Secreted amyloid-β precursor protein functions as a GABA B R1a ligand to modulate synaptic transmission

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484 · see citing works

Large-scale analysis of the yeast proteome by multidimensional protein identification technology

Washburn, M. P., Wolters, D. A., & Yates, J. R. (2001) · Nature Biotechnology · doi:10.1038/85686 · Cited by 4,759 · see citing works

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619 · see citing works

The CCPN data model for NMR spectroscopy: Development of a software pipeline

Vranken, W., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinás, M., Ulrich, E. L., Markley, J. L., Ionides, J., & Laue, E. D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20449 · Cited by 3,222 · see citing works

The Xplor-NIH NMR molecular structure determination package

Schwieters, C. D., Kuszewski, J. J., Tjandra, N., & Clore, G. M. (2003) · Journal of Magnetic Resonance · doi:10.1016/s1090-7807(02)00014-9 · Cited by 2,371 · see citing works

Direct analysis of protein complexes using mass spectrometry

Link, A. J., Eng, J. K., Schieltz, D. M., Carmack, E., Mize, G. J., Morris, D. R., Garvik, B. M., & Yates, J. R. (1999) · Nature Biotechnology · doi:10.1038/10890 · Cited by 2,218 · see citing works

Evaluation of Multidimensional Chromatography Coupled with Tandem Mass Spectrometry (LC/LC−MS/MS) for Large-Scale Protein Analysis: The Yeast Proteome

Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L., & Gygi, S. P. (2002) · Journal of Proteome Research · doi:10.1021/pr025556v · Cited by 1,652 · see citing works

APP Processing and Synaptic Function

Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644 · see citing works

Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus

Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611 · see citing works

DTASelect and Contrast: Tools for Assembling and Comparing Protein Identifications from Shotgun Proteomics

Tabb, D. L., McDonald, W. H., & Yates, J. R. (2002) · Journal of Proteome Research · doi:10.1021/pr015504q · Cited by 1,369 · see citing works

Characterization and Chromosomal Localization of a cDNA Encoding Brain Amyloid of Alzheimer's Disease

Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,333 · see citing works

ScanImage: Flexible software for operating laser scanning microscopes

Pologruto, T. A., Sabatini, B. L., & Svoboda, K. (2003) · BioMedical Engineering OnLine · doi:10.1186/1475-925x-2-13 · Cited by 1,297 · see citing works

Trafficking and Proteolytic Processing of APP

Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works

Network abnormalities and interneuron dysfunction in Alzheimer disease

Palop, J. J., & Mucke, L. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.141 · Cited by 1,022 · see citing works

Molecular Structure and Physiological Functions of GABA B Receptors

Bettler, B., Kaupmann, K., Mosbacher, J., & Gassmann, M. (2004) · Physiological Reviews · doi:10.1152/physrev.00036.2003 · Cited by 927 · see citing works

Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins

Wilhelm, B. G., Mandad, S., Truckenbrodt, S., Kröhnert, K., Schäfer, C., Rammner, B., Koo, S. J., Claßen, G. A., Krauss, M., Haucke, V., et al. (2014) · Science · doi:10.1126/science.1252884 · Cited by 770 · see citing works

Not just amyloid: physiological functions of the amyloid precursor protein family

Müller, U. C., Deller, T., & Korte, M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.29 · Cited by 634 · see citing works

Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides.

Robakis, N. K. R. K., Ramakrishna, N., Wolfe, G. C., & Wisniewski, H. M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.12.4190 · Cited by 603 · see citing works

Thy1-GCaMP6 transgenic mice for neuronal population imaging in vivo

Dana, H., Chen, T.-W., Hu, A., Shields, B. C., Guo, C., Looger, L. L., Kim, D. S., & Svoboda, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108697 · Cited by 574 · see citing works

Amyloid-β as a positive endogenous regulator of release probability at hippocampal synapses

Abramov, E., Dolev, I., Fogel, H., Ciccotosto, G. D., Ruff, E., & Slutsky, I. (2009) · Nature Neuroscience · doi:10.1038/nn.2433 · Cited by 499 · see citing works

Mice with Combined Gene Knock-Outs Reveal Essential and Partially Redundant Functions of Amyloid Precursor Protein Family Members

