The roles of GxxxG motif and gamma-secretase components in APP processing

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

Fernández‐Escamilla, A. M., Rousseau, F., Schymkowitz, J. W. H., & Serrano, L. G. (2004) · Nature Biotechnology · doi:10.1038/nbt1012 · Cited by 1,663 · see citing works

Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo

Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., Prada, C.-M., Kim, G., Seekins, S., Yager, D., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80230-5 · Cited by 1,478 · see citing works

Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1

Duff, K., Eckman, C., Zehr, C., Yu, X., Prada, C.-M., Pérez‐Tur, J., Hutton, M., Buée, L., Harigaya, Y., Yager, D., et al. (1996) · Nature · doi:10.1038/383710a0 · Cited by 1,453 · see citing works

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 · see citing works

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice

Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271 · see citing works

The role of presenilin cofactors in the γ-secretase complex

Takasugi, N., Tomita, T., Hayashi, I., Tsuruoka, M., Niimura, M., Takahashi, Y., Thinakaran, G., & Iwatsubo, T. (2003) · Nature · doi:10.1038/nature01506 · Cited by 869 · see citing works

Loss of Presenilin Function Causes Impairments of Memory and Synaptic Plasticity Followed by Age-Dependent Neurodegeneration

Saura, C. A., Choi, S.-Y., Beglopoulos, V., Malkani, S., Zhang, D., Rao, B. S. S., Chattarji, S., Kelleher, R. J., Kandel, E. R., Duff, K., et al. (2004) · Neuron · doi:10.1016/s0896-6273(04)00182-5 · Cited by 757 · see citing works

Presenilins Form ER Ca2+ Leak Channels, a Function Disrupted by Familial Alzheimer's Disease-Linked Mutations

Tu, H., Nelson, O. L., Bezprozvanny, A., Wang, Z., Lee, S.-F., Hao, Y.-H., Serneels, L., Strooper, B. D., Yu, G., & Борисович, Б. И. (2006) · Cell · doi:10.1016/j.cell.2006.06.059 · Cited by 691 · see citing works

Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions

Senes, A., Gerstein, M., & Engelman, D. M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3488 · Cited by 609 · 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

γ-Secretase: proteasome of the membrane?

Kopan, R., & Ilagan, M. X. G. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1406 · Cited by 554 · see citing works

Nicastrin Functions as a γ-Secretase-Substrate Receptor

Shah, S., Lee, S.-F., Tabuchi, K., Hao, Y.-H., Yu, C., LaPlant, Q. C., Ball, H. L., Dann, C. E., Südhof, T. C., & Yu, G. (2005) · Cell · doi:10.1016/j.cell.2005.05.022 · Cited by 470 · see citing works

A Hundred Years of Alzheimer's Disease Research

Hardy, J. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.016 · Cited by 467 · see citing works

Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>

Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4849-06.2007 · Cited by 359 · see citing works

Loss‐of‐function presenilin mutations in Alzheimer disease

Strooper, B. D. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400897 · Cited by 351 · see citing works

TMP21 is a presenilin complex component that modulates γ-secretase but not ɛ-secretase activity

Chen, F., Hasegawa, H., Schmitt‐Ulms, G., Kawarai, T., Böhm, C., Katayama, T., Gu, Y., Sanjo, N., Glista, M. J., Rogaeva, E. A., et al. (2006) · Nature · doi:10.1038/nature04667 · Cited by 301 · see citing works

The Ratio of Monomeric to Aggregated Forms of Aβ40 and Aβ42 Is an Important Determinant of Amyloid-β Aggregation, Fibrillogenesis, and Toxicity

Jan, A., Gokce, O., Luthi-Carter, R., & Lashuel, H. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803159200 · Cited by 291 · see citing works

GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42

Munter, L. M., Voigt, P., Harmeier, A., Kaden, D., Gottschalk, K. E., Weise, C., Pipkorn, R., Schaefer, M. K. E., Langosch, D., & Multhaup, G. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601616 · Cited by 284 · see citing works

Presenilins are essential for regulating neurotransmitter release

Zhang, C., Wu, B., Beglopoulos, V., Wines-Samuelson, M., Zhang, D., Dragatsis, I., Südhof, T. C., & Shen, J. (2009) · Nature · doi:10.1038/nature08177 · Cited by 280 · see citing works

Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins

Kim, S., Jeon, T., Oberai, A., Yang, D., Schmidt, J. J., & Bowie, J. U. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501234102 · Cited by 279 · see citing works

Substrate-targeting γ-secretase modulators

Kukar, T. L., Ladd, T. B., Bann, M. A., Fraering, P. C., Narlawar, R., Maharvi, G. M., Healy, B., Chapman, R., Welzel, A. T., Price, R. W., et al. (2008) · Nature · doi:10.1038/nature07055 · Cited by 276 · see citing works

Direct and Potent Regulation of γ-Secretase by Its Lipid Microenvironment

Osenkowski, P., Ye, W., Wang, R., Wolfe, M. S., & Selkoe, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801925200 · Cited by 269 · see citing works

γ-Secretase Heterogeneity in the Aph1 Subunit: Relevance for Alzheimer’s Disease

Serneels, L., Biervliet, J. V., Craessaerts, K., Dejaegere, T., Horré, K., Houtvin, T. V., Esselmann, H., Paul, S., Schäfer, M., Berezovska, O., et al. (2009) · Science · doi:10.1126/science.1171176 · Cited by 259 · see citing works

APP Processing and Synaptic Plasticity in Presenilin-1 Conditional Knockout Mice

Yu, H., Saura, C. A., Choi, S., Sun, L. D., Yang, X., Handler, M., Kawarabayashi, T., Younkin, L. H., Fedeles, B. I., Wilson, M. A., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00417-2 · Cited by 255 · see citing works

Amyloid-β peptide (Aβ) neurotoxicity is modulated by the rate of peptide aggregation: Aβ dimers and trimers correlate with neurotoxicity

Hung, L. W., Ciccotosto, G. D., Giannakis, E., Tew, D. J., Perez, K., Masters, C. L., Cappai, R., Wade, J. D., & Barnham, K. J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3916-08.2008 · Cited by 210 · see citing works

CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production

Zhou, S., Zhou, H., Walian, P. J., & Jap, B. K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502768102 · Cited by 199 · see citing works

The Orphan G Protein–Coupled Receptor 3 Modulates Amyloid-Beta Peptide Generation in Neurons

Thathiah, A., Spittaels, K., Hoffmann, M., Staes, M., Cohen, A., Horré, K., Vanbrabant, M., Coun, F., Baekelandt, V., Delacourte, A., et al. (2009) · Science · doi:10.1126/science.1160649 · Cited by 196 · see citing works

Inhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42

Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J.-N., & Smith, S. O. (2006) · Biochemistry · doi:10.1021/bi052485f · Cited by 191 · see citing works

When loss is gain: reduced presenilin proteolytic function leads to increased Aβ42/Aβ40

Wolfe, M. S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400896 · Cited by 190 · see citing works

Proteomic Profiling of γ-Secretase Substrates and Mapping of Substrate Requirements

Hemming, M. L., Elias, J. E., Gygi, S. P., & Selkoe, D. J. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060257 · Cited by 171 · see citing works

Potential role of presenilin-regulated signaling pathways in sporadic neurodegeneration

Koo, E. H., & Kopan, R. (2004) · Nature Medicine · doi:10.1038/nm1065 · Cited by 154 · see citing works

Presenilin/γ-Secretase-mediated Cleavage of the Voltage-gated Sodium Channel β2-Subunit Regulates Cell Adhesion and Migration

Kim, D. Y., Ingano, L. A. M., Carey, B. W., Pettingell, W. H., & Kovacs, D. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412938200 · Cited by 146 · see citing works

Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs

Kienlen‐Campard, P., Tasiaux, B., Hees, J. V., Li, M., Huysseune, S., Sato, T., Fei, J. Z., Aimoto, S., Courtoy, P. J., Smith, S. O., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707142200 · Cited by 138 · see citing works

Analysis of the γ-secretase interactome and validation of its association with tetraspanin-enriched microdomains

Wakabayashi, T., Craessaerts, K., Bammens, L., Bentahir, M., Borgions, F., Herdewijn, P., Staes, A., Timmerman, E., Vandekerckhove, J., Rubinstein, E., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1978 · Cited by 135 · see citing works

Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization

Murray, M. M., Bernstein, S. L., Nyugen, V., Condron, M. M., Teplow, D. B., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8092604 · Cited by 128 · see citing works

Disease modifying therapy for AD?¹

Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117 · see citing works

A Conserved GXXXG Motif in APH-1 Is Critical for Assembly and Activity of the γ-Secretase Complex

Lee, S.-F., Shah, S., Yu, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309745200 · Cited by 116 · see citing works

Synaptic activity prompts γ-secretase–mediated cleavage of EphA4 and dendritic spine formation

Inoue, E., Deguchi‐Tawarada, M., Togawa, A., Matsui, C., Arita, K., Katahira-Tayama, S., Sato, T., Yamauchi, E., Oda, Y., & Takai, Y. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809151 · Cited by 114 · see citing works

BRI2 (ITM2b) Inhibits A  Deposition In Vivo

Kim, J., Miller, V. M., Levites, Y., West, K. J., Zwizinski, C. W., Moore, B. D., Troendle, F. J., Bann, M., Verbeeck, C., Price, R. W., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0891-08.2008 · Cited by 113 · see citing works

A helix-to-coil transition at the ε-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis

Sato, T., Tang, T.-C., Reubins, G., Fei, J. Z., Fujimoto, T., Kienlen‐Campard, P., Constantinescu, S. N., Octave, J., Aimoto, S., & Smith, S. O. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812261106 · Cited by 111 · see citing works

Aβ40 Protects Non-toxic Aβ42 Monomer from Aggregation

Yan, Y., & Wang, C. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.014 · Cited by 99 · see citing works

Sortilin, SorCS1b, and SorLA Vps10p sorting receptors, are novel γ-secretase substrates

Nyborg, A. C., Ladd, T. B., Zwizinski, C. W., Lah, J. J., & Golde, T. E. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-3 · Cited by 96 · see citing works

Role of Amyloid- Glycine 33 in Oligomerization, Toxicity, and Neuronal Plasticity

Harmeier, A., Wozny, C., Rost, B. R., Munter, L. M., Hua, H., Georgiev, O., Beyermann, M., Hildebrand, P. W., Weise, C., Schaffner, W., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1336-09.2009 · Cited by 94 · see citing works

Regulation of tyrosinase trafficking and processing by presenilins: Partial loss of function by familial Alzheimer's disease mutation

Wang, R., Tang, P., Wang, P., Boissy, R. E., & Zheng, H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509822102 · Cited by 90 · see citing works

Dual roles of the transmembrane protein p23/TMP21 in the modulation of amyloid precursor protein metabolism

Vetrivel, K. S., Gong, P., Bowen, J. W., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-4 · Cited by 80 · see citing works

Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants

Gorman, P. M., Kim, S., Guo, M., Melnyk, R. A., McLaurin, J., Fraser, P. E., Bowie, J. U., & Chakrabartty, A. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-17 · Cited by 78 · see citing works

An alternative interpretation of the amyloid Aβ hypothesis with regard to the pathogenesis of Alzheimer's disease

Marchesi, V. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503181102 · Cited by 74 · see citing works

Low Density Lipoprotein Receptor-related Protein (LRP) Interacts with Presenilin 1 and Is a Competitive Substrate of the Amyloid Precursor Protein (APP) for γ-Secretase

Lleó, A., Waldron, E., Arnim, C. A. F. V., Herl, L. D., Tangredi, M. M., Peltan, I. D., Strickland, D. K., Koo, E. H., Hyman, B. T., Pietrzik, C. U., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413969200 · Cited by 67 · see citing works

Purification, Pharmacological Modulation, and Biochemical Characterization of Interactors of Endogenous Human γ-Secretase

Winkler, E., Hobson, S., Fukumori, A., Dümpelfeld, B., Luebbers, T., Baumann, K., Haass, C., Hopf, C., & Steiner, H. (2009) · Biochemistry · doi:10.1021/bi801204g · Cited by 66 · see citing works

Histopathological and molecular heterogeneity among individuals with dementia associated with Presenilin mutations

Maarouf, C. L., Daugs, I. D., Spina, S., Vidal, R., Kokjohn, T. A., Patton, R., Kalback, W. M., Luehrs, D. C., Walker, D. G., Castaño, E. M., et al. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-20 · Cited by 65 · see citing works

Presenilins in Memory, Alzheimer's Disease, and Therapy

Marjaux, E., Hartmann, D., & Strooper, B. D. (2004) · Neuron · doi:10.1016/s0896-6273(04)00218-1 · Cited by 63 · see citing works

Formation of Pmel17 Amyloid Is Regulated by Juxtamembrane Metalloproteinase Cleavage, and the Resulting C-terminal Fragment Is a Substrate for γ-Secretase

