Pyroglutamate Formation Influences Solubility and Amyloidogenicity of Amyloid Peptides

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · see citing works

A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR

Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., & Tycko, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262663499 · Cited by 1,847 · see citing works

Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)

Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774 · see citing works

Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen

Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 684 · see citing works

Dominant and differential deposition of distinct β-amyloid peptide species, AβN3(pE), in senile plaques

Saido, T. C., Iwatsubo, T., Mann, D. M. A., Shimada, H., Ihara, Y., & Kawashima, S. (1995) · Neuron · doi:10.1016/0896-6273(95)90301-1 · Cited by 587 · see citing works

Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice

McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565 · see citing works

A stop-codon mutation in the BRI gene associated with familial British dementia

Vidal, R., Frangione, B., Rostagno, A., Mead, S., Révész, T., Plant, G., & Ghiso, J. (1999) · Nature · doi:10.1038/21637 · Cited by 466 · see citing works

A Recessive Mutation in the APP Gene with Dominant-Negative Effect on Amyloidogenesis

Fede, G. D., Catania, M., Morbin, M., Rossi, G., Suardi, S., Mazzoleni, G., Merlin, M., Gıovagnolı, A. R., Prioni, S., Erbetta, A., et al. (2009) · Science · doi:10.1126/science.1168979 · Cited by 415 · see citing works

Glutaminyl cyclase inhibition attenuates pyroglutamate Aβ and Alzheimer's disease–like pathology

Schilling, S., Zeitschel, U., Hoffmann, T., Heiser, U., Francke, M., Kehlen, A., Holzer, M., Hutter-Paier, B., Prokesch, M., Windisch, M., et al. (2008) · Nature Medicine · doi:10.1038/nm.1872 · Cited by 357 · see citing works

Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance

Balbach, J. J., Petkova, A. T., Oyler, N. A., Antzutkin, O. N., Gordon, D. J., Meredith, S. C., & Tycko, R. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75244-2 · Cited by 312 · see citing works

Amino-terminal Deletions Enhance Aggregation of β-Amyloid Peptides in Vitro

Pike, C. J., Overman, M. J., & Cotman, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23895 · Cited by 302 · see citing works

A decamer duplication in the 3′ region of the <i>BRI</i> gene originates an amyloid peptide that is associated with dementia in a Danish kindred

Vidal, R., Révész, T., Rostagno, A., Kim, E., Holton, J. L., Bek, T., Bojsen-Møller, M., Braendgaard, H., Plant, G., Ghiso, J., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.080076097 · Cited by 300 · see citing works

Life on the edge: a link between gene expression levels and aggregation rates of human proteins

Tartaglia, G. G., Pechmann, S., Dobson, C. M., & Vendruscolo, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.03.005 · Cited by 289 · see citing works

Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain

Saido, T. C., Yamao-Harigaya, W., Iwatsubo, T., & Kawashima, S. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12970-0 · Cited by 270 · see citing works

The aggregation kinetics of Alzheimer's β‐amyloid peptide is controlled by stochastic nucleation

Hortschansky, P., Schroeckh, V., Christopeit, T., Zandomeneghi, G., & Fändrich, M. (2005) · Protein Science · doi:10.1110/ps.041266605 · Cited by 266 · see citing works

On the Seeding and Oligomerization of pGlu-Amyloid Peptides (<i>in vitro</i>)

Schilling, S., Lauber, T., Schaupp, M., Manhart, S., Scheel, E., Böhm, G., & Demuth, H.-U. (2006) · Biochemistry · doi:10.1021/bi0612667 · Cited by 254 · see citing works

Full-length amyloid-beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques.

Iwatsubo, T., Saido, T. C., Mann, D. M. A., Lee, V. M.-Y., & Trojanowski, J. Q. (1996) · Europe PMC (PubMed Central) · Cited by 248 · see citing works

The Aβ 3-Pyroglutamyl and 11-Pyroglutamyl Peptides Found in Senile Plaque Have Greater β-Sheet Forming and Aggregation Propensities in Vitro than Full-Length Aβ

He, W., & Barrow, C. J. (1999) · Biochemistry · doi:10.1021/bi990563r · Cited by 216 · see citing works

Pyroglutamate‐modified amyloid β‐peptides – AβN3(pE) – strongly affect cultured neuron and astrocyte survival

Russo, C., Violani, E., Salis, S., Venezia, V., Dolcini, V., Damonte, G., Benatti, U., D’Arrigo, C., Patrone, E., Carlo, P., et al. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01107.x · Cited by 201 · see citing works

Structural Features of the Aβ Amyloid Fibril Elucidated by Limited Proteolysis

Kheterpal, I., Williams, A. D., Murphy, C. L., Bledsoe, B., & Wetzel, R. B. (2001) · Biochemistry · doi:10.1021/bi010805z · Cited by 199 · see citing works

β-Amyloid Is Different in Normal Aging and in Alzheimer Disease

Piccini, A., Russo, C., Gliozzi, A., Relini, A., Vitali, A., Borghi, R., Giliberto, L., Armirotti, A., D’Arrigo, C., Bachi, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501694200 · Cited by 193 · see citing works

High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain

Güntert, A., Döbeli, H., & Bohrmann, B. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.08.027 · Cited by 180 · see citing works

Presenilin-1 mutations in Alzheimer's disease

Russo, C., Schettini, G., Saido, T. C., Hulette, C. M., Lippa, C. F., Lannfelt, L., Ghetti, B. F., Gambetti, P., Tabaton, M., & Teller, J. K. (2000) · Nature · doi:10.1038/35014735 · Cited by 156 · see citing works

Amino-Terminally Truncated Aβ Peptide Species Are the Main Component of Cotton Wool Plaques

Miravalle, L., Calero, M., Takao, M., Roher, A. E., Ghetti, B. F., & Vidal, R. (2005) · Biochemistry · doi:10.1021/bi0508237 · Cited by 140 · see citing works

Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution

Schilling, S., Wasternack, C., & Demuth, H. (2008) · Biological Chemistry · doi:10.1515/bc.2008.111 · Cited by 102 · see citing works

Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells

Cynis, H., Schilling, S., Bodnár, M., Hoffmann, T., Heiser, U. F., Saido, T. C., & Demuth, H. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.08.003 · Cited by 85 · see citing works

Systemic Amyloid Deposits in Familial British Dementia*

Ghiso, J., Holton, J., Miravalle, L., Calero, M., Lashley, T., Vidal, R., Houlden, H., Wood, N., Neubert, T., Rostagno, A., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105956200 · Cited by 80 · see citing works

Amino‐truncated amyloid β‐peptide (Aβ5‐40/42) produced from caspase‐cleaved amyloid precursor protein is deposited in Alzheimer’s disease brain

Takeda, K., Araki, W., Akiyama, H., & Tabira, T. (2004) · The FASEB Journal · doi:10.1096/fj.03-1070fje · Cited by 53 · see citing works

Contribution of Structural Peculiarities of Onconase to Its High Stability and Folding Kinetics

Arnold, U., Schulenburg, C., Schmidt, D., & Ulbrich‐Hofmann, R. (2006) · Biochemistry · doi:10.1021/bi0525223 · Cited by 37 · see citing works

Increased Generation of Alternatively Cleaved β‐Amyloid Peptides in Cells Expressing Mutants of the Amyloid Precursor Protein Defective in Endocytosis

Cescato, R., Dumermuth, E., Spiess, M., et al. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.741131.x · Cited by 36 · see citing works

The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens

Liao, Y. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg746 · Cited by 35 · see citing works

Chromosome 13 dementia syndromes as models of neurodegeneration

Ghiso, J. A., Révész, T., Holton, J. L., Rostagno, A. A., Lashley, T., Houlden, H., Gibb, G., Anderton, B. H., Bek, T., Bojsen‐Møller, M., et al. (2001) · Amyloid · doi:10.3109/13506120108993826 · Cited by 26 · see citing works

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

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

A Plaque-Specific Antibody Clears Existing β-amyloid Plaques in Alzheimer's Disease Mice

DeMattos, R. B., Lu, J., Tang, Y., Racke, M. M., DeLong, C. A., Tzaferis, J. A., Hole, J. T., Forster, B. M., McDonnell, P. C., Liu, F., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.10.029 · Cited by 442 · see citing works

Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease

Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372 · see citing works

Amyloidogenic amyloid-β-peptide variants induce microbial agglutination and exert antimicrobial activity

Spitzer, P., Condic, M., Herrmann, M., Oberstein, T. J., Scharin-Mehlmann, M., Gilbert, D. F., Friedrich, O., Grömer, T., Kornhuber, J., Lang, R., et al. (2016) · Scientific Reports · doi:10.1038/srep32228 · Cited by 128 · see citing works

Selective Hippocampal Neurodegeneration in Transgenic Mice Expressing Small Amounts of Truncated Aβ Is Induced by Pyroglutamate–Aβ Formation

Alexandru, A., Jagla, W., Graubner, S., Becker, A., Bäuscher, C., Kohlmann, S., Sedlmeier, R., Raber, K. A., Cynis, H., Rönicke, R., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.1794-11.2011 · Cited by 102 · see citing works

Intracellular Amyloid-β Accumulation in Calcium-Binding Protein-Deficient Neurons Leads to Amyloid-β Plaque Formation in Animal Model of Alzheimer's Disease

Moon, M., Hong, H.-S., Nam, D. W., Baik, S. H., Song, H., Kook, S.-Y., Kim, Y. S., Lee, J., & Mook-Jung, I. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-111778 · Cited by 60 · see citing works

Comparative pathobiology of β-amyloid and the unique susceptibility of humans to Alzheimer's disease

Rosen, R. F., Tomidokoro, Y., Farberg, A. S., Dooyema, J., Ciliax, B., Preuss, T. M., Neubert, T. A., Ghiso, J. A., LeVine, H., & Walker, L. C. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.04.019 · Cited by 46 · see citing works

Transgenic Expression of Intraneuronal Aβ ₄₂ But Not Aβ ₄₀ Leads to Cellular Aβ Lesions, Degeneration, and Functional Impairment without Typical Alzheimer's Disease Pathology

Abramowski, D., Rabe, S., Upadhaya, A. R., Reichwald, J., Danner, S., Staab, D., Capetillo-Zarate, E., Yamaguchi, H., Saido, T. C., Wiederhold, K.-H., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4586-11.2012 · Cited by 41 · see citing works

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Susquehanna Chorale Spring Concert "Roots and Wings"

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A GEOMETRIC MEAN IN THE FURUTA INEQUALITY

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Darstellung perhalogenierter Dimethyldisulfane durch photochemische Reaktion von CSF2 und CSFCI mit Sulfenylbromiden bzw. ‐chloriden

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