On the Seeding and Oligomerization of pGlu-Amyloid Peptides (in vitro)

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

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599 · see citing works

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 · 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

An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp ₇₁₇ ) Mutants

Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471 · see citing works

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452 · 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

Structure‐Activity Analyses of β‐Amyloid Peptides: Contributions of the β25–35 Region to Aggregation and Neurotoxicity

Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699 · 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

Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain

Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7013 · Cited by 676 · 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 Portrait of Alzheimer Secretases--New Features and Familiar Faces

Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493 · see citing works

Prolines and Aamyloidogenicity in Fragments of the Alzheimer's Peptide .beta./A4

Wood, S. J., Wetzel, R. B., Martin, J. D., & Hurle, M. R. (1995) · Biochemistry · doi:10.1021/bi00003a003 · Cited by 313 · 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

[20] Kinetic analysis of amyloid fibril formation

Naiki, H., & Gejyo, F. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09022-9 · Cited by 287 · 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

Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides.

Fischer, W. H., & Spiess, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.11.3628 · Cited by 261 · 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

Aβ40-Lactam(D23/K28) Models a Conformation Highly Favorable for Nucleation of Amyloid

Sciarretta, K. L., Gordon, D. J., Petkova, A. T., Tycko, R., & Meredith, S. C. (2005) · Biochemistry · doi:10.1021/bi0474867 · Cited by 245 · 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

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

Amyloid β Protein Starting Pyroglutamate at Position 3 Is a Major Component of the Amyloid Deposits in the Alzheimer's Disease Brain

Harigaya, Y., Saido, T. C., Eckman, C. B., Prada, C.-M., Shoji, M., & Younkin, S. G. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3490 · Cited by 202 · 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

An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes.

Busby, W. H., Quackenbush, G. E., Humm, J. H., Youngblood, W. W., & Kizer, J. S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47446-7 · Cited by 193 · 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

Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions

Schilling, S., Hoffmann, T., Manhart, S., Hoffmann, M., & Demuth, H. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00300-x · Cited by 172 · 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

Stereoselective Interactions of Peptide Inhibitors with the β-Amyloid Peptide

Chalifour, R. J., McLaughlin, R. W., Lavoie, L., Morissette, C., Tremblay, N., Boulé, M., Sarazin, P., Stéa, D., Lacombe, D., Tremblay, P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212694200 · 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

Heterogeneity of water‐soluble amyloid β‐peptide in Alzheimer's disease and Down's syndrome brains

Russo, C., Saido, T. C., DeBusk, L. M., Tabaton, M., Gambetti, P. L., & Teller, J. K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00564-4 · Cited by 122 · see citing works

The Solvent Protection of Alzheimer Amyloid-β-(1–42) Fibrils as Determined by Solution NMR Spectroscopy

Olofsson, A., Sauer-Eriksson, A. E., & Öhman, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508962200 · Cited by 121 · 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

The increased activity of BACE1 correlates with oxidative stress in Alzheimer's disease

Borghi, R., Patriarca, S., Traverso, N., Piccini, A., Storace, D., Garuti, A., Cirmena, G., Odetti, P. R., & Tabaton, M. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.05.004 · Cited by 82 · see citing works

Quantification of Modified Amyloid β Peptides in Alzheimer Disease and Down Syndrome Brains

Hosoda, R., Saido, T. C., Otvos, L., Arai, T., Mann, D. M. A., Lee, V. M.-Y., Trojanowski, J. Q., & Iwatsubo, T. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199811000-00012 · Cited by 79 · see citing works

Identification of Amino-Terminally and Phosphotyrosine-Modified Carboxy-Terminal Fragments of the Amyloid Precursor Protein in Alzheimer's Disease and Down's Syndrome Brain

Russo, C., Salis, S., Dolcini, V., Venezia, V., Song, X., Teller, J. K., & Schettini, G. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0357 · Cited by 75 · see citing works

Familial Danish Dementia

Tomidokoro, Y., Lashley, T., Rostagno, A., Neubert, T. A., Bojsen-Møller, M., Braendgaard, H., Plant, G., Holton, J., Frangione, B., Révész, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504038200 · Cited by 68 · see citing works

Commentary: Aβ N- Terminal Isoforms: Critical contributors in the course of AD pathophysiology

Tekirian, T. L. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3209 · Cited by 28 · see citing works

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 881 · see citing works

Motor deficits, neuron loss, and reduced anxiety coinciding with axonal degeneration and intraneuronal Aβ aggregation in the 5XFAD mouse model of Alzheimer's disease.