Kummer, M. P., Maruyama, H., Hülsmann, C., Baches, S., Weggen, S., & Koo, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808904200 · Cited by 60 · see citing works

Amyloid β-Protein Precursor Juxtamembrane Domain Regulates Specificity of γ-Secretase-dependent Cleavages

Ren, Z., Schenk, D., Basi, G. S., & Shapiro, I. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702739200 · Cited by 59 · see citing works

The insulin-like growth factor 1 (IGF-1) receptor is a substrate for γ-secretase-mediated intramembrane proteolysis

McElroy, B., Powell, J. C., & McCarthy, J. V. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.05.062 · Cited by 58 · see citing works

Structural Role of Glycine in Amyloid Fibrils Formed from Transmembrane α-Helices

Liu, W., Crocker, E., Zhang, W., Elliott, J. I., Luy, B., Li, H., Aimoto, S., & Smith, S. O. (2005) · Biochemistry · doi:10.1021/bi047827g · Cited by 56 · see citing works

Evidence That CD147 Modulation of β-Amyloid (Aβ) Levels Is Mediated by Extracellular Degradation of Secreted Aβ*♦

Vetrivel, K. S., Zhang, X.-L., Meckler, X., Cheng, H., Lee, S.-H., Gong, P., Lopes, K. O., Chen, Y., Iwata, N., Yin, K., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801037200 · Cited by 52 · see citing works

Chemical Cross-linking Provides a Model of the γ-Secretase Complex Subunit Architecture and Evidence for Close Proximity of the C-terminal Fragment of Presenilin with APH-1

Steiner, H., Winkler, E., & Haass, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709067200 · Cited by 46 · see citing works

Intramembrane Proteolysis of GXGD-type Aspartyl Proteases Is Slowed by a Familial Alzheimer Disease-like Mutation

Fluhrer, R., Fukumori, A., Martin, L., Grammer, G., Haug‐Kröper, M., Klier, B., Winkler, E., Kremmer, E., Condron, M. M., Teplow, D. B., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806092200 · Cited by 38 · see citing works

Complex Patterns of Histidine, Hydroxylated Amino Acids and the GxxxG Motif Mediate High-affinity Transmembrane Domain Interactions

Herrmann, J. R., Panitz, J. C., Unterreitmeier, S., et al. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.058 · Cited by 33 · see citing works

Selective modulation of amyloid‐β peptide degradation by flurbiprofen, fenofibrate, and related compounds regulates Aβ levels

Abdul‐Hay, S. O., Edirisinghe, P. D., & Thatcher, G. R. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06355.x · Cited by 18 · see citing works

TMP21 regulates Aβ production but does not affect caspase-3, p53, and neprilysin

Dolcini, V., Dunys, J., Sévalle, J., Chen, F., Guillot‐Sestier, M., George‐Hyslop, P. S., Fraser, P. E., & Checler, F. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.151 · Cited by 16 · see citing works

Genetic Dissection of γ-Secretase-Dependent and-Independent Functions of Presenilin in Regulating Neuronal Cell Cycle and Cell Death

Kallhoff, V., Hu, L., Chen, X., Pautler, R. G., & Zheng, H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2873-08.2008 · Cited by 14 · see citing works

The GxxxG Motif in the Transmembrane Domain of AβPP Plays an Essential Role in the Interaction of CTFβ with the γ-secretase Complex and the Formation of Amyloid-β

Mao, G., Tan, J., Cui, M., et al. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1132 · Cited by 9 · see citing works

Cloning and Characterization of Rat BAT3 cDNA

Ozaki, T., Hanaoka, E., Naka, M., et al. (1999) · DNA and Cell Biology · doi:10.1089/104454999315222 · Cited by 22 · see citing works

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Preprint

Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

Anthoxanthum Mosaic Virus

Catherall, P. L. (1970) · Plant Pathology · doi:10.1111/j.1365-3059.1970.tb00999.x · Cited by 6 · see citing works

Ecological and evolutionary importance of neighbors in the grass Anthoxanthum odoratum

Platenkamp, G. A. J., & Foin, T. C. (1990) · Oecologia · doi:10.1007/bf00317753 · Cited by 21 · see citing works

Viral pathogens and the advantage of sex in the perennial grass Anthoxanthum odoratum

Kelley, S. E. (1997) · Springer eBooks · doi:10.1007/978-94-009-0077-6_3 · Cited by 39 · see citing works