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

Globular and Protofibrillar Aβ Aggregates Impair Neurotransmission by Different Mechanisms

Moreth, J., Kroker, K. S., Schwanzar, D., Schnack, C., Arnim, C. A. F. V., Hengerer, B., Rosenbrock, H., & Kußmaul, L. (2013) · Biochemistry · doi:10.1021/bi3016444 · Cited by 24

A Dual-Pronged Approach: A Ruthenium(III) Complex That Modulates Amyloid-β Aggregation and Disrupts Its Formed Aggregates

Yawson, G. K., Will, M. F., Huffman, S. E., Strandquist, E. T., Bothwell, P. J., Oliver, E. B., Apuzzo, C. F., Platt, D. C., Weitzel, C. S., Jones, M. A., et al. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c01651 · Cited by 22

Experimental Inhibition of Fibrillogenesis and Neurotoxicity by amyloid-beta (Aβ) and Other Disease-Related Peptides/Proteins by Plant Extracts and Herbal Compounds

Kumar, S., Okello, E. J., & Harris, J. R. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_13 · Cited by 23

RS‐4252 Inhibits Amyloid β‐Induced Cytotoxicity in HeLa Cells

Nishimura, S., Murasugi, T., Kubo, T., Kaneko, I., Meguro, M., Marumoto, S., Kogen, H., Koyama, K., Oda, T., & Nakagami, Y. (2003) · Pharmacology & Toxicology · doi:10.1034/j.1600-0773.2003.930104.x · Cited by 22

Structural and functional properties of peptides based on the N-terminus of HIV-1 gp41 and the C-terminus of the amyloid-beta protein

Gordon, L. M., Nisthal, A., Lee, A. B., Eskandari, S., Ruchala, P. P., Jung, C., Waring, A. J., & Mobley, P. W. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.05.002 · Cited by 22

Two-Photon and Time-Resolved Fluorescence Spectroscopy as Probes for Structural Determination in Amyloid-β Peptides and Aggregates

Clark, T. B., Ziółkowski, M., Schatz, G. C., & Goodson, T. G., III (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp500883s · Cited by 22

Fibrillar tau alters cerebral endothelial cell metabolism, vascular inflammatory activation, and barrier function in vitro and in vivo

Guzman‐Hernandez, R. A., & Fossati, S. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70077 · Cited by 23

The conformational epitope for a new Aβ42 protofibril‐selective antibody partially overlaps with the peptide N‐terminal region

Colvin, B. A., Rogers, V. A., Kulas, J. A., Ridgway, E. A., Amtashar, F. S., Combs, C. K., & Nichols, M. R. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14211 · Cited by 21

Functional adlayers on Au electrodes: some recent applications in hydrogen evolution and oxygen reduction

Chattopadhyay, S., Sarkar, A., Chatterjee, S., & Dey, A. (2017) · Journal of Materials Chemistry A · doi:10.1039/c7ta09179f · Cited by 21

Self-Assembly of Aβ40, Aβ42 and Aβ43 Peptides in Aqueous Mixtures of Fluorinated Alcohols

Pachahara, S. K., Adicherla, H., & Nagaraj, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136567 · Cited by 21

Glutamatergic synaptic depression by synthetic amyloid β‐peptide in the medial septum

Santos‐Torres, J., de la Fuente, A., Criado, J. M., Riolobos, A. S., Heredia, M., & Yajeya, J. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21150 · Cited by 21

Apolipoprotein Aβ: Black Sheep in a Good Family

Kontush, A. (2004) · Brain Pathology · doi:10.1111/j.1750-3639.2004.tb00088.x · Cited by 21

NMR structure of the Arctic mutation of the Alzheimer’s Aβ(1–40) peptide docked to SDS micelles

Usachev, K. S., Filippov, A. V., Khairutdinov, B. I., Antzutkin, O. N., & Klochkov, V. V. (2014) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2014.08.030 · Cited by 20

Influence of the electric field on supramolecular structure and properties of amyloid-specific reagent Congo red

Spólnik, P., Król, M., Stopa, B., Konieczny, L., Piekarska, B., Rybarska, J., Zemanek, G., Jagusiak, A., Piwowar, P., Szoniec, G., et al. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0750-z · Cited by 20