Jawhar, S., Trawicka, A., Jenneckens, C., Bayer, T. A., & Wirths, O. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.05.027 · Cited by 623 · 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

Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β

Nussbaum, J. M., Schilling, S., Cynis, H., Silva, A., Swanson, E., Wangsanut, T., Tayler, K., Wiltgen, B., Hatami, A., Rönicke, R., et al. (2012) · Nature · doi:10.1038/nature11060 · Cited by 427 · 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

Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease

Thal, D. R., Walter, J., Saido, T. C., & Fändrich, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1375-y · Cited by 319 · see citing works

Longitudinal, Quantitative Assessment of Amyloid, Neuroinflammation, and Anti-Amyloid Treatment in a Living Mouse Model of Alzheimer's Disease Enabled by Positron Emission Tomography

Maeda, J., Ji, B., Irie, T., Tomiyama, T., Maruyama, M., Okauchi, T., Staufenbiel, M., Iwata, N., Ono, M., Saido, T. C., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0673-07.2007 · Cited by 300 · see citing works

Aβ deposits in older non-demented individuals with cognitive decline are indicative of preclinical Alzheimer's disease

Villemagne, V. L., Pike, K. E., Darby, D., Maruff, P. T., Savage, G. R., Ng, S., Ackermann, U., Cowie, T., Currie, J. N., Chan, S. G., et al. (2008) · Neuropsychologia · doi:10.1016/j.neuropsychologia.2008.02.008 · Cited by 291 · see citing works

Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease

Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 288 · see citing works

Microglia convert aggregated amyloid-β into neurotoxic forms through the shedding of microvesicles

Joshi, P., Turola, E., Ruiz, A., Bergami, A., Libera, D. D., Benussi, L., Giussani, P., Magnani, G., Comı, G., Legname, G., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.180 · Cited by 274 · see citing works

The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes

Nhan, H. S., Chiang, K., & Koo, E. H. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1347-2 · Cited by 256 · see citing works

Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors

Siklos, M. I., BenAissa, M., & Thatcher, G. R. J. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.08.001 · Cited by 248 · see citing works

Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities

Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235 · see citing works

Pyroglutamate Formation Influences Solubility and Amyloidogenicity of Amyloid Peptides

Schlenzig, D., Manhart, S., Cinar, Y., Kleinschmidt, M., Hause, G., Willbold, D., Funke, S. A., Schilling, S., & Demuth, H.-U. (2009) · Biochemistry · doi:10.1021/bi900818a · Cited by 228 · see citing works

Near-infrared fluorescence molecular imaging of amyloid beta species and monitoring therapy in animal models of Alzheimer’s disease

Zhang, X., Tian, Y., Zhang, C. M., Tian, X., Ross, A., Moir, R. D., Sun, H., Tanzi, R. E., Moore, A. V., & Ran, C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505420112 · Cited by 227 · see citing works

Pyroglutamate Amyloid-β (Aβ): A Hatchet Man in Alzheimer Disease

Jawhar, S., Wirths, O., & Bayer, T. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.288308 · Cited by 220 · see citing works

Dendritic Spine Pathology in Neurodegenerative Diseases

Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201 · see citing works

Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimer's disease

Britschgi, M., Olin, C. E., Johns, H. T., Takeda-Uchimura, Y., LeMieux, M. C., Rufibach, K., Rajadas, J., Zhang, H., Tomooka, B., Robinson, W. H., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904866106 · Cited by 201 · see citing works

Immunotherapy for Alzheimer’s disease: hoops and hurdles

Lemere, C. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-36 · Cited by 196 · see citing works

Phosphorylation of amyloid beta (Aβ) peptides – A trigger for formation of toxic aggregates in Alzheimer's disease

Kumar, S., & Walter, J. (2011) · Aging · doi:10.18632/aging.100362 · Cited by 181 · see citing works

Actin dynamics and cofilin‐actin rods in alzheimer disease

Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181 · see citing works

Effects of in vivo conditions on amyloid aggregation

Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 179 · see citing works

Transgenic mouse models of alzheimer disease: Developing a better model as a tool for therapeutic interventions.

Kitazawa, M., Medeiros, R., & M. LaFerla, F. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315786 · Cited by 178 · see citing works

Intraneuronal pyroglutamate-Abeta 3–42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model

Wirths, O., Breyhan, H., Cynis, H., Schilling, S., Demuth, H.-U., & Bayer, T. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0557-5 · Cited by 174 · see citing works

A Greek Tragedy: The Growing Complexity of Alzheimer Amyloid Precursor Protein Proteolysis *

Andrew, R., Kellett, K., Thinakaran, G., & Hooper, N. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.746032 · Cited by 156 · see citing works

Cathepsin B in neurodegeneration of Alzheimer's disease, traumatic brain injury, and related brain disorders

HOOK, V. Y. H., Yoon, M. C., Mosier, C., Ito, G., Podvin, S., Head, B. P., Rissman, R. A., O’Donoghue, A. J., & Hook, G. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140428 · Cited by 170 · see citing works

Focusing the amyloid cascade hypothesis on N-truncated Abeta peptides as drug targets against Alzheimer’s disease

Bayer, T. A., & Wirths, O. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1287-x · Cited by 168 · see citing works

Alanine-2 Carbonyl is an Oxygen Ligand in Cu 2+ Coordination of Alzheimer’s Disease Amyloid-β Peptide − Relevance to N-Terminally Truncated Forms

Drew, S. C., Masters, C. L., & Barnham, K. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903669a · Cited by 166 · see citing works

Do Post-Translational Modifications Influence Protein Aggregation in Neurodegenerative Diseases: A Systematic Review

Schaffert, L.-N., & Carter, W. G. (2020) · Brain Sciences · doi:10.3390/brainsci10040232 · Cited by 165 · see citing works

Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 2: Dependence of Cu(II) binding sites with Aβ sequences

Hureau, C., & Dorlet, P. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.034 · Cited by 148 · see citing works

Pyroglutamate-3 Amyloid-β Deposition in the Brains of Humans, Non-Human Primates, Canines, and Alzheimer Disease–Like Transgenic Mouse Models

Frost, J. L., Le, K. X., Cynis, H., Ekpo, E., Kleinschmidt, M., Palmour, R. M., Ervin, F. R., Snigdha, S., Cotman, C. W., Saido, T. C., et al. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.05.005 · Cited by 132 · see citing works

The Caenorhabditis elegans Aβ1–42 Model of Alzheimer Disease Predominantly Expresses Aβ3–42

McColl, G., Roberts, B. R., Gunn, A. P., Perez, K. A., Tew, D. J., Masters, C. L., Barnham, K. J., Cherny, R. A., & Bush, A. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.028514 · Cited by 131 · see citing works

QUINT: Workflow for Quantification and Spatial Analysis of Features in Histological Images From Rodent Brain

Yates, S. C., Groeneboom, N. E., Coello, C. S., Lichtenthaler, S. F., Kuhn, P., Demuth, H.-U., Hartlage‐Rübsamen, M., Roßner, S., Leergaard, T. B., Kreshuk, A., et al. (2019) · Frontiers in Neuroinformatics · doi:10.3389/fninf.2019.00075 · Cited by 130 · 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

APP/Aβ structural diversity and Alzheimer's disease pathogenesis

Roher, A. E., Kokjohn, T. A., Clarke, S. G., Sierks, M. R., Maarouf, C. L., Serrano, G. E., Sabbagh, M., & Beach, T. G. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.007 · Cited by 121 · see citing works

Amyloidogenic Processing of Amyloid Precursor Protein: Evidence of a Pivotal Role of Glutaminyl Cyclase in Generation of Pyroglutamate-Modified Amyloid-β

Cynis, H., Scheel, E., Saido, T. C., Schilling, S., & Demuth, H. (2008) · Biochemistry · doi:10.1021/bi800250p · Cited by 117 · see citing works

Are N- and C-terminally truncated Aβ species key pathological triggers in Alzheimer's disease?

Dunys, J., Valverde, A., & Checler, F. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.r118.003999 · Cited by 71 · see citing works

Glutaminyl Cyclase in Human Cortex: Correlation with (pGlu)-Amyloid-β Load and Cognitive Decline in Alzheimer's Disease

Morawski, M., Schilling, S., Kreuzberger, M., Waniek, A., Jäger, C., Koch, B. M., Cynis, H., Kehlen, A., Arendt, T., Hartlage‐Rübsamen, M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131535 · Cited by 114 · see citing works

Insights into Alzheimer disease pathogenesis from studies in transgenic animal models

Schaeffer, E. L., Figueiró, M., & Gattaz, W. F. (2011) · Clinics · doi:10.1590/s1807-59322011001300006 · Cited by 114 · see citing works

Overlapping profiles of Aβ peptides in the Alzheimer's disease and pathological aging brains

Moore, B. D., Chakrabarty, P., Levites, Y., Kukar, T. L., Baine, A.-M. T., Moroni, T., Ladd, T. B., Das, P., Dickson, D. W., & Golde, T. E. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt121 · Cited by 112 · see citing works

Porphyromonas gingivalis Infection Induces Amyloid-β Accumulation in Monocytes/Macrophages

Nie, R., Wu, Z., Ni, J., Zeng, F., Yu, W., Zhang, Y., Kadowaki, T., Kashiwazaki, H., Teeling, J. L., & Zhou, Y. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190298 · Cited by 112 · see citing works

Safety, tolerability and immunogenicity of an active anti-Aβ40 vaccine (ABvac40) in patients with Alzheimer’s disease: a randomised, double-blind, placebo-controlled, phase I trial

Lacosta, A.-M., Pascual-Lucas, M., Pesini, P., Casabona, D., Pérez-Grijalba, V., Marcos-Campos, I., Sarasa, L., Canudas, J., Badi, H., Monleón, I., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0340-8 · Cited by 111 · see citing works

The Cysteine Protease Inhibitor, E64d, Reduces Brain Amyloid-β and Improves Memory Deficits in Alzheimer's Disease Animal Models by Inhibiting Cathepsin B, but not BACE1, β-Secretase Activity

Hook, G., HOOK, V. Y. H., & Kindy, M. S. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110101 · Cited by 111 · see citing works

Neuron Loss in Transgenic Mouse Models of Alzheimer's Disease

Wirths, O., & Bayer, T. A. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/723782 · Cited by 110 · see citing works

Molecular basis for passive immunotherapy of Alzheimer's disease

Gardberg, A. S., Dice, L. T., Ou, S. K.-H., Rich, R. L., Helmbrecht, E., Ko, J., Wetzel, R. B., Myszka, D. G., Patterson, P. H., & Dealwis, C. G. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705888104 · Cited by 107 · see citing works

Pyroglutamate Abeta pathology in APP/PS1KI mice, sporadic and familial Alzheimer’s disease cases

Wirths, O., Bethge, T., Marcello, A., Harmeier, A., Jawhar, S., Lucassen, P. J., Multhaup, G., Brody, D. L., Esparza, T., Ingelsson, M., et al. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-009-0314-x · Cited by 106 · see citing works

Overexpression of Glutaminyl Cyclase, the Enzyme Responsible for Pyroglutamate Aβ Formation, Induces Behavioral Deficits, and Glutaminyl Cyclase Knock-out Rescues the Behavioral Phenotype in 5XFAD Mice

Jawhar, S., Wirths, O., Schilling, S., Graubner, S., Demuth, H., & Bayer, T. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185819 · Cited by 105 · see citing works

Global brain delivery of neprilysin gene by intravascular administration of AAV vector in mice

Iwata, N., Sekiguchi, M., Hattori, Y., Takahashi, A., Asai, M., Ji, B., Higuchi, M., Staufenbiel, M., Muramatsu, S., & Saido, T. C. (2013) · Scientific Reports · doi:10.1038/srep01472 · Cited by 104 · 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

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

The ART of Loss: Aβ Imaging in the Evaluation of Alzheimer’s Disease and other Dementias

Villemagne, V. L., Fodero‐Tavoletti, M. T., Pike, K. E., Cappai, R., Masters, C. L., & Rowe, C. C. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8019-y · Cited by 97 · see citing works

Cathepsin B Gene Knockout Improves Behavioral Deficits and Reduces Pathology in Models of Neurologic Disorders

Hook, G., Reinheckel, T., Ni, J., Wu, Z., Kindy, M. S., Peters, C., & HOOK, V. Y. H. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000527 · Cited by 95 · see citing works

Neurovascular dysfunction and vascular amyloid accumulation as early events in Alzheimer's disease

Apátiga-Pérez, R., Soto-Rojas, L. O., Campa-Córdoba, B. B., Luna‐Viramontes, N. I., Cuevas, E., Villanueva‐Fierro, I., Ontiveros‐Torres, M. Á., Bravo-Muñoz, M., Flores-Rodríguez, P., Garcés‐Ramírez, L., et al. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00814-4 · Cited by 90 · see citing works

APP/PS1KI bigenic mice develop early synaptic deficits and hippocampus atrophy

Breyhan, H., Wirths, O., Duan, K., Marcello, A., Rettig, J., & Bayer, T. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0539-7 · Cited by 87 · see citing works

Isolation of an Isoenzyme of Human Glutaminyl Cyclase: Retention in the Golgi Complex Suggests Involvement in the Protein Maturation Machinery

Cynis, H., Rahfeld, J., Stephan, A., Kehlen, A., Koch, B. M., Wermann, M., Demuth, H., & Schilling, S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.078 · Cited by 87 · 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

Amyloid-β Peptide Aβ3pE-42 Induces Lipid Peroxidation, Membrane Permeabilization, and Calcium Influx in Neurons

Gunn, A. P., Wong, B. X. W., Johanssen, T., Griffith, J. C., Masters, C. L., Bush, A. I., Barnham, K. J., Duce, J. A., & Cherny, R. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.655183 · Cited by 84 · see citing works

Passive Immunization against Pyroglutamate-3 Amyloid-β Reduces Plaque Burden in Alzheimer-Like Transgenic Mice: A Pilot Study

Frost, J. L., Liu, B., Kleinschmidt, M., Schilling, S., Demuth, H., & Lemere, C. A. (2012) · Neurodegenerative Diseases · doi:10.1159/000335913 · Cited by 82 · see citing works

N‐Terminal pyroglutamate formation of Aβ38 and Aβ40 enforces oligomer formation and potency to disrupt hippocampal long‐term potentiation

Schlenzig, D., Rönicke, R., Cynis, H., Ludwig, H., Scheel, E., Reymann, K. G., Saido, T. C., Hause, G., Schilling, S., & Demuth, H. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07707.x · Cited by 82 · see citing works

Brain Pyroglutamate Amyloid-β is Produced by Cathepsin B and is Reduced by the Cysteine Protease Inhibitor E64d, Representing a Potential Alzheimer's Disease Therapeutic

Hook, G., Yu, J., Toneff, T., Kindy, M. S., & HOOK, V. Y. H. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131370 · Cited by 82 · see citing works

Alternative pathways for production of β-amyloid peptides of Alzheimer's disease

HOOK, V. Y. H., Schechter, I., Demuth, H., & Hook, G. (2008) · Biological Chemistry · doi:10.1515/bc.2008.124 · Cited by 82 · see citing works

Pyroglutamate-Aβ: Role in the natural history of Alzheimer's disease

Gunn, A. P., Masters, C. L., & Cherny, R. A. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.08.015 · Cited by 79 · see citing works

