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

Barghorn, Stefan; Nimmrich, Volker; Striebinger, Andreas; Krantz, Carsten; Keller, Patrick; Janson, Bodo; Bahr, Michael; Schmidt, Martin; Bitner, Robert S.; Harlan, John; Barlow, Eve; Ebert, Ulrich; Hillen, Heinz

doi:10.1111/j.1471-4159.2005.03407.x

Cited by 559Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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

Barghorn, Stefan, Nimmrich, Volker, Striebinger, Andreas, Krantz, Carsten, Keller, Patrick, Janson, Bodo, Bahr, Michael, Schmidt, Martin +5 more·2005·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2005.03407.x

Open this paper in CoChat — free account

Abstract

Amyloid beta-peptide (Abeta)(1-42) oligomers have recently been discussed as intermediate toxic species in Alzheimer's disease (AD) pathology. Here we describe a new and highly stable Abeta(1-42) oligomer species which can easily be prepared in vitro and is present in the brains of patients with AD and Abeta(1-42)-overproducing transgenic mice. Physicochemical characterization reveals a pure, highly water-soluble globular 60-kDa oligomer which we named 'Abeta(1-42) globulomer'. Our data indicate that Abeta(1-42) globulomer is a persistent structural entity formed independently of the fibrillar aggregation pathway. It is a potent antigen in mice and rabbits eliciting generation of Abeta(1-42) globulomer-specific antibodies that do not cross-react with amyloid precursor protein, Abeta(1-40) and Abeta(1-42) monomers and Abeta fibrils. Abeta(1-42) globulomer binds specifically to dendritic processes of neurons but not glia in hippocampal cell cultures and completely blocks long-term potentiation in rat hippocampal slices. Our data suggest that Abeta(1-42) globulomer represents a basic pathogenic structural principle also present to a minor extent in previously described oligomer preparations and that its formation is an early pathological event in AD. Selective neutralization of the Abeta globulomer structure epitope is expected to have a high potential for treatment of AD.

Integrity signals

Registry

Crossref · 10.1111/j.1471-4159.2005.03407.x

Cites

41 of 41 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

In hippocampal slices, synthetic Aβ oligomers cause rapid LTP inhibition.
“In hippocampal slices, synthetic oligomers cause rapid LTP inhibition (Barghorn et al., 2005; Fa et al., 2010; Jurgensen et al., 2011; Lambert et al., 1998; Nimmrich et al., 2008; Rammes et al., 2011; Wang et al., 2002).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Barghorn et al., 2005