Structure‐Activity Relationships for a Series of Compounds that Inhibit Aggregation of the Alzheimer's Peptide, Aβ42

McKoy, A. F., Chen, J., Schüpbach, T., & Hecht, M. H. (2014) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12341 · Cited by 20

Methylene blue activates the PMCA activity and cross-interacts with amyloid β-peptide, blocking Aβ-mediated PMCA inhibition

Berrocal, M., Corbacho‐Cuello, I., Gutiérrez‐Merino, C., & Mata, A. M. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.07.012 · Cited by 20

In Situ Observation of Amyloid Nucleation and Fibrillation by FastScan Atomic Force Microscopy

Huang, Q., Wang, H., Gao, H., Cheng, P., Zhu, L., Wang, C., & Yang, Y. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b03143 · Cited by 20

Early active immunization with Aβ 3–10 -KLH vaccine reduces tau phosphorylation in the hippocampus and protects cognition of mice

Cao, Y., Wang, J.-C., Zhu, K., Zhang, H., Wang, G., & Liu, H. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.266061 · Cited by 20

Mathematical Models to Shed Light on Amyloid-Beta and Tau Protein Dependent Pathologies in Alzheimer’s Disease

Vosoughi, A., Sadigh‐Eteghad, S., Ghorbani, M., Shahmorad, S., Farhoudi, M., Rafi, M. A., & Omidi, Y. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.09.017 · Cited by 20

Molecular dynamics studies of hexamers of amyloid‐β peptide (16–35) and its mutants: Influence of charge states on amyloid formation

Han, W., & Wu, Y. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21232 · Cited by 20

Refining the amyloid β peptide and oligomer fingerprint ambiguities in Alzheimer’s disease: Mass spectrometric molecular characterization in brain, cerebrospinal fluid, blood, and plasma

Michno, W., Blennow, K., Zetterberg, H., & Brinkmalm, G. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15466 · Cited by 18

Stability of early-stage amyloid-β(1–42) aggregation species

Coalier, K. A., Paranjape, G. S., Karki, S., & Nichols, M. R. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.08.017 · Cited by 20

Two Distinct Conformations of Aβ Aggregates on the Surface of Living PC12 Cells

Bateman, D. A., & Chakrabartty, A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.01.056 · Cited by 19

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions

Cieplak, A. S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180905 · Cited by 21

Aptamers Selected for Recognizing Amyloid β-Protein—A Case for Cautious Optimism

Rahimi, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030668 · Cited by 18

Metal- and UV- Catalyzed Oxidation Results in Trapped Amyloid-β Intermediates Revealing that Self-Assembly Is Required for Aβ-Induced Cytotoxicity

Maina, M. B., Burra, G., Al‐Hilaly, Y. K., Mengham, K., Fennell, K., & Serpell, L. C. (2020) · iScience · doi:10.1016/j.isci.2020.101537 · Cited by 18

Mechanisms of the self-assembly of EAK16-family peptides into fibrillar and globular structures: molecular dynamics simulations from nano- to micro-seconds

Emamyari, S., Kargar, F., Sheikhhassani, V., Emadi, S., & Fazli, H. (2015) · European Biophysics Journal · doi:10.1007/s00249-015-1024-y · Cited by 19

Influence of Hyperglycemic Conditions on Self-Association of the Alzheimer’s Amyloid β (Aβ1–42) Peptide

Menon, S., & Sengupta, N. (2017) · ACS Omega · doi:10.1021/acsomega.7b00018 · Cited by 19

Probing the role of ortho-dihydroxy groups on lysozyme fibrillation

Konar, M., Ghosh, D., Roy, P., & Dasgupta, S. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.12.115 · Cited by 19

Amyloid-β(1−42) Fibrillar Precursors Are Optimal for Inducing Tumor Necrosis Factor-α Production in the THP-1 Human Monocytic Cell Line

Ajit, D., Udan, M. L. D., Paranjape, G. S., & Nichols, M. R. (2009) · Biochemistry · doi:10.1021/bi9003777 · Cited by 18

Concentration dependent switch in the kinetic pathway of lysozyme fibrillation: Spectroscopic and microscopic analysis

Kumar, E. K., Prasad, D. K., & Prabhu, N. P. (2017) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2017.04.011 · Cited by 19

Envisaging the Structural Elevation in the Early Event of Oligomerization of Disordered Amyloid β Peptide

