cited by 51

Small moleculeβ‐amyloid inhibitors that stabilize protofibrillar structuresin vitroimprove cognition and pathology in a mouse model of Alzheimer’s disease

Hawkes, C. A., Deng, L., Shaw, J. E., Nitz, M., & McLaurin, J. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07052.x · Cited by 53

Exploring the Mechanism of Inhibition of Au Nanoparticles on the Aggregation of Amyloid-β(16-22) Peptides at the Atom Level by All-Atom Molecular Dynamics

Song, M., Sun, Y., Luo, Y., Zhu, Y., Liu, Y., & Li, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061815 · Cited by 52

Internalisation and toxicity of amyloid‐β 1‐42 are influenced by its conformation and assembly state rather than size

Vadukul, D. M., Maina, M. B., Franklin, H., Nardecchia, A., Serpell, L. C., & Marshall, K. E. (2020) · FEBS Letters · doi:10.1002/1873-3468.13919 · Cited by 51

Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalline intermediate phase

Hamodrakas, S. J., Hoenger, A., & Iconomidou, V. A. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.004 · Cited by 52

The Arctic mutation interferes with processing of the amyloid precursor protein

Stenh, C., Nilsberth, C., ck, J. H., Engvall, B., Nšslund, J., & Lannfelt, L. (2002) · Neuroreport · doi:10.1097/00001756-200210280-00005 · Cited by 52

Bacterial Extracellular DNA Promotes β-Amyloid Aggregation

Tetz, G. V., & Tetz, V. (2021) · Microorganisms · doi:10.3390/microorganisms9061301 · Cited by 50

A Kinetic Model for β-Amyloid Adsorption at the Air/Solution Interface and Its Implication to the β-Amyloid Aggregation Process

Jiang, D., Dinh, K. L., Ruthenburg, T. C., Zhang, Y., Su, L., Land, D. P., & Zhou, F. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp8085792 · Cited by 51

Hacking the Code of Amyloid Formation

Pastor, M. T., Esteras‐Chopo, A., & Serrano, L. G. (2007) · Prion · doi:10.4161/pri.1.1.4100 · Cited by 51

The Cu(II)/Aβ/Human Serum Albumin Model of Control Mechanism for Copper-Related Amyloid Neurotoxicity

Rózga, M., & Bal, W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900358j · Cited by 54

Early detection of insulin fibrillation: a fluorescence lifetime assay to probe the pre-fibrillar regime.

Mohanty, J., Choudhury, S., Pal, H., & Bhasikuttan, A. C. (2012) · Chemical Communications · doi:10.1039/c2cc16974f · Cited by 46

Surface enhanced Raman spectroscopy distinguishes amyloid Β‐protein isoforms and conformational states

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