The Rat Brain in Stereotaxic Coordinates
Paxinos, G., & Watson, C. (1983) · Elsevier eBooks · doi:10.1016/c2009-0-63235-9 · Cited by 28,585 · see citing works
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Diffusible, nonfibrillar ligands derived from Aβ <sub>1–42</sub> 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 · see citing works
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052 · see citing works
High-Level Neuronal Expression of Aβ<sub>1–42</sub>in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856 · see citing works
Natively unfolded proteins: A point where biology waits for physics
Uversky, V. N. (2002) · Protein Science · doi:10.1110/ps.4210102 · Cited by 1,815 · see citing works
The Nature of the Arrestin·Receptor Complex Determines the Ultimate Fate of the Internalized Receptor
Pan, L., Gurevich, E. V., & Gurevich, V. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209532200 · Cited by 1,758 · see citing works
P <scp>ROTOFIBRILS</scp> , P <scp>ORES</scp> , F <scp>IBRILS, AND</scp> N <scp>EURODEGENERATION</scp> : Separating the Responsible Protein Aggregates from The Innocent Bystanders
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650 · see citing works
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530 · see citing works
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268 · see citing works
Clinical, pathological, and neurochemical changes in dementia: a subgroup with preserved mental status and numerous neocortical plaques
Katzman, R., Terry, R., DeTeresa, R., Brown, T., Davies, P., Fuld, P., Renbing, X., & Peck, A. (1988) · Annals of Neurology · doi:10.1002/ana.410230206 · Cited by 1,225 · see citing works
Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease
Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207 · see citing works
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works
Amyloid fibrillogenesis: themes and variations
Rochet, J., & Lansbury, P. T. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00049-4 · Cited by 1,095 · see citing works
Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061 · see citing works
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015 · see citing works
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954 · see citing works
Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer’s disease
Georganopoulou, D. G., Chang, L., Nam, J.-M., Thaxton, C. S., Mufson, E. J., Klein, W. L., & Mirkin, C. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409336102 · Cited by 835 · see citing works
On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.
Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., & Teplow, D. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1125 · Cited by 784 · see citing works
Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains
Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618 · see citing works
The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging
Wang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567 · see citing works
The Formation of Highly Soluble Oligomers of α-Synuclein Is Regulated by Fatty Acids and Enhanced in Parkinson's Disease
Sharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00024-2 · Cited by 562 · see citing works
Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527 · see citing works
Block of Long-Term Potentiation by Naturally Secreted and Synthetic Amyloid β-Peptide in Hippocampal Slices Is Mediated via Activation of the Kinases c-Jun N-Terminal Kinase, Cyclin-Dependent Kinase 5, and p38 Mitogen-Activated Protein Kinase as well as Metabotropic Glutamate Receptor Type 5
Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., & Anwyl, R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1633-03.2004 · Cited by 437 · see citing works
Two Types of Alzheimer's β-Amyloid (1–40) Peptide Membrane Interactions: Aggregation Preventing Transmembrane Anchoring Versus Accelerated Surface Fibril Formation
Bokvist, M., Lindström, F., Watts, A. G., & Gröbner, G. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.046 · Cited by 375 · see citing works
Aggregation of Secreted Amyloid β-Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture
Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydel, R. E., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9564 · Cited by 364 · see citing works
Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
Barghorn, S., & Mandelkow, E. (2002) · Biochemistry · doi:10.1021/bi026469j · Cited by 341 · see citing works
Self-citation
Membrane Disruption by Alzheimer β-Amyloid Peptides Mediated through Specific Binding to Either Phospholipids or Gangliosides
McLaurin, J., & Chakrabartty, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26482 · Cited by 333 · see citing works
Amyloid β‐peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease
Verdier, Y., Zarándi, M., & Penke, B. (2004) · Journal of Peptide Science · doi:10.1002/psc.573 · Cited by 262 · see citing works
Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro
Chirita, C. N., Necula, M., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301663200 · Cited by 244 · see citing works
Truncated beta‐amyloid peptide species in pre‐clinical Alzheimer's disease as new targets for the vaccination approach
Sergeant, N., Bombois, S., Ghestem, A., Drobecq, H., Kostanjevečki, V., Missiaen, C., Wattez, A., David, J. P., Vanmechelen, E., Sergheraert, C., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01818.x · Cited by 213 · see citing works
Rapid Anionic Micelle-mediated α-Synuclein Fibrillization in Vitro
Necula, M., Chirita, C. N., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308231200 · Cited by 211 · see citing works
Adult-derived neural precursors transplanted into multiple regions in the adult brain
Herrera, D. G., García‐Verdugo, J. M., & Álvarez-Buylla, A. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 204 · see citing works
Modulation of Alzheimer-like synaptic and cholinergic deficits in transgenic mice by human apolipoprotein E depends on isoform, aging, and overexpression of amyloid β peptides but not on plaque formation
Buttini, M., Yu, G.-Q., Shockley, K., Huang, Y., Jones, B., Masliah, E., Mallory, M., Yeo, T., Longo, F. M., & Mucke, L. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-24-10539.2002 · Cited by 183 · cited 1× · see citing works
“Further evidence for a key role of soluble Ab in AD pathogenesis came from reports that a cognitive impairment develops well before deposition of insoluble Ab in mice transgenic for human APP (Hsia et al. 1999; Mucke et al. 2000; Buttini et al. 2002).”
Background
Low Concentrations of Sodium Dodecyl Sulfate Induce the Extension of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH
Yamamoto, S., Hasegawa, K., Yamaguchi, I., Tsutsumi, S., Kardos, J., Goto, Y., Gejyo, F., & Naiki, H. (2004) · Biochemistry · doi:10.1021/bi049262u · Cited by 181 · see citing works
Conformation-dependent antibodies target diseases of protein misfolding
Glabe, C. C. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.08.009 · Cited by 154 · see citing works
Denatured collapsed states in protein folding: Example of apomyoglobin
Tcherkasskaya, O., & Uversky, V. N. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1089 · Cited by 107 · see citing works
Fleecy Amyloid Deposits in the Internal Layers of the Human Entorhinal Cortex are Comprised of N-terminal Truncated Fragments of Aβ
Thal, D. R., Sassin, I., Schultz, C., Haass, C., Braak, E., & Braak, H. (1999) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199902000-00010 · Cited by 77 · see citing works