Roy, A., Chandra, K., Dolui, S., & Maiti, N. C. (2017) · ACS Omega · doi:10.1021/acsomega.7b00522 · Cited by 18

The blood clotting F actor XIIIa forms unique complexes with amyloid‐beta ( A β) and colocalizes with deposited A β in cerebral amyloid angiopathy

de Jager, M., Boot, M. V., Bol, J. G. J. M., Brevé, J. J. P., Jongenelen, C. A. M., Drukarch, B., & Wilhelmus, M. M. M. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12244 · Cited by 18

Tuning self-assembled morphology of the Aβ(16–22) peptide by substitution of phenylalanine residues

Wang, J., Tao, K., Zhou, P., Pambou, E., Li, Z., Xu, H., Rogers, S. E., King, S. M., & Lu, J. R. (2016) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2016.07.052 · Cited by 18

Synthesis, Structure, and Cholinergic Effect of Novel Neuroprotective Compounds Bearing the Tacrine Pharmacophore

Kristián, P., Hamuľaková, S., Jun, D., Kuča, K., Imrich, J., Danihel, I., Böhm, S., & Klika, K. D. (2008) · Heterocycles · doi:10.3987/com-08-s(n)83 · Cited by 18

ALZ ‐801 prevents amyloid β‐protein assembly and reduces cytotoxicity: A preclinical experimental study

Muramatsu, D., Watanabe‐Nakayama, T., Tsuji, M., Umeda, K., Hikishima, S., Nakano, H., Sakashita, Y., Ikeda, T., Konno, H., Kodera, N., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202402622r · Cited by 18

Amyloid oligomers and their membrane toxicity - A perspective study

Nutini, A. (2024) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2024.01.002 · Cited by 17

Stabilization Mechanism for a Nonfibrillar Amyloid β Oligomer Based on Formation of a Hydrophobic Core Determined by Dissipative Particle Dynamics

Kawai, R., Chiba, S., Okuwaki, K., Kanada, R., Doi, H., Ono, M., Mochizuki, Y., & Okuno, Y. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00602 · Cited by 17

Insights in the structural understanding of amyloidogenicity and mutation-led conformational dynamics of amyloid beta (Aβ) through molecular dynamics simulations and principal component analysis

Raghavan, S. S., Iqbal, S., Ayyadurai, N., & Gunasekaran, K. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1871955 · Cited by 18

Aggregation of Aβ(1–42) in the presence of short peptides: conformational studies

Laczkó, I., Vass, E., Soós, K., Fülöp, L., Zarándi, M., & Penke, B. (2008) · Journal of Peptide Science · doi:10.1002/psc.990 · Cited by 17

A synthetic amyloid lawn system for high-throughput analysis of amyloid toxicity and drug screening

Girigoswami, K., Ku, S. H., Ryu, J., & Park, C. B. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.03.022 · Cited by 17

Validation and Characterization of a Novel Peptide That Binds Monomeric and Aggregated β-Amyloid and Inhibits the Formation of Neurotoxic Oligomers

Barr, R. K., Verdile, G., Wijaya, L. K., Morici, M., Taddei, K., Gupta, V. B., Pedrini, S., Jin, L., Nicolazzo, J. A., Knock, E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679993 · Cited by 16

Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures

Terrill, S. E., Colvin, B. A., Davenport, R. E., & Nichols, M. R. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.03.017 · Cited by 18

Nordihydroguaiaretic Acid Does Not Disaggregate β-Amyloid(1–40) Protofibrils but Does Inhibit Growth Arising from Direct Protofibril Association

Moss, M. A., Varvel, N. H., Nichols, M. R., Reed, D. K., & Rosenberry, T. L. (2004) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)05642-6 · Cited by 17

Alzheimer's Disease Aβ Peptide Fragment 10–30 Forms a Spectrum of Metastable Oligomers with Marked Preference for N to N and C to C Monomer Termini Proximity

Jabłonowska, A., Bakun, M., Kupniewska-Kozak, A., & Dadlez, M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.083 · Cited by 17

Two-Photon and Time-Resolved Fluorescence Conformational Studies of Aggregation in Amyloid Peptides

Wang, Y., Clark, T. B., & Goodson, T. G., III (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp101496y · Cited by 17

pH Effects on the Conformational Preferences of Amyloid β‐Peptide (1–40) in HFIP Aqueous Solution by NMR Spectroscopy