Heber, S., Herms, J. W., Gajic, V., Hainfellner, J. A., Aguzzi, A., Rülicke, T., Kretzschmar, H. A., von Koch, C., Sisodia, S. S., Tremml, P., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-21-07951.2000 · Cited by 495 · see citing works

Secreted form of amyloid β protein precursor is involved in the growth regulation of fibroblasts

Saitoh, T., Sundsmo, M. P., Roch, J., Kimura, N., Cole, G. M., Schubert, D. A., Oltersdorf, T., & Schenk, D. B. (1989) · Cell · doi:10.1016/0092-8674(89)90096-2 · Cited by 471 · see citing works

The Presynaptic Particle Web

Phillips, G. R., Huang, J. K., Wang, Y., Tanaka, H., Shapiro, L. S., Zhang, W., Shan, W., Arndt, K., Frank, M., Gordon, R. E., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00450-0 · Cited by 438 · see citing works

Combined automated NOE assignment and structure calculation with CYANA

Güntert, P., & Buchner, L. (2015) · Journal of Biomolecular NMR · doi:10.1007/s10858-015-9924-9 · Cited by 403 · see citing works

η-Secretase processing of APP inhibits neuronal activity in the hippocampus

Willem, M., Tahirovic, S., Busche, M. A., Ovsepian, S. V., Chafai, M., Kootar, S., Hornburg, D., Evans, L. D. B., Moore, S., Daria, A., et al. (2015) · Nature · doi:10.1038/nature14864 · Cited by 398 · cited 2× · see citing works

The Secreted β-Amyloid Precursor Protein Ectodomain APPsα Is Sufficient to Rescue the Anatomical, Behavioral, and Electrophysiological Abnormalities of APP-Deficient Mice

Ring, S., Weyer, S. W., Kilian, S. B., Waldron, E., Pietrzik, C. U., Filippov, M. A., Herms, J., Buchholz, C., Eckman, C. B., Korte, M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.1026-07.2007 · Cited by 390 · see citing works

Presynaptic inhibition of miniature excitatory synaptic currents by baclofen and adenosine in the hippocampus.

Scanziani, M., Capogna, M., Gähwiler, B., & Thompson, S. (1992) · Neuron · doi:10.1016/0896-6273(92)90244-8 · Cited by 386 · see citing works

LRRTM2 Interacts with Neurexin1 and Regulates Excitatory Synapse Formation

de Wit, J., Sylwestrak, E., O’Sullivan, M. L., Otto, S. J., Tiglio, K., Savas, J. N., Yates, J. R., Comoletti, D., Taylor, P., & Ghosh, A. (2009) · Neuron · doi:10.1016/j.neuron.2009.12.019 · Cited by 376 · see citing works

Age-related cognitive deficits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the β-amyloid precursor protein

Dawson, G. R., Seabrook, G. R., Zheng, H., Smith, D. W., Graham, S. J., O'Dowd, G., Bowery, B. J., Boyce, S., Trumbauer, M. E., Chen, H. Y., et al. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00410-2 · Cited by 364 · see citing works

Regulation of neuronal GABAB receptor functions by subunit composition

Gassmann, M., & Bettler, B. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3249 · Cited by 364 · see citing works

Extremely long-lived nuclear pore proteins in the rat brain

Savas, J. N., Toyama, B. H., Xu, T., Yates, J. R., & Hetzer, M. W. (2012) · Science · doi:10.1126/science.1217421 · Cited by 335 · see citing works

Activation of K+ channels and suppression of neuronal activity by secreted β-amyloid-precursor protein

Furukawa, K., Barger, S. W., Blalock, E. M., & Mattson, M. P. (1996) · Nature · doi:10.1038/379074a0 · Cited by 332 · see citing works

Differential Compartmentalization and Distinct Functions of GABAB Receptor Variants

Vigot, R., Barbieri, S., Bräuner‐Osborne, H., Tureček, R., Shigemoto, R., Zhang, Y., Luján, R., Jacobson, L. H., Biermann, B., Fritschy, J., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.04.014 · Cited by 311 · see citing works

Organization and functions of mGlu and GABAB receptor complexes

Pin, J., & Bettler, B. (2016) · Nature · doi:10.1038/nature20566 · Cited by 274 · see citing works

Mechanisms contributing to the deficits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein

Seabrook, G. R., Smith, D. W., Bowery, B. J., Easter, A., Reynolds, T., Fitzjohn, S. M., Morton, R. A., Zheng, H., Dawson, G. R., SIRINATHSINGHJI, D. J. S., et al. (1999) · Neuropharmacology · doi:10.1016/s0028-3908(98)00204-4 · Cited by 256 · see citing works

Implications of GABAergic Neurotransmission in Alzheimer’s Disease

Li, Y., Sun, H., Chen, Z., Xu, H.-X., Bu, G.-J., & Zheng, H. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00031 · Cited by 252 · see citing works

DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure

Cheung, M.-S., Maguire, M. L., Stevens, T. J., & Broadhurst, R. W. (2009) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2009.11.008 · Cited by 251 · see citing works

Release of amyloid beta-protein precursor derivatives by electrical depolarization of rat hippocampal slices

Nitsch, R. M., Farber, S. A., Growdon, J. H., & Wurtman, R. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5191 · Cited by 244 · see citing works

An Extracellular Interactome of Immunoglobulin and LRR Proteins Reveals Receptor-Ligand Networks

Özkan, E., Carrillo, R. A., Eastman, C., Weiszmann, R., Waghray, D., Johnson, K. G., Zinn, K., Celniker, S., & García, K. C. (2013) · Cell · doi:10.1016/j.cell.2013.06.006 · Cited by 232 · see citing works

Validation of Tandem Mass Spectrometry Database Search Results Using DTASelect

Cociorva, D., Tabb, D. L., & Yates, J. R. (2006) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi1304s16 · Cited by 228 · see citing works

Transient intercellular adhesion: the importance of weak protein-protein interactions

van der Merwe, P. A., & Barclay, A. N. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90109-0 · Cited by 214 · see citing works

Endogenous secreted amyloid precursor protein-α regulates hippocampal NMDA receptor function, long-term potentiation and spatial memory

Taylor, C. J., Ireland, D. R., Ballagh, I. H., Bourne, K., Marechal, N. M., Turner, P. R., Bilkey, D. K., Tate, W. P., & Abraham, W. C. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.04.011 · Cited by 204 · see citing works

GABAB receptors: synaptic functions and mechanisms of diversity

Ulrich, D., & Bettler, B. (2007) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2007.04.001 · Cited by 201 · see citing works

SGS742: the first GABAB receptor antagonist in clinical trials

Froestl, W., Gallagher, M., Jenkins, H., Madrid, A., Melcher, T., Teichman, S. L., Mondadori, C., & Pearlman, R. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.07.030 · Cited by 194 · see citing works

Amyloid precursor protein (APP) regulates synaptic structure and function

Tyan, S.-H., Shih, A. Y.-J., Walsh, J. J., Maruyama, H., Sarsoza, F., Ku, L., Eggert, S., Hof, P. R., Koo, E. H., & Dickstein, D. L. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.07.009 · Cited by 191 · see citing works

Acute function of secreted amyloid precursor protein fragment APPsα in synaptic plasticity

Hick, M., Herrmann, U., Weyer, S. W., Mallm, J., Tschäpe, J., Borgers, M., Mercken, M. H., Roth, F. C., Draguhn, A., Slomianka, L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1368-x · Cited by 186 · see citing works

Secreted form of β-amyloid precursor protein shifts the frequency dependency for induction of LTD, and enhances LTP in hippocampal slices

Ishida, A., Furukawa, K., Keller, J. N., & Mattson, M. P. (1997) · Neuroreport · doi:10.1097/00001756-199707070-00009 · Cited by 178 · see citing works

Genetic Suppression of Transgenic APP Rescues Hypersynchronous Network Activity in a Mouse Model of Alzeimer's Disease

Born, H. A., Kim, J.-Y., Savjani, R. R., Das, P., Dabaghian, Y. A., Guo, Q., Yoo, J. W., Schuler, D. R., Cirrito, J. R., Zheng, H., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.5171-13.2014 · Cited by 178 · see citing works

Study of the synthesis and secretion of normal and artificial mutants of murine amyloid precursor protein (APP): cleavage of APP occurs in a late compartment of the default secretion pathway.