Misfolding of Amyloidogenic Proteins at Membrane Surfaces: The Impact of Macromolecular Crowding

Bokvist, M., & Gröbner, G. (2007) · Journal of the American Chemical Society · doi:10.1021/ja076059o · Cited by 78 · see citing works

Pyroglutamate Amyloid β (Aβ) Aggravates Behavioral Deficits in Transgenic Amyloid Mouse Model for Alzheimer Disease

Wittnam, J. L., Portelius, E., Zetterberg, H., Gustavsson, M. K., Schilling, S., Koch, B. C. P., Demuth, H., Blennow, K., Wirths, O., & Bayer, T. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308601 · Cited by 77 · see citing works

Alzheimer's Disease: Recent Advances and Future Perspectives

Ubhi, K. K., & Masliah, E. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129028 · Cited by 76 · see citing works

Cerebral amyloidosis: amyloid subunits, mutants and phenotypes

Rostagno, A. A., Holton, J. L., Lashley, T., Révész, T., & Ghiso, J. A. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0182-4 · Cited by 76 · see citing works

Inhibition of glutaminyl cyclase prevents pGlu‐Aβ formation after intracortical/hippocampal microinjection in vivo/in situ

Schilling, S., Appl, T., Hoffmann, T., Cynis, H., Schulz, K., Jagla, W., Friedrich, D., Wermann, M., Buchholz, M., Heiser, U. F., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05471.x · Cited by 76 · see citing works

Neuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models

Wirths, O., & Zampar, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218144 · Cited by 75 · see citing works

Cathepsins S, B and L with aminopeptidases display β-secretase activity associated with the pathogenesis of Alzheimer’s disease

Schechter, I., & Ziv, E. (2011) · Biological Chemistry · doi:10.1515/bc.2011.054 · Cited by 75 · see citing works

Posttranslational modification impact on the mechanism by which amyloid‐β induces synaptic dysfunction

Grochowska, K. M., Yuanxiang, P., Bär, J., Raman, R., Brugal, G. N., Sahu, G., Schweizer, M., Bikbaev, A. F., Schilling, S., Demuth, H., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643519 · Cited by 73 · see citing works

Structure–Activity Relationships of Benzimidazole-Based Glutaminyl Cyclase Inhibitors Featuring a Heteroaryl Scaffold

Ramsbeck, D., Buchholz, M., Koch, B. M., Böhme, L., Hoffmann, T., Demuth, H., & Heiser, U. F. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4001709 · Cited by 70 · see citing works

The Precursor to Glutathione (GSH), γ-Glutamylcysteine (GGC), Can Ameliorate Oxidative Damage and Neuroinflammation Induced by Aβ40 Oligomers in Human Astrocytes

Braidy, N., Zarka, M. H., Jugder, B., Welch, J. H., Jayasena, T., Chan, D. K. Y., Sachdev, P. S., & Bridge, W. J. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00177 · Cited by 70 · see citing works

Inhibitors for Human Glutaminyl Cyclase by Structure Based Design and Bioisosteric Replacement

Buchholz, M., Hamann, A., Aust, S., Brandt, W., Böhme, L., Hoffmann, T., Schilling, S., Demuth, H., & Heiser, U. F. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900969p · Cited by 69 · see citing works

Glutaminyl cyclase contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Aβ deposits in hippocampus via distinct cellular mechanisms

Hartlage‐Rübsamen, M., Morawski, M., Waniek, A., Jäger, C., Zeitschel, U., Koch, B. C. P., Cynis, H., Schilling, S., Schliebs, R., Demuth, H., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0806-2 · Cited by 66 · see citing works

Pyroglutamylated amyloid-β is associated with hyperphosphorylated tau and severity of Alzheimer’s disease

Mandler, M., Walker, L., Santic, R., Hanson, P. S., Upadhaya, A. R., Colloby, S. J., Morris, C. M., Thal, D. R., Thomas, A. J., Schneeberger, A., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1296-9 · Cited by 65 · see citing works

Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy

Pérez-Garmendia, R., & Gevorkian, G. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311050004 · Cited by 65 · see citing works

