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

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

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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

A Ferrocene‐Tagged Amyloid‐β Fragment for Rapid Screening of Aggregation Inhibitors from Natural Compounds by HPLC‐Electrochemical Detection

Zhang, L., Kai, T., Sun, Z., Hao, Y., Tu, Q., & Zhou, F. (2013) · Electroanalysis · doi:10.1002/elan.201300025 · Cited by 5

Design of a Coiled-Coil-based Model Peptide System to Explore the Fundamentals of Amyloid Fibril Formation

Steinmetz, M. O., Garc�a-Echeverr�a, C., & Kammerer, R. A. (2005) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-004-1720-4 · Cited by 5

Amyloid fibrillation of an intrinsically disordered plant phloem protein At PP16-1 under acidic condition

Swarupini, D. S., & Bhuyan, A. K. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.03.004 · Cited by 5

Inhibitors of beta-amyloid aggregation: still an issue of structure and function?

Talaga, P. E. (2004) · Drug Discovery Today Therapeutic Strategies · doi:10.1016/j.ddstr.2004.05.002 · Cited by 5

Differential binding and activation of caspase‐3 in cultured hippocampal neurons by assembly forms of Aβ1–42

John, P. A. S. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21251 · Cited by 5

Resilience and charge-dependent fibrillation of functional amyloid: Interactions of Pseudomonas biofilm-associated FapB and FapC amyloids

Golan, N., Parizat, A., Tabachnikov, O., Barnea, E., Olsen, W. P., Otzen, D. E., & Landau, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108096 · Cited by 4

A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils

Grover, S., Pham, T., Jones, A., Pereira, C. S., Maurino, M. V. D., Garrad, E. C., Makoni, N. J., Parks, A., Domalewski, R. J., Riggio, G., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15817 · Cited by 5

Self‐assembly of a peptide with a tandem repeat of the Aβ16‐22 sequence linked by a β turn‐promoting dipeptide sequence

Sundari, C. S., Bikshapathy, E., & Nagaraj, R. (2015) · Biopolymers · doi:10.1002/bip.22753 · Cited by 4

Methods for Studying and Structure–Function Relationships of Non-Fibrillar Protein Assemblies in Alzheimer's Disease and Related Disorders

Bitan, F. R. A. G. (2014) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608058525114020014 · Cited by 4

Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping

Hirota, S., Chiu, C.-L., Chang, C.-J., Lo, P.-H., Chen, T., Yang, H., Yamanaka, M., Mashima, T., Xie, C., Masuhara, H., et al. (2022) · Chemical Communications · doi:10.1039/d2cc04647d · Cited by 4

Differential effects of amyloid-beta peptide aggregation status on in vivo retinal neurotoxicity

Watts, H. R. (2010) · Eye and Brain · doi:10.2147/eb.s9902 · Cited by 4

A New Interpretative Paradigm for Conformational Protein Diseases

Agnati, L. F., Guidolin, D., Woods, A. S., Ciruela, F., Carone, C., Vallelunga, A., Escuela, D. O. B., Genedani, S., & Fuxé, K. (2013) · Current Protein and Peptide Science · doi:10.2174/1389203711314020006 · Cited by 4

The Potential of Small Molecules in Preventing Tau Oligomer Formation and Toxicity

Gerson, J. E., Cascio, F. L., & Kayed, R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00006-5 · Cited by 4

Alzheimer’s Disease and Type 2 Diabetes: Different Pathologies and Same Features

Di, M., Picone, P., Carrotta, R., Giacomazza, D., & San, P. L. (2011) · InTech eBooks · doi:10.5772/24390 · Cited by 4

Real-time protein aggregation monitoring with a Bloch surface wave-based approach

Santi, S., Barakat, E., Descrovi, E., Neier, R., & Herzig, H. P. (2014) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.2052842 · Cited by 4

Pharmacophore Fragment-Based Prediction and Gas-Phase ab Initio Optimization of Carvedilol Conformations

Almeida, D. R. P., Gasparro, D. M., Fülöp, F., & Csizmadia, I. G. (2004) · The Journal of Physical Chemistry A · doi:10.1021/jp040196f · Cited by 4

Synthesis of 6-[2-(Benzoxazol-2-ylmethylamino)ethoxy]-1-Alkyl-1H-lndole-2-Carboxylic acid and inhibitory activity on β-Amyloid aggregation