Flagged first, then by citations

Sorted by citations

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938 · see citing works
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971 · see citing works
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870 · see citing works
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783 · see citing works
Effects of secreted oligomers of amyloid β‐protein on hippocampal synaptic plasticity: a potent role for trimers
Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., & Selkoe, D. J. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103754 · Cited by 619 · see citing works
Alzheimer's disease, β‐amyloid, glutamate, NMDA receptors and memantine – searching for the connections
Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500 · see citing works
The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease
Ferreira, S. T., & Klein, W. L. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.08.003 · Cited by 442 · see citing works
Characterization of the microglial phenotype under specific pro-inflammatory and anti-inflammatory conditions: Effects of oligomeric and fibrillar amyloid-β
Michelucci, A., Heurtaux, T., Grandbarbe, L., Morga, E., & Heuschling, P. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.02.003 · Cited by 411 · see citing works
Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering
Sandberg, A., Luheshi, L. M., Söllvander, S., Pereira de Barros, T., Macao, B., Knowles, T. P. J., Biverstål, H., Lendel, C., Ekholm-Petterson, F., Dubnovitsky, A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001740107 · Cited by 358 · see citing works
Soluble Aβ oligomer production and toxicity
Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356 · see citing works
Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
Tomic, J. L., Pensalfini, A., Head, E., & Glabe, C. G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.024 · Cited by 336 · see citing works
Sensitive ELISA detection of amyloid‐β protofibrils in biological samples
Englund, H., Sehlin, D., Johansson, A., Nilsson, L. N. G., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04759.x · Cited by 292 · see citing works
Amyloid β-protein oligomers and Alzheimer’s disease
Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt226 · Cited by 276 · see citing works
High‐molecular‐weight β‐amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients
Fukumoto, H., Tokuda, T., Kasai, T., Ishigami, N., Hidaka, H., Kondo, M., Allsop, D., & Nakagawa, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150359 · Cited by 264 · see citing works
Intracellular accumulation of amyloid-beta – a predictor for synaptic dysfunction and neuron loss in Alzheimer’s disease
Bayer (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00008 · Cited by 252 · see citing works
Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory
Cournia, Z., Allen, T. W., Andricioaei, I., Antonny, B., Baum, D., Brannigan, G., Buchete, N.-V., Deckman, J. T., Delemotte, L., del Val, C., et al. (2015) · The Journal of Membrane Biology · doi:10.1007/s00232-015-9802-0 · Cited by 235 · see citing works
Increased Accumulation of Intraneuronal Amyloid β in HIV-Infected Patients
HNRC, Achim, C. L., Adame, A., Dumaop, W., Everall, I. P., & Masliah, E. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9152-8 · Cited by 205 · see citing works
Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer’s disease immunotherapeutics
Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190 · see citing works
Therapeutic significance of NR2B-containing NMDA receptors and mGluR5 metabotropic glutamate receptors in mediating the synaptotoxic effects of β-amyloid oligomers on long-term potentiation (LTP) in murine hippocampal slices
Rammes, G., Hasenjäger, A., Sroka-Saidi, K., Deussing, J. M., & Parsons, C. G. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.051 · Cited by 163 · see citing works
Alzheimer's disease amyloid β-protein and synaptic function
Ondrejcak, T., Klyubin, I., Hu, N.-W., Barry, A. E., Cullen, W. K., & Rowan, M. J. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8091-0 · Cited by 146 · see citing works
Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models
Kostylev, M. A., Kaufman, A. C., Nygaard, H. B., Patel, P., Haas, L. T., Gunther, E. C., Vortmeyer, A., & Strittmatter, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.643577 · Cited by 133 · see citing works
Alzheimer’s disease as oligomeropathy
Ono, K. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.010 · Cited by 129 · see citing works
Generation and Therapeutic Efficacy of Highly Oligomer-Specific β-Amyloid Antibodies
Hillen, H., Barghorn, S., Striebinger, A., Labkovsky, B., Müller, R., Nimmrich, V., Nolte, M. W., Perez-Cruz, C., van der Auwera, I., van Leuven, F., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5721-09.2010 · Cited by 113 · see citing works
Self-citation
Investigating How Peptide Length and a Pathogenic Mutation Modify the Structural Ensemble of Amyloid Beta Monomer
Lin, Y.-S., Bowman, G. R., Beauchamp, K. A., & Pande, V. S. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.002 · Cited by 111 · see citing works
Assembly and Interrogation of Alzheimer’s Disease Genetic Networks Reveal Novel Regulators of Progression
Aubry, S., Shin, W., Crary, J. F., Lefort, R., Qureshi, Y. H., Lefebvre, C., Califano, A., & Shelanski, M. L. (2015) · PLOS ONE · doi:10.1371/journal.pone.0120352 · Cited by 106 · see citing works
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108 · see citing works
Aβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015725 · Cited by 105 · see citing works
“In vitro oligomers composed of ,12 Ab42 monomers were prepared as described [23] and diluted at varying concentrations into normal CSF before being subjected to the MPA (Figure 3).”
Method
Molecular basis of β-amyloid oligomer recognition with a conformational antibody fragment
Morgado, I., Wieligmann, K., Bereza, M., Rönicke, R., Meinhardt, K., Annamalai, K., Baumann, M., Wacker, J., Hortschansky, P., Malešević, M., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206433109 · Cited by 80 · see citing works
Biophysical analyses of synthetic amyloid-β(1–42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-β oligomers
Moore, B. D., Rangachari, V., Tay, W. M., Milkovic, N. M., & Rosenberry, T. L. (2009) · Biochemistry · doi:10.1021/bi901571t · Cited by 43 · see citing works
Efficacy of cyclin dependent kinase 4 inhibitors as potent neuroprotective agents against insults relevant to alzheimer's disease
Sanphui, P., Pramanik, S. K., Chatterjee, N., Moorthi, P., Banerji, B., & Biswas, S. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078842 · Cited by 38 · see citing works
Targeting Generation of Antibodies Specific to Conformational Epitopes of Amyloid &#946;-Derived Neurotoxins
Lambert, M., Velasco, P., Viola, K., & Klein, W. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601876 · Cited by 29 · see citing works
A chemical screening approach reveals that indole fluorescence is quenched by pre-fibrillar but not fibrillar amyloid-β
Reinke, A. A., Seh, H. Y., & Gestwicki, J. E. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.07.082 · Cited by 26 · see citing works

Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils
Fu, X., Korenaga, T., Fu, L., Xing, Y., Guo, Z., Matsushita, T., Hosokawa, M., Naiki, H., Baba, S., Kawata, Y., et al. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00295-9 · Cited by 44 · see citing works
Induction of Murine AA Amyloidosis by Various Homogeneous Amyloid Fibrils and Amyloid‐like Synthetic Peptides
Liu, Y., Cui, D., Hoshii, Y., et al. (2007) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2007.02005.x · Cited by 37 · see citing works
Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Willbold, D., Strodel, B., Schroeder, G. F., Hoyer, W., & Heise, H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00196 · Cited by 222 · see citing works
Nucleobindin 1 Caps Human Islet Amyloid Polypeptide Protofibrils to Prevent Amyloid Fibril Formation
Gupta, R., Kapoor, N., Raleigh, D. P., & Sakmar, T. P. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.04.017 · Cited by 24 · see citing works
Role of tau in the polymerization of peptides from β-amyloid precursor protein
Caputo, C. B., Sygowski, L. A., Scott, C. W., & Sobel, I. R. E. (1992) · Brain Research · doi:10.1016/0006-8993(92)91478-w · Cited by 23 · see citing works

Authors: Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., Barlow, E., Ebert, U., & Hillen, H.
Affiliations: Abbott (Germany) (DE)
Abbott (United States) (US)
ORCID: Barghorn, Stefan
Schmidt, Martin
Harlan, John
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2005-08-31
Volume: 95
Issue: 3
Pages: 834-847
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2005.03407.x
OpenAlex: W2126958454
Cited by: 559
References: 41
Citations by year: 2026: 7 · 2025: 14 · 2024: 12 · 2023: 19 · 2022: 19 · 2021: 21 · 2020: 18 · 2019: 21 · 2018: 25 · 2017: 23 · 2016: 24 · 2015: 19 · 2014: 29 · 2013: 40 · 2012: 40
FWCI: 17.78
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid beta peptide 1-42, amyloid-beta oligomers, Alzheimer's disease, antigenic determinants, long-term potentiation, hippocampus, transgenic mice, neurotoxicity
MeSH terms: Alzheimer Disease, Animals, Antibodies, Antibody Specificity, Epitopes, Cells, Cultured, Fatty Acids, Hippocampus, Humans, Male, Mice, Transgenic, Neurons, Peptide Fragments, Protein Conformation, Rabbits, Solubility, Water, Amyloid beta-Peptides, Rats, Sprague-Dawley, Long-Term Potentiation, Mice, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks