Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

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

Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor

Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403

Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein

Weidemann, A., König, G., Bunke, D., Fischer, P. Q., Salbaum, J. M., Masters, C. L., & Beyreuther, K. T. (1989) · Cell · doi:10.1016/0092-8674(89)90177-3 · Cited by 1,233

Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity

Kitaguchi, N., Takahashi, Y., Tokushima, Y., Shiojiri, S., & Ito, H. (1988) · Nature · doi:10.1038/331530a0 · Cited by 1,083

Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction

Sarin, V. K., Kent, S. B. H., Tam, J. P., & Merrifield, R. B. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90704-1 · Cited by 1,066

A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors

Ponte, P. A., Gonzalez‐DeWhitt, P. A., Schilling, J., Miller, J., Hsu, D. K., Greenberg, B., Davis, K. L., Wallace, W., Lieberburg, I. M., Fuller, F. H., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,050

Road to Alzheimer’s Disease: The Pathomechanism Underlying

Anand, R., Kaushal, A., Wani, W. Y., & Gill, K. D. (2011) · Pathobiology · doi:10.1159/000332218 · Cited by 16

Time-Evolved SERS Signatures of DEP-Trapped Aβ and Zn2+Aβ Peptides Revealed by a Sub-10 nm Electrode Nanogap

Vu, K. H. P., Lee, M., Blankenburg, G. H., Chang, Y., Chu, M.-L., Erbe, A., Lesser‐Rojas, L., Chen, Y., & Chou, C. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c01521 · Cited by 15

EDEM1 Regulates Amyloid Precursor Protein (APP) Metabolism and Amyloid-β Production

Nowakowska-Gołacka, J., Czapiewska, J., Sominka, H., Sowa-Rogozińska, N., & Słomińska-Wojewódzka, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010117 · Cited by 14

Structural properties of Aβ (1–40) peptide in protonation stage of one, two, and three: New insights from the histidine protonation behaviors

Sun, Y., Yao, Z., & Shi, H. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.11.061 · Cited by 15

Fine Mapping of the Amyloid β-Protein Binding Site on Myelin Basic Protein

Kotarba, A. E., Aucoin, D., Hoos, M. D., Smith, S. O., & Nostrand, W. E. V. (2013) · Biochemistry · doi:10.1021/bi4001936 · Cited by 15

Electrochemical detection of Zn(II)- and Cu(II)-induced amyloid-β aggregation: Quantitative aspects and application to amyloid-β isoforms

Suprun, E. V., Radko, S. P., Andreev, E. A., Khmeleva, S. A., Kozin, S. A., Makarov, A. А., Archakov, A. I., & Shumyantseva, V. V. (2017) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2017.03.011 · 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

Aβ Upregulates and Colocalizes with LGI3 in Cultured Rat Astrocytes

Kimura, N., Ishii, Y., Suzaki, S., Negishi, T., Kyuwa, S., & Yoshikawa, Y. (2007) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-006-9127-8 · Cited by 16

Role of fibrillar Aβ25–35in the inflammation induced rat model with respect to oxidative vulnerability

Masilamoni, J. G., Jesudason, E. P., Jesudoss, K. S., Murali, J., Paul, S. F. D., & Rajadas, J. (2005) · Free Radical Research · doi:10.1080/10715760500117373 · Cited by 15

Proteic composition of corpora amylacea in the bovine mammary gland

Claudon, C., Francin, M., Marchal, E., Straczeck, J., Laurent, F., & Nabet, P. (1998) · Tissue and Cell · doi:10.1016/s0040-8166(98)80040-2 · Cited by 15

Molecular pathology of Alzheimer's disease

MULLAN, M. J. (1993) · International Review of Psychiatry · doi:10.3109/09540269309037798 · Cited by 16

Decreased Brain pH Correlated With Progression of Alzheimer Disease Neuropathology: A Systematic Review and Meta-Analyses of Postmortem Studies

Hagihara, H., & Miyakawa, T. (2024) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyae047 · Cited by 16