Lee, S., & Jeon, R. (2005) · Archives of Pharmacal Research · doi:10.1007/bf02978201 · Cited by 4

An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation

Yates, E. V., Meisl, G., Knowles, T., & Dobson, C. (2016) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b09663 · Cited by 5

A chemically engineered, stable oligomer mimic of amyloid β42 containing an oxime switch for fibril formation

Yamamoto, M., Shinoda, K., Ni, J., Sasaki, D., Kanai, M., & Sohma, Y. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob01875h · Cited by 4

Epitope-specific antibody fragments block aggregation of AGelD187N, an aberrant peptide in gelsolin amyloidosis

Leimu, L., Holm, P., Gąciarz, A., Haavisto, O., Prince, S., Pesonen, U., Huovinen, T., & Lamminmäki, U. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107507 · Cited by 3

A VEGF Fragment Encompassing Residues 10–30 Inhibits Aβ1–42 Amyloid Aggregation and Exhibits Neuroprotective Properties Matching the Full-Length Protein

Zimbone, S., Giuffrida, M. L., Sciacca, M. F. M., Carrotta, R., Librizzi, F., Milardi, D., & Grasso, G. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00669 · Cited by 3

Establishing the Links Between Aβ Aggregation and Cytotoxicity In Vitro Using Biophysical Approaches

Jan, A., & Lashuel, H. A. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-551-0_16 · Cited by 3

Cogitations on a proteocentric lexicon

Teplow, D. B. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00159-7 · Cited by 3

Amyloid imagingin vivo: implications for Alzheimer's disease management

Verhoeff, N. P. L. G. (2007) · Expert Opinion on Medical Diagnostics · doi:10.1517/17530059.1.3.337 · Cited by 3

APP-Based Transgenic Models: The Tg2576 Model

Deacon, R. M. J. (2010) · Neuromethods · doi:10.1007/978-1-60761-898-0_19 · Cited by 3

Assembly of redox active metallo-enzymes and metallo-peptides on electrodes: Abiological constructs to probe natural processes

Sarkar, A., Chattopadhyay, S., Mukherjee, M., Dey, S. G., & Dey, A. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102142 · Cited by 3

Few Ramachandran Angle Changes Provide Interaction Strength Increase in Aβ42 versus Aβ40 Amyloid Fibrils

Bastidas, O. H., Green, B., Sprague, M., & Peters, M. H. (2016) · Scientific Reports · doi:10.1038/srep36499 · Cited by 3

Comparison of Cerebrospinal Fluid Amyloidogenic Nanoplaques With Core Biomarkers of Alzheimer’s Disease

Aksnes, M., Tiiman, A., Edwin, T. H., Terenius, L. Y., Bogdanović, N., Vukojević, V. B., & Knapskog, A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.608628 · Cited by 3

Thermodynamics and Protein Folding

Baskakov, I. V. (2005) · doi:10.1002/9783527619344.ch4 · Cited by 3

AMYLOID: A NATURAL NANOMATERIAL

Maji, S. K. (2011) · International Journal of Nanoscience · doi:10.1142/s0219581x11009362 · Cited by 2

Preparation and Structural Characterization of Pre-fibrillar Assemblies of Amyloidogenic Proteins

Frydman‐Marom, A., Bram, Y., & Gazit, E. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_3 · Cited by 2

Antifibrillizing agents catalyze the formation of unstable intermediate aggregates of beta‐amyloid

Wang, M. S., Boddapati, S. P., & Sierks, M. R. (2010) · Biotechnology Progress · doi:10.1002/btpr.396 · Cited by 2

The Amyloid _-Protein and Alzheimer's Disease

Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2

Correlation between Stability and Propensity to Form Amyloid-like Fibrils

Kenig, M., Türk, V., Rabzelj, S., & erovnik, E. (2004) · CRC Press eBooks · doi:10.1201/9781420037494.ch7 · Cited by 2

Spectroscopic Studies of Proteins and Their Interactions with Lipids and Small Molecules

Xiong, J. (2014) · MOspace Institutional Repository (University of Missouri) · Cited by 2

Dityrosine cross-link trapping of amyloid-β intermediates reveals that self-assembly is required for Aβ-induced cytotoxicityPreprint

