The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site
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Distal APP mutations such as London (V717I) lack an effect on meprin-β generation of Aβ2-X.
“as opposed to the lack of effect of distal mutations (i.e., London (V717I)”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Schonherr et al., 2016
Meprin-β competes in vivo with α-secretase for membrane-bound APP.
“suggesting in vivo competition with α-secretase for membrane-bound APP (Schonherr et al., 2016).”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Schonherr et al., 2016
Meprin-β deletion in mice correlates with higher levels of sAPPα.
“meprin-β deletion in mice correlates with higher levels of sAPPα”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Schonherr et al., 2016
APP mutations proximal to the β-cleavage site, such as Swedish (K670N-M671L) or Icelandic (A673T), prevent the generation of Aβ2-X by meprin-β.
“APP mutations proximal to the β-cleavage site, like the Swedish (K670N-M671L) or the “protective” Icelandic (A673T), prevent the generation of Aβ2–X by meprin-β”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Schonherr et al., 2016
Amino acid composition around the β-cleavage site is important for meprin-β.
“highlighting the importance for meprin-β of aminoacid composition around the β-cleavage site (Schonherr et al., 2016).”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Schonherr et al., 2016
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Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388 · cited 1×
“Cells were infected with a recombinant adenovirus expressing human APP695 at a concentration of 100 pfu/cell for 6 h in DIV1 as described [68].”
Self-citationKuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621 · cited 1×
“192 specific for sAPPβ, mAb 22C11 recognizing the APP ectodomain, and actin for loading control [44].”
Self-citationBouter, Y., Dietrich, K., Wittnam, J. L., Rezaei-Ghaleh, N., Pillot, T., Papot-Couturier, S., Lefebvre, T., Sprenger, F., Wirths, O., Zweckstetter, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1129-2 · Cited by 175
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Metadata
- Authors
- Schönherr, C., Bien, J., Isbert, S., Wichert, R., Prox, J., Altmeppen, H., Kumar, S., Walter, J., Lichtenthaler, S. F., Weggen, S., Glatzel, M., Becker-Pauly, C., & Pietrzik, C. U.
- Venue
- Molecular Neurodegeneration
- Published
- 2016-02-19
- Volume
- 11
- Issue
- 1
- ISSN
- 1750-1326
- PMC
- PMC4759862
- Cited by
- 76
- References
- 5
- Language
- en
- Funders
- Deutsche Forschungsgemeinschaft (DE) (PI379/6-1, PI379/5-2)
- Sonderforschungsbereich (CRC877)
- Bundesministerium für Bildung und Forschung (DE)
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