A novel method for expression and purification of authentic amyloid-β with and without 15N labels

Liao, Y., & Chen, Y. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.05.002 · Cited by 14

Bax inhibitor 1 is a γ-secretase–independent presenilin-binding protein

Wu, S., Song, W., Wong, C. C. L., & Shi, Y. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810870116 · Cited by 14

Reduced Influence of apoE on Aβ43 Aggregation and Reduced Vascular Aβ43 Toxicity as Compared with Aβ40 and Aβ42

Jäkel, L., Biemans, E. A. L. M., Klijn, C. J. M., Kuiperij, H. B., & Verbeek, M. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01873-x · Cited by 15

Evidence for D-Aspartyl-β-Amyloid Secretase Activity in Human Brain

Lee, J. M., Petrucelli, L., Fisher, G. H., Ramdath, S., Castillo, J., Fiore, M. M. D., & D’Aniello, A. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.2.125 · Cited by 14

The protective role of dl-α-lipoic acid in biogenic amines catabolism triggered by Aβ amyloid vaccination in mice

Jesudason, E. P., Masilamoni, J. G., Kirubagaran, R., Dicky John Davis, G., & Rajadas, J. (2005) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2005.01.010 · Cited by 14

Congo red reverses amyloid β protein-induced cellular stress in astrocytes

Abe, K., Kato, M., & Saitō, H. (1997) · Neuroscience Research · doi:10.1016/s0168-0102(97)00081-3 · Cited by 14

Spectroscopic investigations of synthetic beta amyloid peptides of Alzheimer's disease

Elhaddaoui, A., Pigorsch, E., Delacourte, A., & Turrell, S. (1995) · Journal of Molecular Structure · doi:10.1016/0022-2860(95)08558-d · Cited by 14

Biological Markers for Alzheimer's Disease

Tapiola, T. (2001) · Cited by 14

Involvement of amyloid as a central step in the development of Alzheimer's disease

Robakis, N. K. R. K., & Pangalos, M. N. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90189-9 · Cited by 14

The Role of Aβ-Peptide on Spatial Memory, EEG, Auditory Evoked Potentials And Nicotinic Cholinergic Receptors in A/P Transgenic Mice

Wang, J. (2003) · Cited by 14

Complement activation by the amyloid proteins Aβ peptide and β2-microglobulin

Nybo, M., Nielsen, E. H., & Svehag, S.-E. (1999) · Amyloid · doi:10.3109/13506129909007338 · Cited by 13

Potential role of IP3/Ca2+ signaling and phosphodiesterases: Relevance to neurodegeneration in Alzheimer’s disease and possible therapeutic strategies

Dutta, B. J., Singh, S., Seksaria, S., Gupta, G. D., Bodakhe, S. H., & Singh, A. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115071 · Cited by 15

The N-terminal region of myelin basic protein reduces fibrillar amyloid-β deposition in Tg-5xFAD mice

Ou-Yang, M.-H., Xu, F., Liao, M.-C., Davis, J., Robinson, J. K., & Nostrand, W. E. V. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.10.006 · Cited by 14

Aging, microglia and cytoskeletal regulation are key factors in the pathological evolution of the APP23 mouse model for Alzheimer's disease

Janssen, L., Dubbelaar, M. L., Holtman, I. R., de Boer-Bergsma, J. J., Eggen, B. J. L., Boddeke, H. W. G. M., Deyn, P. P. D., & Dam, D. V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.014 · Cited by 13

Selecting Aβ Isoforms for An Alzheimer’s Disease Cerebrospinal Fluid Biomarker Panel

Somers, C., Goossens, J., Engelborghs, S., & Bjerke, M. (2017) · Biomarkers in Medicine · doi:10.2217/bmm-2016-0276 · Cited by 13

Self-assembling peptides in biomedicine and bioengineering

Koutsopoulos, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-100736-5.00015-6 · Cited by 13

Biological Effects and Mechanisms of Taurine in Various Therapeutics

Sharma, S., Sahoo, B. M., & Banik, B. K. (2023) · Current Drug Discovery Technologies · doi:10.2174/1570163820666230525101353 · Cited by 14

Copper Modulation of Amyloid Beta 42 Interactions with Model Membranes

Weber, D. K., Gehman, J. D., Separovic, F., & Sani, M. (2012) · Australian Journal of Chemistry · doi:10.1071/ch12015 · Cited by 13

Humanin Structural Versatility and Interaction with Model Cerebral Cortex Membranes

Pistolesi, S., Rossini, L., Ferro, E., Basosi, R., Trabalzini, L., & Pogni, R. (2009) · Biochemistry · doi:10.1021/bi900187s · Cited by 13

Studies on the Role of Amino Acid Stereospecificity in Amyloid Beta Aggregation

Gupta, V. B., Indi, S. S., & Rao, K. S. J. (2007) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-0070-z · Cited by 13

pH-Dependent Conformational Ensemble and Polymorphism of Amyloid-β Core Fragment

Xu, W., Zhang, C., Morozova‐Roche, L. A., Zhang, J. Z. H., & Mu, Y. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp404034x · Cited by 14

Thiazole–Carbonyl Interactions: A Case Study Using Phenylalanine Thiazole Cyclic Tripeptides

Mali, S. M., Schneider, T. F., Bandyopadhyay, A., Jadhav, S. V., Werz, D. B., & Gopi, H. N. (2012) · Crystal Growth & Design · doi:10.1021/cg301147s · Cited by 13

Effect of d-amino acids at Asp23 and Ser26 residues on the conformational preference of Aβ20–29 peptides

Shanmugam, G., Polavarapu, P. L., Hallgas, B., & Májer, Z. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.136 · Cited by 13

Astrocytic uptake of posttranslationally modified amyloid‐β leads to endolysosomal system disruption and induction of pro‐inflammatory signaling

Wirth, S., Schlößer, A., Beiersdorfer, A., Schweizer, M., Woo, M. S., Friese, M. A., Lohr, C., & Grochowska, K. M. (2024) · Glia · doi:10.1002/glia.24539 · Cited by 12

Ultrafast colorimetric determination of predominant protein structure evolution with gold nanoplasmonic particles

Kim, H. Y., & Choi, I. (2015) · Nanoscale · doi:10.1039/c5nr06517h · Cited by 12

Autophagy-ERK1/2-Involved Disinhibition of Hippocampal Neurons Contributes to the Pre-Synaptic Toxicity Induced by Aβ 42 Exposure

Yin, Y., Zhao, Y., Han, S., Zhang, N., Chen, H., & Wang, X. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170246 · Cited by 12

New Insights into the Structural and Binding Properties on Aβ Mature Fibrils Due to Histidine Protonation Behaviors

Shi, H., Sun, Y., Yao, Z., & Bai, M. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00487 · Cited by 12

Proposal of therapeutic curcumin derivatives for Alzheimer’s disease based on ab initio molecular simulations

Shinzato, T., Sato, R., Suzuki, K., Tomioka, S., Sogawa, H., Shulga, S., Blume, Y. B., & Kurita, N. (2019) · Chemical Physics Letters · doi:10.1016/j.cplett.2019.136883 · Cited by 12

Blood and Cerebrospinal Fluid Autoantibody to Aβ Levels in Patients with Alzheimer’s Disease: a Meta-Analysis Study

Li, X., Li, X., Liu, Q., & Cheng, Y. (2020) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01528-5 · Cited by 13

Probing Alzheimer amyloid peptide aggregation using a cell-free fluorescent protein refolding method

Arslan, P. E., & Chakrabartty, A. (2009) · Biochemistry and Cell Biology · doi:10.1139/o09-038 · Cited by 12

Development of a humanized C1q A chain knock-in mouse: Assessment of antibody independent ß-amyloid induced complement activation

Li, M., Ager, R. R., Fraser, D. A., Tjokro, N. O., & Tenner, A. J. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.02.022 · Cited by 12