Valerio, M., Porcelli, F., Zbilut, J. P., Giuliani, A., Manetti, C., & Conti, F. (2008) · ChemMedChem · doi:10.1002/cmdc.200700324 · Cited by 18

A Molecular Dynamics Study of the Interaction of d-Peptide Amyloid Inhibitors with Their Target Sequence Reveals a Potential Inhibitory Pharmacophore Conformation

Esteras‐Chopo, A., Morra, G., Moroni, E., Serrano, L. G., de la Paz, M. L., & Colombo, G. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.076 · Cited by 17

Kinetics of peptide secondary structure conversion during amyloid β-protein fibrillogenesis

Steckmann, T., Awan, Z., Gerstman, B. S., & Chapagain, P. P. (2012) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2012.02.012 · Cited by 17

The Amyloid β Protein

Lazo, N. D., Maji, S. K., Fradinger, E. A., Bitan, G., & Teplow, D. B. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch17 · Cited by 18

PaCS Is a Novel Cytoplasmic Structure Containing Functional Proteasome and Inducible by Cytokines/Trophic Factors

Sommi, P., Necchi, V., Vitali, A., Montagna, D., Luigi, A. D., Salmona, M., Ricci, V., & Solcia, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082560 · Cited by 16

Early oligomerization stages for the non-amyloid component of α-synuclein amyloid

Eugene, C., Laghaei, R., & Mousseau, N. (2014) · The Journal of Chemical Physics · doi:10.1063/1.4896381 · Cited by 16

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

Kundel, F., Tosatto, L., Whiten, D. R., Wirthensohn, D. C., Horrocks, M. H., & Klenerman, D. (2018) · FEBS Journal · doi:10.1111/febs.14409 · Cited by 16

Search for New Aggregable Fragments of Human Insulin

Świontek, M., Frączyk, J., Waśko, J., Chaberska, A., Pietrzak, Ł., Kaminski, Z. J., Szymański, Ł., Wiak, S., & Kolesińska, B. (2019) · Molecules · doi:10.3390/molecules24081600 · Cited by 16

AβP1-42 incorporation and channel formation in planar lipid membranes: the role of cholesterol and its oxidation products

Meleleo, D., Galliani, A., & Notarachille, G. (2013) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9513-0 · Cited by 18

A peptide probe for detection of various beta-amyloid oligomers

Hu, Y., Su, B., Zheng, H., & Kim, J. R. (2012) · Molecular BioSystems · doi:10.1039/c2mb25148e · Cited by 17

α-Glycerylphosphorylethanolamine rescues astrocytes from mitochondrial impairment and oxidative stress induced by amyloid β-peptides

Bisaglia, M. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(03)00131-1 · Cited by 16

A spectroscopic study of some of the peptidyl radicals formed following hydroxyl radical attack on β-amyloid and α-synuclein

Tabner, B. J., Turnbull, S., King, J. E., Benson, F. E., El‐Agnaf, O. M. A., & Allsop, D. (2006) · Free Radical Research · doi:10.1080/10715760600632545 · Cited by 16

Interactions of Alzheimer amyloid peptides with cultured cells and brain tissue, and their biological consequences

Bateman, D. A., & Chakrabartty, A. (2004) · Biopolymers · doi:10.1002/bip.10561 · Cited by 16

Secondary Structure Assignment of Amyloid-β Peptide Using Chemical Shifts

Wood, G. P. F., & Röthlisberger, U. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct200156e · Cited by 15

Is abeta a sufficient biomarker for monitoring anti-abeta clinical studies? A critical review

Moreth, J., Mavoungou, C., & Schindowski, K. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00025 · Cited by 15

Amyloid-like assembly of the low complexity domain of yeast Nab3

O'Rourke, T. W., Loya, T. J., Head, P. E., Horton, J., & Reines, D. (2015) · Prion · doi:10.1080/19336896.2014.997618 · Cited by 18

Estrés oxidativo, péptido β-amiloide y enfermedad de Alzheimer

Manzano‐León, N., & Mas‐Oliva, J. (2006) · Gaceta Médica de México · Cited by 16

Differing modes of interaction between monomeric Aβ1–40 peptides and model lipid membranes: an AFM study