N‐terminal truncated pyroglutamyl β amyloid peptide Aβpy3‐42 shows a faster aggregation kinetics than the full‐length Aβ1‐42

D’Arrigo, C., Tabaton, M., & Perico, A. (2009) · Biopolymers · doi:10.1002/bip.21271 · Cited by 63 · see citing works

Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly

Barritt, J. D., & Viles, J. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.684084 · Cited by 62 · see citing works

Isoglutaminyl cyclase contributes to CCL2-driven neuroinflammation in Alzheimer’s disease

Hartlage‐Rübsamen, M., Waniek, A., Meißner, J., Morawski, M., Schilling, S., Jäger, C., Kleinschmidt, M., Cynis, H., Kehlen, A., Arendt, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1395-2 · Cited by 61 · 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

Intracellular accumulation of aggregated pyroglutamate amyloid beta: convergence of aging and Aβ pathology at the lysosome

Kimpe, L. D., van Haastert, E. S., Kaminari, A., Zwart, R., Rutjes, H., Hoozemans, J. J. M., & Scheper, W. (2012) · AGE · doi:10.1007/s11357-012-9403-0 · Cited by 60 · see citing works

Review on the APP/PS1KI mouse model: intraneuronal Aβ accumulation triggers axonopathy, neuron loss and working memory impairment

Bayer, T. A., & Wirths, O. (2008) · Genes, Brain and Behavior · doi:10.1111/j.1601-183x.2007.00372.x · Cited by 60 · see citing works

Mutant Presenilin 1 Increases the Expression and Activity of BACE1

Giliberto, L., Borghi, R., Piccini, A., Mangerini, R., Sorbi, S., Cirmena, G., Garuti, A., Ghetti, B. F., Tagliavini, F., Mughal, M. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805685200 · Cited by 56 · see citing works

The spectrum of preclinical Alzheimer's disease pathology and its modulation by ApoE genotype

Pletniková, O., Kageyama, Y., Rudow, G. L., LaClair, K. D., Albert, M., Crain, B. J., Tian, J., Fowler, D. R., & Troncoso, J. C. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.07.007 · Cited by 56 · see citing works

Enhanced Fibril Fragmentation of N‐Terminally Truncated and Pyroglutamyl‐Modified Aβ Peptides

Wulff, M., Baumann, M., Thümmler, A., Yadav, J. K., Heinrich, L., Knüpfer, U., Schlenzig, D., Schierhorn, A., Rahfeld, J., Horn, U., et al. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201511099 · Cited by 53 · see citing works

Mammalian glutaminyl cyclases and their isoenzymes have identical enzymatic characteristics

Stephan, A., Wermann, M., von Bohlen, A., Koch, B. M., Cynis, H., Demuth, H., & Schilling, S. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07337.x · Cited by 53 · see citing works

CuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function

Stefaniak, E., & Bal, W. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01399 · Cited by 53 · see citing works

Differential toxicity, conformation and morphology of typical initial aggregation states of Aβ1-42 and Aβpy3-42 beta-amyloids

Galante, D., Corsaro, A., Florio, T., Vella, S., Pagano, A., Sbrana, F., Vassalli, M., Perico, A., & D’Arrigo, C. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.08.010 · Cited by 51 · see citing works

Acetylcholinesterase inhibitors from the toadstool Cortinarius infractus

Geissler, T., Brandt, W., Porzel, A., Schlenzig, D., Kehlen, A., Wessjohann, L. A., & Arnold, N. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.01.074 · Cited by 50 · see citing works

Cu II Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes?

Borghesani, V., Aliès, B., & Hureau, C. (2017) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201700776 · Cited by 49 · see citing works

Discrete Molecular Dynamics Study of Oligomer Formation by N-Terminally Truncated Amyloid β-Protein

Meral, D., & Urbanc, B. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.010 · Cited by 48 · see citing works

Effector function of anti-pyroglutamate-3 Aβ antibodies affects cognitive benefit, glial activation and amyloid clearance in Alzheimer’s-like mice

Crehan, H., Liu, B., Kleinschmidt, M., Rahfeld, J., Le, K. X., Caldarone, B. J., Frost, J. L., Hettmann, T., Hutter‐Paier, B., O’Nuallain, B., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0579-8 · Cited by 48 · see citing works

Pyroglutamate-Aβ 3 and 11 colocalize in amyloid plaques in Alzheimer's disease cerebral cortex with pyroglutamate-Aβ 11 forming the central core

Sullivan, C. P., Berg, E. A., Elliott-Bryant, R., Fishman, J. B., McKee, A. C., Morin, P. J., Shia, M. A., & Fine, R. E. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.09.071 · Cited by 46 · see citing works

Alzheimer’s Disease Model System Using Drosophila

Tsuda, L., & Lim, Y. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-0529-0_3 · Cited by 46 · see citing works

A critical concentration of N-terminal pyroglutamylated amyloid beta drives the misfolding of Ab1-42 into more toxic aggregates

Galante, D., Ruggeri, F. S., Dietler, G., Pellistri, F., Gatta, E., Corsaro, A., Florio, T., Perico, A., & D’Arrigo, C. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.08.037 · Cited by 45 · see citing works

Passive Aβ Immunotherapy: Current Achievements and Future Perspectives

Schilling, S., Rahfeld, J., Lues, I., & Lemere, C. A. (2018) · Molecules · doi:10.3390/molecules23051068 · Cited by 45 · see citing works

Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways

Dammers, C., Schwarten, M., Buell, A. K., & Willbold, D. (2017) · Chemical Science · doi:10.1039/c6sc04797a · Cited by 45 · see citing works

Copper Coordination to Native N-Terminally Modified versus Full-Length Amyloid-β: Second-Sphere Effects Determine the Species Present at Physiological pH

Aliès, B., Bijani, C., Sayen, S., Guillon, E., Faller, P., & Hureau, C. (2012) · Inorganic Chemistry · doi:10.1021/ic302097d · Cited by 44 · see citing works

Emerging roles of N- and C-terminally truncated Aβ species in Alzheimer’s disease

Wirths, O., & Zampar, S. (2019) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1702972 · Cited by 44 · see citing works

C-Terminal Tetrapeptides Inhibit Aβ42-Induced Neurotoxicity Primarily through Specific Interaction at the N-Terminus of Aβ42

Li, H., Du, Z., Lopes, D. H. J., Fradinger, E. A., Wang, C., & Bitan, G. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200982p · Cited by 43 · see citing works

Pyroglutamate Formation Influences Solubility and Amyloidogenicity of Amyloid Peptides

Schlenzig, D., Manhart, S., Cinar, Y., Kleinschmidt, M., Hause, G., Willbold, D., Funke, S. A., Schilling, S., & Demuth, H.-U. (2009) · Biochemistry · doi:10.1021/bi900818a · Cited by 228 · see citing works

N‐Terminal pyroglutamate formation of Aβ38 and Aβ40 enforces oligomer formation and potency to disrupt hippocampal long‐term potentiation

Schlenzig, D., Rönicke, R., Cynis, H., Ludwig, H., Scheel, E., Reymann, K. G., Saido, T. C., Hause, G., Schilling, S., & Demuth, H. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07707.x · Cited by 82 · see citing works

P3‐412: N‐terminal truncation and pyroglutamate modification of amyloid peptides: Potential strategies to interfere with neurodegenerative pathogenesis in Alzheimer's disease, FBD, FDD

Schilling, S., Cynis, H., Rönicke, R., Reymann, K. G., Seifert, F., Schlenzig, D., & Demuth, H. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.1955

O5‐01‐04: N‐terminal pyroglutamate (pGlu) formation enhances Aß oligomer formation and potency to disrupt hippocampal LTP

Schilling, S., Schlenzig, D., Rönicke, R., Cynis, H., Reymann, K. G., Saido, T. C., & Demuth, H. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.1972

P3–430: Conformation–dependent antibodies reveal the complexity of amyloid formation via seeding and cross–seeding

Kayed, R., & Glabe, C. G. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1701 · Cited by 1 · see citing works