Studies on the Interactions of Copper and Zinc Ions with β-Amyloid Peptides by a Surface Plasmon Resonance Biosensor

Yao, F., Zhang, R., Tian, H., & Li, X. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130911832 · Cited by 12

Fibrillogenesis in gelsolin-related familial amyloidosis

Maury, C. P. J., Nurmiaho‐Lassila, E., Boysen, G., & Liljeström, M. (2003) · Amyloid · doi:10.1080/13506129.2003.12088564 · Cited by 12

Expression and processing of pathologic proteins in alzheimer's disease

Anderton, B. H. (1993) · Hippocampus · doi:10.1002/hipo.1993.4500030726 · Cited by 12

Induced pluripotent stem cell models as a tool to investigate and test fluid biomarkers in Alzheimer's disease and frontotemporal dementia

McInvale, J. J., Canoll, P., & Hargus, G. (2024) · Brain Pathology · doi:10.1111/bpa.13231 · Cited by 11

Live Cell FRET Imaging Reveals Amyloid β-Peptide Oligomerization in Hippocampal Neurons

Gao, Y., Wennmalm, S., Winblad, B. G., Schedin‐Weiss, S., & Tjernberg, L. O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094530 · Cited by 11

Amyloid cascade hypothesis, tau synthesis, and role of oxidative stress in AD

Vyas, J., Raytthatha, N., & Prajapati, B. G. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13205-6.00023-6 · Cited by 13

Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure

Altman, R., Ly, S., Hilt, S., Petrlová, J., Maezawa, I., Kálai, T., Hideg, K., Jin, L., Laurence, T. A., & Voss, J. C. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.09.002 · Cited by 11

Late age increase in soluble amyloid-beta levels in the APP23 mouse model despite steady-state levels of amyloid-beta-producing proteins

Janssen, L., Keppens, C., Deyn, P. P. D., & Dam, D. V. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.10.027 · Cited by 11

Increase in the β‐Sheet Character of an Amyloidogenic Peptide upon Adsorption onto Gold and Silver Surfaces

Soltani, N., & Gholami, M. R. (2016) · ChemPhysChem · doi:10.1002/cphc.201601000 · Cited by 11

Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa

Fu, Z., Nostrand, W. E. V., & Smith, S. O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031225 · Cited by 11

Cytotoxic Intermediates in the Fibrillation Pathway: Aβ Oligomers in Alzheimer’s Disease as a Case Study

Klein, W. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_4 · Cited by 11

Protease Inhibitors and their Involvement in Neurological Disorders

Tizón, B., & Levy, E. (2007) · Springer eBooks · doi:10.1007/978-0-387-30379-6_20 · Cited by 11

Protein Folding, Nucleation Phenomena and Delayed Neurodegeneration in Alzheimer's Disease

Fox, N. C., Harvey, R. J., & Rossor, M. N. (1996) · Reviews in the Neurosciences · doi:10.1515/revneuro.1996.7.1.21 · Cited by 11

Human amylin mimicks amyloid β protein-induced reactive gliosis and inhibition of cellular redox activity in cultured astrocytes

Abe, K., Kato, M., & Saitō, H. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00595-7 · Cited by 11

Neuronal membrane conductance activated by amyloid β peptide: importance of peptide conformation

Li, W., Czilli, D. L., & Simmons, L. K. (1995) · Brain Research · doi:10.1016/0006-8993(95)00264-q · Cited by 11

Changes in expression of lymphocyte amyloid precursor protein mRNA isoforms in normal aging and Alzheimer's disease

Ebstein, R. P., Nemanov, L., Lubarski, G., Dano, M., Trevis, T., & Korczyn, A. D. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00227-j · Cited by 11

In vitro and in vivo models to unravel the potential roles of β/A4 in the pathogenesis of alzheimer's disease

Snow, A. D., & Malouf, A. T. (1993) · Hippocampus · doi:10.1002/hipo.1993.4500030729 · Cited by 11