Maina, M. B., Mengham, K., Burra, G., Al-Hilaly, Y. K., & Serpell, L. (2020) · bioRxiv · doi:10.1101/2020.03.25.007690 · Cited by 2

Biologically Active Fragment of the Receptor for Advanced Glycation End Products (RAGE) Is Able to Inhibit Oligomerization of the Beta-Amyloid

Volkova, T. D., Avetisyan, A. V., Koroev, D. O., Kamynina, A. V., Balasanyants, S. M., Simonyan, R. A., & Volpina, O. M. (2022) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162022040197 · Cited by 1

Effect of C- and N-Terminal Polyhistidine Tags on Aggregation of Influenza A Virus Nuclear Export Protein

Koroleva, O. N., Kuzmina, N. V., Tolstova, A. P., Dubrovin, E. V., & Drutsa, V. L. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924120125 · Cited by 1

GAL-201 as a Promising Amyloid-β-Targeting Small-Molecule Approach for Alzheimer’s Disease Treatment: Consistent Effects on Synaptic Plasticity, Behavior and Neuroinflammation

Riemann, K., von Ahsen, J., Böhm, T., Schlegel, M., Kreuzer, M., Fenzl, T., Russ, H., Parsons, C. G., & Rammes, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094167 · Cited by 1

Aortic Stiffness and Alzheimer’s Disease: The Medin Connection

Triposkiadis, F. K., Xanthopoulos, A. V., Boudoulas, H. K., & Brutsaert, D. L. (2025) · Biomolecules · doi:10.3390/biom15081148 · Cited by 2

On the potential roles of TDP-43 in the formation of membraneless organelles and their transformation into toxic aggregates

Sergeeva, O. S., Neklesova, M. V., Reushev, V. A., Artemov, A. V., Константинович, Т. К., Константинович, Т. К., Uversky, V. N., & Fonin, A. V. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152808 · Cited by 2

Structure and Toxicity of the Prefibrillar Aggregation States of Beta Peptides in Alzheimer’s Disease

Perico, A., Galante, D., & D’Arrigo, C. (2011) · InTech eBooks · doi:10.5772/20764 · Cited by 1

Neurotoxicity of the Alzheimer’s β-Amyloid Peptide

Howlett, D. R. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-888-5_6 · Cited by 1

Comparative study on the conformational stability of human and murine amyloid β peptide

Shen, L., & Ji, H. (2011) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2011.06.012 · Cited by 1

Pathology of synapses in neurological diseases

Schwarzman, A. L., & Sarantseva, S. V. (2014) · Biology Bulletin Reviews · doi:10.1134/s2079086415020085 · Cited by 1

Aggregation Propensity of Neuronal Receptors: Potential Implications in Neurodegenerative Disorders

Navarro, S., Díaz-Caballero, M., Illa, R., & Ventura, S. (2015) · Future Science OA · doi:10.4155/fso.15.39 · Cited by 1

Stochiometric Inhibition of β-Amyloid Fibrillogenesis using Cα,α-Disubstituted Amino Acid Containing Peptides

Etienne, M. A., Bett, C. K., Aucoin, J. P., Jensen, T. J., McCarley, R. L., Ajmo, T., Herber, D. L., Morgan, D., & Hammer, R. P. (2010) · Springer eBooks · doi:10.1007/978-0-387-26575-9_201 · Cited by 1

The Application of Biophysical Techniques to the Study of the Inhibition of Aggregation of Aβ Using PINPs Liposomes

Tinker, C. L. (2016) · Springer theses · doi:10.1007/978-3-319-39534-0_8 · Cited by 1

Alzheimer’s Disease and the Aggregation of Amyloid β

Tinker, C. L. (2016) · Springer theses · doi:10.1007/978-3-319-39534-0_3 · Cited by 1

Alzheimer’s Disease and Mechanism-Based Attempts to Enhance Cognition

Draffin, J. E., Knafo, S., & Heneka, M. T. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-417042-1.00009-7 · Cited by 1

Amyloid-β Effects on Peripheral Nerve: A New Model System

Stecker, M. M., Srivastava, A., & Reiss, A. B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914488 · Cited by 2

Molecular insight into cross-interaction between amyloid β isoforms and its effect on aggregation pathways