Sheikh, K. H., Giordani, C., McManus, J. J., Hovgaard, M. B., & Jarvis, S. (2011) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2011.11.011 · Cited by 15

Is there correlation between Aβ-heme peroxidase activity and the peptide aggregation state? A literature review combined with hypothesis

Khodarahmi‬, R., & Ashrafi-Kooshk, M. R. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.09.074 · Cited by 15

Strikingly different effects of cholesterol and 7-ketocholesterol on lipid bilayer-mediated aggregation of amyloid beta (1-42)

Phan, H. T. T., Shimokawa, N., Sharma, N., Takagi, M., & Vestergaard, M. C. M. (2018) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2018.04.007 · Cited by 15

A rapid method to measure beta-amyloid induced neurotoxicity in vitro

Patel, D. A., & Good, T. A. (2006) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2006.10.004 · Cited by 15

Mitochondrial dysfunction induced by a post-translationally modified amyloid linked to a familial mutation in an alternative model of neurodegeneration

Todd, K. L., Fossati, S., Ghiso, J. A., & Rostagno, A. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.09.010 · Cited by 15

HSPB2/MKBP, a novel and unique member of the small heat‐shock protein family

Hu, Z., Yang, B., Lu, W., Zhou, W., Zeng, L., Li, T., & Wang, X. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21682 · Cited by 15

Oligomeric amyloid-β(1–42) induces THP-1 human monocyte adhesion and maturation

Crouse, N. R., Ajit, D., Udan, M. L. D., & Nichols, M. R. (2008) · Brain Research · doi:10.1016/j.brainres.2008.11.093 · Cited by 17

Insulin Fibril Nucleation: The Role of Prefibrillar Aggregates

Smith, M. I., Sharp, J. S., & Roberts, C. J. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.131482 · Cited by 15

Targeting APP metabolism for the treatment of Alzheimer's disease

Sambamurti, K., Hardy, J., Refolo, L. M., & Lahiri, D. K. (2002) · Drug Development Research · doi:10.1002/ddr.10077 · Cited by 14

Binding of amyloid peptides to domain‐swapped dimers of other amyloid‐forming proteins may prevent their neurotoxicity

Taler‐Verčič, A., & Žerovnik, E. (2010) · BioEssays · doi:10.1002/bies.201000079 · Cited by 14

Amyloid-β and the Failure to Form Mitochondrial Cristae: A Biomimetic Study Involving Artificial Membranes

Khalifat, N., Puff, N., Dliaa, M., & Angelova, M. I. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110389 · Cited by 14

All or none fibrillogenesis of a prion peptide

Zou, W., Yang, D., Fraser, P. E., Cashman, N. R., & Chakrabartty, A. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02415.x · Cited by 14

Amyloid β derived switch-peptides as a tool for investigation of early events of aggregation: a combined experimental and theoretical approach

Paul, A., Sharma, B., Mondal, T., Thalluri, K., Paul, S., & Mandal, B. (2015) · MedChemComm · doi:10.1039/c5md00466g · Cited by 13

Adsorption of Amyloid β (1-40) Peptide at Liquid Interfaces

Brezesinski, G., Maltseva, E., & Möhwald, H. (2006) · Zeitschrift für Physikalische Chemie · doi:10.1524/zpch.2007.221.1.95 · Cited by 14

Probing the amyloid-β(1–40) fibril environment with substituted tryptophan residues

Touchette, J. C., Williams, L. L., Ajit, D., Gallazzi, F., & Nichols, M. R. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.12.007 · Cited by 14

Role of Polyunsaturated Fatty Acids for Misfolding Protein Aggregations

Kim, Y., & Takahashi, R. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.021 · Cited by 14

Neprilysin protects human neuronal progenitor cells against impaired development caused by amyloid-β peptide

Mazur‐Kolecka, B., & Frackowiak, J. (2006) · Brain Research · doi:10.1016/j.brainres.2006.09.064 · Cited by 14

Intrinsic Amyloidogenic Behavior of Terminally Protected Alzheimer’s Aβ17–21 Peptide: Self-Aggregation and Amyloid-Like Fibril Formation

Haldar, D., & Banerjee, A. (2007) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-006-9072-x · Cited by 14

Design and Characterization of Chemically Stabilized Aβ42 Oligomers

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