Strooper, B. D., Umans, L., Leuven, F. V., & BERGHE, H. V. D. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.2.295 · Cited by 152 · see citing works

Modular composition and dynamics of native GABAB receptors identified by high-resolution proteomics

Schwenk, J., Pérez‐Garci, E., Schneider, A., Kollewe, A., Gauthier‐Kemper, A., Fritzius, T., Raveh, A., Dinamarca, M. C., Hanuschkin, A., Bildl, W., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4198 · Cited by 146 · see citing works

GABAB receptor antagonist SGS742 improves spatial memory and reduces protein binding to the cAMP response element (CRE) in the hippocampus

Helm, K. A., Haberman, R. P., Dean, S. L., Hoyt, E. C., Melcher, T., Lund, P. K., & Gallagher, M. (2005) · Neuropharmacology · doi:10.1016/j.neuropharm.2005.01.019 · Cited by 118 · see citing works

Amyloid Precursor Protein Regulates Ca v 1.2 L-type Calcium Channel Levels and Function to Influence GABAergic Short-Term Plasticity

Yang, L., Wang, Z., Wang, B., Justice, N. J., & Zheng, H. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4104-09.2009 · Cited by 117 · see citing works

Therapeutic Potential of Secreted Amyloid Precursor Protein APPsα

Mockett, B. G., Richter, M., Abraham, W. C., & Müller, U. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00030 · Cited by 115 · see citing works

APP modulates KCC2 expression and function in hippocampal GABAergic inhibition

Chen, M., Wang, J., Jiang, J., Zheng, X., Justice, N. J., Wang, K., Ran, X., Li, Y., Huo, Q., Zhang, J., et al. (2017) · eLife · doi:10.7554/elife.20142 · Cited by 109 · see citing works

The Amyloid Precursor Protein Controls Adult Hippocampal Neurogenesis through GABAergic Interneurons

Wang, B., Wang, Z., Sun, L., Yang, L., Li, H., Cole, A. L., Rodriguez-Rivera, J., Lu, H., & Zheng, H. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2848-14.2014 · Cited by 107 · see citing works

Comparative analysis of single and combined APP/APLP knockouts reveals reduced spine density in APP-KO mice that is prevented by APPsα expression

Weyer, S. W., Zagrebelsky, M., Herrmann, U., Hick, M., Ganss, L., Gobbert, J., Gruber, M., Altmann, C., Körte, M., Deller, T., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-36 · Cited by 98 · see citing works

The Sorting Receptor SorCS1 Regulates Trafficking of Neurexin and AMPA Receptors

Savas, J. N., Ribeiro, L. F., Wierda, K. D. B., Wright, R., DeNardo, L. A., Rice, H. C., Chamma, I., Wang, Y., Zemla, R., Lavallée‐Adam, M., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.08.007 · Cited by 92 · see citing works

Redundancy and divergence in the amyloid precursor protein family

Shariati, S. A., & Strooper, B. D. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.026 · Cited by 92 · see citing works

The Sushi Domains of GABA B Receptors Function as Axonal Targeting Signals

Biermann, B., Ivankova-Susankova, K., Bradaïa, A., Aziz, S. A., Besseyrias, V., Kapfhammer, J. P., Missler, M., Gassmann, M., & Bettler, B. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3172-09.2010 · Cited by 92 · see citing works

Presynaptic inhibition by baclofen of miniature EPSCs and IPSCs in substantia gelatinosa neurons of the adult rat spinal dorsal horn

Iyadomi, M., Iyadomi, I., Kumamoto, E., Tomokuni, K., & Yoshimura, M. (2000) · Pain · doi:10.1016/s0304-3959(99)00285-7 · Cited by 91 · see citing works

Structural Analysis of the Complement Control Protein (CCP) Modules of GABAB Receptor 1a

Blein, S., Ginham, R., Uhrı́n, D., Smith, B. O., Soares, D. C., Veltel, S., McIlhinney, R. A. J., White, J. H. M., & Barlow, P. N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406540200 · Cited by 65 · see citing works

Roles of GABAB receptor subtypes in presynaptic auto- and heteroreceptor function regulating GABA and glutamate release

Waldmeier, P. C., Kaupmann, K., & Urwyler, S. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0095-7 · Cited by 56 · see citing works

GABAB receptor deficiency causes failure of neuronal homeostasis in hippocampal networks

Vertkin, I., Styr, B., Slomowitz, E., Ofir, N., Shapira, I., Berner, D., Fedorova, T., Laviv, T., Barak-Broner, N., Greitzer-Antes, D., et al. (2015) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1424810112 · Cited by 51 · see citing works

Similar levels of long-term potentiation in amyloid precursor protein -null and wild-type mice in the CA1 region of picrotoxin treated slices

Fitzjohn, S. M., Morton, R. A., Kuenzi, F. M., Davies, C. H., Seabrook, G. R., & Collingridge, G. L. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01204-0 · Cited by 46 · see citing works

Innervation by a GABAergic Neuron Depresses Spontaneous Release in Glutamatergic Neurons and Unveils the Clamping Phenotype of Synaptotagmin-1

Wierda, K. D. B., & Sørensen, J. B. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3934-13.2014 · Cited by 40 · see citing works

Secreted amyloid precursor protein-alpha can restore novel object location memory and hippocampal LTP in aged rats

Xiong, M., Jones, O. D., Peppercorn, K., Ohline, S. M., Tate, W. P., & Abraham, W. C. (2016) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2016.08.002 · Cited by 40 · see citing works

Analysis of the Overall Structure of the Multi-Domain Amyloid Precursor Protein (APP)

Coburger, I., Dahms, S. O., Roeser, D., Gührs, K., Hortschansky, P., & Than, M. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081926 · Cited by 39 · see citing works

Soluble amyloid-β precursor protein binds its cell surface receptor in a cooperative fashion with glypican and syndecan proteoglycans

Reinhard, C., Borgers, M., David, G., & Strooper, B. D. (2013) · Journal of Cell Science · doi:10.1242/jcs.137919 · Cited by 39 · see citing works

<scp> GABA _B </scp> receptor subtypes differentially modulate synaptic inhibition in the dentate gyrus to enhance granule cell output

Foster, J. D., Kitchen, I., Bettler, B., & Chen, Y. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12073 · Cited by 33 · see citing works

Ecto-Fc MS identifies ligand-receptor interactions through extracellular domain Fc fusion protein baits and shotgun proteomic analysis

Savas, J. N., de Wit, J., Comoletti, D., Zemla, R., Ghosh, A., & Yates, J. R. (2014) · Nature Protocols · doi:10.1038/nprot.2014.140 · Cited by 29 · see citing works

GABAB receptor‐mediated inhibition of spontaneous inhibitory synaptic currents in rat midbrain culture.

Rohrbacher, J., Jarolimek, W., Lewen, A., & Misgeld, U. (1997) · The Journal of Physiology · doi:10.1113/jphysiol.1997.sp022055 · Cited by 27 · see citing works

β‐Secretase cleavage is not required for generation of the intracellular C‐terminal domain of the amyloid precursor family of proteins

Frigerio, C. S., Fadeeva, J. V., Minogue, A. M., Citron, M., LEUVEN, F. V., Staufenbiel, M., Paganetti, P., Selkoe, D. J., & Walsh, D. M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07579.x · Cited by 25 · see citing works

Alzheimer disease

Knopman, D. S., Amieva, H., Petersen, R. C., Chételat, G., Holtzman, D. M., Hyman, B. T., Nixon, R. A., & Jones, D. T. (2021) · Nature Reviews Disease Primers · doi:10.1038/s41572-021-00269-y · Cited by 2,606 · see citing works

The Amyloid-β Pathway in Alzheimer’s Disease

Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952 · see citing works

The β-Secretase BACE1 in Alzheimer’s Disease

Hampel, H., Vassar, R., De Strooper, B., Hardy, J., Willem, M., Singh, N., Zhou, J., Yan, R., Vanmechelen, E., De Vos, A., et al. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2020.02.001 · Cited by 694 · see citing works

Bidirectional relationship between sleep and Alzheimer’s disease: role of amyloid, tau, and other factors

Wang, C., & Holtzman, D. M. (2019) · Neuropsychopharmacology · doi:10.1038/s41386-019-0478-5 · Cited by 589 · see citing works

Lipid metabolism and Alzheimer's disease: clinical evidence, mechanistic link and therapeutic promise

Yin, F. (2023) · The FEBS Journal · doi:10.1111/febs.16344 · Cited by 441 · see citing works