Wang, L., Park, S., Choi, J. H., Lee, C. Y., Eom, K., & Kwon, T. (2025) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2025.2475221 · Cited by 1

Single-Molecule Studies of Amyloidogenic Proteins

Kellermayer, M., Karsai, Á., Murvai, Ü., Erdélyi‐Bótor, S., Kardos, J., & Pires, R. H. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4921-8_7 · Cited by 1

Mouse Models of Alzheimer’s Disease

German, D. C. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_16 · Cited by 1

Impact of aspartate racemization on the conformational stability of Aβ(1–42)

Shen, L., & Ji, H. (2010) · Journal of Molecular Structure THEOCHEM · doi:10.1016/j.theochem.2010.04.014 · Cited by 1

Targets and Strategies Toward the Development of Alzheimer Therapeutics

Wolfe, M. S. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2016_14 · Cited by 2

Reviews in Computational Chemistry, Volume 22

Crippen, G. M. (2006) · Journal of the American Chemical Society · Cited by 1

Aβ Structure and Aggregation

Glabe, C. G., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_7 · Cited by 1

Interaction of Alzheimer Amyloid Peptide with Cell Surfaces and Artificial Membranes

Bateman, D. A., & Chakrabartty, A. (2011) · Wiley eBooks · doi:10.1002/9783527634323.ch11 · Cited by 1

Domain swapping as a molecular mechanism in amyloidosis

Wahlbom, M. (2007) · Lund University Publications (Lund University) · Cited by 1

Apolipoprotein E: Structural and Functional Interactions with Amyloid β

Stine, W. B., & LaDu, M. J. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch10 · Cited by 1

Protein Folding, Unfolding and Aggregation Studied Using an All-Atom Model with~a~Simplified Interaction Potential

Irbäck, A. (2007) · Springer eBooks · doi:10.1007/978-3-540-74029-2_10 · Cited by 1

Characterization of Interactions Between Misfolding Proteins and Molecular Chaperones by NMR Spectroscopy

Reif, B., & Narayanan, S. (2006) · Springer eBooks · doi:10.1007/128_066 · Cited by 1

Impact of Physical Exercise on the Hippocampal Pathology and Cognition in a Mouse Model of Alzheimer's Disease

Maliszewska‐Cyna, E. (2016) · TSpace (University of Toronto) · Cited by 1

Protein Misfolding and Disease

Scheinost, J. C., Boldt, G. E., & Wentworth, P. (2012) · Chemical biology · doi:10.1002/9781118435762.ch19 · Cited by 1

The dynamic nature of amyloid-beta protein aggregation and its association to Alzheimer’s disease

Vilaprinyó-Pascual, S. (2015) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)

Nanotechnology for Cerebral Delivery of Nutraceuticals for the Treatment of Neurodegenerative Diseases

Sahni, J. K., Doggui, S., Dao, L. H., & Ramassamy, C. (2011) · Wiley eBooks · doi:10.1002/9780470960844.ch10

Structural and Toxic Properties of Protein Aggregates: Towards a Molecular Understanding of Alzheimer's Disease

Wang, L., & Campioni, S. (2011) · InTech eBooks · doi:10.5772/20922

Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine

Stefani, M. (2011) · Wiley eBooks · doi:10.1002/9783527634323.ch5

Fluorescence correlation spectroscopy: ultrasensitive detection in clear and turbid media

Tahari, A. (2006) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)

Thermodynamics of Amyloid Formation

Baskakov, I. V. (2008) · Protein Science Encyclopedia · doi:10.1002/9783527610754.md12

Protein Misfolding and Disease

Scheinost, J. C., Boldt, G. E., & Wentworth, P. (2008) · Wiley eBooks · doi:10.1002/9780470048672.wecb647

Protein misfolding and amyloid formation

Nerelius, C. (2009) · Epsilon Open Archive (Sveriges lantbruksuniversitet biblioteket (Swedish University of Agricultural Sciences))

Anti‐Misfolding and Anti‐Fibrillization Therapies for Protein Misfolding Disorders

Martin, Z. S., & Soto, C. A. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch43

Study of the aggregation process of the amyloid beta-protein associated to Alzheimer's disease. Examination of pharmaceutically important small molecules.

Vidal, B. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Alzheimer's disease and dementia with Lewy bodies: Special focus on the role of serpins

Nielsen, H. M. (2007) · Lund University Publications (Lund University)

Pathogenic mechanisms of the Arctic Alzheimer mutation.

Sahlin, C. (2007) · Uppsala University Publications (Uppsala University)

Biophysical Investigations of the Aβ Aggregation Process

Muni, S. C. (2014) · D-Scholarship@Pitt (University of Pittsburgh)

Biophysical understanding of novel synthetic amyloid-beta (Abeta) prions in Alzheimer's disease

Kumar, A. (2013)

To Fold or To Fibrillate? Serendipity in Stability Studies

Szczepankiewicz, O. (2011) · Lund University Publications (Lund University)

A Drosophila Disease-Model for Transthyretin-associated Amyloidosis

Pokrzywa, M. (2008) · Diva portal (Dalarna University Library)

SPECIFIC AMYLOID-BETA OLIGOMERS IN HUMAN CEREBROSPINAL FLUID

Handoko, M. (2012) · University of Minnesota Digital Conservancy (University of Minnesota)

Characterization of the Alzheimer´s disease-associated clac protein

Söderberg, L. (2005) · Figshare

Amyloid Fibrils: Growth as Seen by Time Lapse, Atomic Force Microscopy

Pavelka, M., & Roth, J. (2010) · Functional Ultrastructure · doi:10.1007/978-3-211-99390-3_148

The kinetics and thermodynamics of polyglutamine aggregation

Landrum, E. (2013) · D-Scholarship@Pitt (University of Pittsburgh)

Targeting cytotoxic species in amyloid diseases

Persson, M. (2012)

Amyloid-β Protofibrils in Alzheimer´s Disease : Focus on Antibodies, Inflammation and Astrocytes

Söllvander, S. (2015) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Establishment and validation of hippocampal LTP for characterization of memory enhancing drugs as potential treatment of Alzheimers disease

Würzburg, J.-M.-U. (2011)

Enfermedad de Alzheimer: una panorámica desde su primera descripción hacia una perspectiva molecular

García, S., Vázquez, R. M. C., Dávalos, E. G. M., Castillo, J. L., Silva, B. M., & Ortiz, A. D. J. V. (2009) · Medicina Interna de México

Self-Assembling Peptides as Potential Carriers for the Delivery of the Hydrophobic Anticancer Agent Ellipticine

Fung, S. (2008) · UWSpace (University of Waterloo)

Dynamics of amyloid plaque formation in Alzheimer’s Disease

McCarter, J. F. (2014) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.17434

Vascular mechanisms of AD pathogenesis

Grossman, H. A. (2010) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t31c1wp9

Protein stability in shear flow

Bekard, I. B. (2010) · Minerva Access (University of Melbourne)

Using capillary electrophoresis to detect amyloid protein aggregation

Kurtz, J. (2012) · Journal of the Arkansas Academy of Science

Synthesis, biophysical analysis and biological evaluation of tricyclic pyrones and pyridinones as anti-alzheimer agents

Rana, S. (2009) · K-State Research Exchange (Kansas State University)

Review Alzheimer ß-amyloid peptides: normal and abnormal localization

Edgar, M. A., & Gouras, G. K. (2002)

Nanoscale Imaging and Characterisation of Amyloid-β

Tinker, C. L. (2016) · Springer theses · doi:10.1007/978-3-319-39534-0

Identification of tissue transglutaminase protein network

Battaglini, P., & Edomi, P. (2010)

Amyloid-β Protofibril Formation and Neurotoxicity : Implications for Alzheimer’s Disease

Johansson, A. (2007) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Untitled work

Shinpo (2000) · doi:10.1002/1097-4547(20001101)62:3

Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates

Walsh, D., Hartley, D., Kusumoto, Y., Fezoui, Y., Condron, M., Lomakin, A. A., Benedek, G., Selkoe, D., & Teplow, D. (1999) · eScholarship (California Digital Library)

Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein

Harper, J. D., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90303-3 · Cited by 452

Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 699

Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease.

Kirkitadze, M. D., & Kowalska, A. (2005) · Acta Biochimica Polonica · doi:10.18388/abp.2005_3454 · Cited by 77

Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & Selkoe, D. J. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 817