Astroglial responses against Aβ initially occur in cerebral primary cortical cultures: species differences between rat and cynomolgus monkey

Kimura, N., Negishi, T., Ishii, Y., Kyuwa, S., & Yoshikawa, Y. (2004) · Neuroscience Research · doi:10.1016/j.neures.2004.03.010 · Cited by 10

Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies

Chen, W., Gamache, E., Richardson, D., Du, Z., & Wang, C. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.08.006 · Cited by 10

A rapid and sensitive method to determine tacrolimus in rat whole blood using liquid–liquid extraction with mild temperature ultrasonication and LC–MS/MS

Park, J. S., Cho, H. R., Kang, M. J., & Choi, Y. S. (2015) · Archives of Pharmacal Research · doi:10.1007/s12272-015-0681-9 · Cited by 10

Aggregation kinetics in the presence of brain lipids of Aβ(1–40) cleaved from a soluble fusion protein

Kael, M. A., Weber, D. K., Separovic, F., & Sani, M. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.03.005 · Cited by 10

Self-assembly of bioinspired and biologically functional materials

Pashuck, E. T., Seeman, N., & Macfarlane, R. J. (2020) · MRS Bulletin · doi:10.1557/mrs.2020.249 · Cited by 10

Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL

Mitchell, S. M., Graham, M. M., Liu, X., & Leonhardt, R. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-87259-y · Cited by 10

Effect of Piedmont mutation (L34V) on the structure, dynamics, and aggregation of Alzheimer’s Aβ40 peptide

Saini, R. K., Thakur, H., & Goyal, B. (2020) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2020.107571 · Cited by 10

Métabolisme du précurseur du peptide amyloïde et présénilines

Checler, F., da Costa, C. A., Dumanchin‐Njock, C., Lopez‐Perez, E., Marambaud, P., Paitel, E., Petit-Paitel, A., & Vincent, B. (2002) · médecine/sciences · doi:10.1051/medsci/20021867717 · Cited by 10

Metal Cations Defibrillize the Amyloid Beta-Protein Fibrils

Chauhan, V. P. S., Ray, I., Chauhan, A., Węgiel, J., & Wı́sniewski, H. M. (1997) · Neurochemical Research · doi:10.1023/a:1022079709085 · Cited by 10

Zinc and Alzheimer's Disease

Maggio, J. E., Esler, W. P., Stimson, E. R., Jennings, J. M., Ghilardi, J. R., & Mantyh, P. W. (1995) · Science · doi:10.1126/science.7604268 · Cited by 11

Beta-amyloid oligomers: recent developments

Borutaite, V., Morkuniene, R., & Valincius, G. (2011) · bmc · doi:10.1515/bmc.2011.019 · Cited by 9

Microbiota-Derived β-Amyloid-like Peptides Trigger Alzheimer’s Disease-Related Pathways in the SH-SY5Y Neural Cell Line

Blanco‐Míguez, A., Tamés-Caunedo, H., Ruas‐Madiedo, P., & Sánchez, B. (2021) · Nutrients · doi:10.3390/nu13113868 · Cited by 11

The detection methods currently available for protein aggregation in neurological diseases

Li, J., Zhou, C.-M., Jin, R.-L., Song, J.-H., Yang, K.-C., Li, Y., Tan, B., & Li, Y. (2024) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2024.102420 · Cited by 9

Insulin Mediates Lipopolysaccharide-Induced Inflammatory Responses and Oxidative Stress in BV2 Microglia

Huang, C.-C., Tsai, S., Liu, S., Yeh, M.-C., Hung, H., Lee, C.-W., Cheng, C., Hsu, P., & Kuo, Y.-M. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s481101 · Cited by 9

Molecular insights into the very early steps of Aβ1-42 pentameric protofibril disassembly by PGG: A molecular dynamics simulation study

Nie, R., Cai, S., Yu, B., Fan, W., Li, H., Tang, S., & Huo, Y. (2022) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2022.119638 · Cited by 9

Molecular insights into the structure destabilization effects of ECG and EC on the Aβ protofilament: An all-atom molecular dynamics simulation study

Nie, R., Zhang, S.-S., Yan, X.-K., Feng, K., Lao, Y.-J., & Bao, Y.-R. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127002 · Cited by 9

PrP106-126 and Aβ1-42 Peptides Induce BV-2 Microglia Chemotaxis and Proliferation

Tu, J., Yang, L., Zhou, X., Qi, K., Wang, J., Kouadir, M., Xu, L., Yin, X., & Zhao, D. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0140-3 · Cited by 9

Cereblon-mediated degradation of the amyloid precursor protein via the ubiquitin-proteasome pathway

Kurihara, T., Asahi, T., & Sawamura, N. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.078 · Cited by 9

In vitro neurotoxicity of amyloid β-peptide cross-linked by transglutaminase

Shinagawa, R., Masuda, S., Sasaki, R., Ikura, K., & Takahata, K. (1997) · Cytotechnology · doi:10.1023/a:1007999114779 · Cited by 9

Protocol for quantitative and qualitative analyses of the in vitro aggregation of synthetic β-amyloid

Chang, P., & Su, Y. (2000) · Brain Research Protocols · doi:10.1016/s1385-299x(00)00031-3 · Cited by 9

Wild‐type, Flemish, and Dutch amyloid‐β exhibit different cytotoxicities depending on Aβ40 to Aβ42 interaction time and concentration ratio

Shahnawaz, M., Sharoar, M. G., Shin, S. Y., & Park, I. (2013) · Journal of Peptide Science · doi:10.1002/psc.2531 · Cited by 9

Kohärente mehrdimensionale Schwingungsspektroskopie von Biomolekülen: Konzepte, Simulationen und Herausforderungen

Zhuang, W., Hayashi, T., & Mukamel, S. (2009) · Angewandte Chemie · doi:10.1002/ange.200802644 · Cited by 9

Inhibition of beta-amyloid precursor protein gene in SK-N-SH cells by piperlonguminine/dihydropiperlonguminine components separated from Chinese herbal medicine Futokadsura stem.

Xia, W. R., Zeng, J., Chen, L.-B., Jiang, A.-L., Xiang, L., Xu, J., Cui, X., & Han, E. (2007) · PubMed · Cited by 9

Oxygen-free radicals and amyloidosis in alzheimer's disease: Is there a connection?

Robakis, N. K. R. K., & Pappolla, M. A. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90077-9 · Cited by 9

High-level expression and in vitro mutagenesis of a fibrillogenic 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein

Gardella, J. E., Gorgone, G., Candela, L., Ghiso, J. A., Castaño, E. M., Frangione, B., & Gorevic, P. D. (1993) · Biochemical Journal · doi:10.1042/bj2940667 · Cited by 9

The immunoreactive profile at the N-terminal region of Aβ1–3/940 but not Aβ 1–42 changes with transition from monomer/dimer to further peptide aggregates

Kametani, F., Tanaka, K., Tokuda, T., & Allsop, D. (1995) · Brain Research · doi:10.1016/0006-8993(95)01195-1 · Cited by 9

Improved synthesis and purification of Alzheimer's Aβ 1–42 and analogs

Milton, S. C. F., Milton, R. C. D. L., Kates, S. A., & Glabe, C. G. (1999) · International Journal of Peptide Research and Therapeutics · doi:10.1007/bf02443630 · Cited by 9

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Stefansson, S., Knight, M., & Ahn, S. N. (2012) · Nanomaterials and Nanotechnology · doi:10.5772/54650 · Cited by 8

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(2011) · Asia-Pacific Biotech News · doi:10.1142/s021903031100053x · Cited by 8

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Wong, P. C., Borchelt, D., Lee, M. K., Pardo, C. A., Thinakaran, G., Martin, L. J., Sisodia, S. S., & Price, D. L. (1998) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4869-0_9 · Cited by 8

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