Pathological mechanisms and therapeutic strategies for Alzheimer’s disease

Tam, K. Y., & Ju, Y. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.320970 · Cited by 415 · see citing works

Amyloid-beta peptide and tau protein crosstalk in Alzheimer’s disease

Villegas, S., Roda, A., Serra-Mir, G., Montoliu-Gaya, L., & Tiessler, L. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.332127 · Cited by 306 · see citing works

Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterol

Wang, H., Kulas, J. A., Wang, C., Holtzman, D. M., Ferris, H. A., & Hansen, S. B. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2102191118 · Cited by 294 · see citing works

GABAergic dysfunction in excitatory and inhibitory (E/I) imbalance drives the pathogenesis of Alzheimer's disease

Bi, D., Wen, L., Wu, Z., & Shen, Y. (2020) · Alzheimer's &amp; Dementia · doi:10.1002/alz.12088 · Cited by 232 · see citing works

Amyloidosis in Alzheimer’s Disease: Pathogeny, Etiology, and Related Therapeutic Directions

Ma, C., Hong, F., & Yang, S. (2022) · Molecules · doi:10.3390/molecules27041210 · Cited by 243 · see citing works

GABAergic Inhibitory Interneuron Deficits in Alzheimer’s Disease: Implications for Treatment

Xu, Y., Zhao, M., Han, Y., & Zhang, H. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00660 · Cited by 203 · see citing works

A single-nuclei RNA sequencing study of Mendelian and sporadic AD in the human brain

Del-Aguila, J. L., Li, Z., Dube, U., Mihindukulasuriya, K. A., Budde, J. P., Fernandez, M. V., Ibanez, L., Bradley, J., Wang, F., Bergmann, K., et al. (2019) · Alzheimer's Research &amp; Therapy · doi:10.1186/s13195-019-0524-x · Cited by 183 · see citing works

Stimulation of neural stem cell differentiation by circularly polarized light transduced by chiral nanoassemblies

Qu, A., Sun, M., Kim, J., Xu, L., Hao, C., Ma, W., Wu, X., Liu, X., Kuang, H., Kotov, N. A., et al. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-00634-4 · Cited by 171 · see citing works

Tipping the Scales: Peptide-Dependent Dysregulation of Neural Circuit Dynamics in Alzheimer’s Disease

Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161 · see citing works

The basis of cellular and regional vulnerability in Alzheimer’s disease

Mrdjen, D., Fox, E., Bukhari, S., Montine, K., Bendall, S., & Montine, T. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02054-4 · Cited by 133 · see citing works

Liver Dysfunction as a Novel Player in Alzheimer’s Progression: Looking Outside the Brain

Estrada, L. D., Ahumada, P., Cabrera, D., & Arab, J. P. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00174 · Cited by 144 · see citing works

Physiology and pharmacology of amyloid precursor protein

Cho, Y., Bae, H., Okun, E., Arumugam, T. V., & Jo, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108122 · Cited by 145 · see citing works

Preclinical Models of Alzheimer's Disease: Relevance and Translational Validity

Mullane, K., & Williams, M. (2019) · Current Protocols in Pharmacology · doi:10.1002/cpph.57 · Cited by 122 · see citing works

Excitatory-inhibitory imbalance in Alzheimer's disease and therapeutic significance

Varela, E. V., Etter, G., & Williams, S. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.04.010 · Cited by 116 · see citing works

The GABAB Receptor—Structure, Ligand Binding and Drug Development

Evenseth, L. S. M., Gabrielsen, M., & Sylte, I. (2020) · Molecules · doi:10.3390/molecules25133093 · Cited by 118 · see citing works

Molecular mechanisms of metabotropic GABA B receptor function

Shaye, H., Stauch, B., Gati, C., & Cherezov, V. (2021) · Science Advances · doi:10.1126/sciadv.abg3362 · Cited by 111 · see citing works

Alzheimer’s disease beyond amyloid: Can the repetitive failures of amyloid-targeted therapeutics inform future approaches to dementia drug discovery?

Mullane, K., & Williams, M. J. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113945 · Cited by 106 · see citing works

Structural and Biophysical Mechanisms of Class C G Protein-Coupled Receptor Function

Ellaithy, A., González‐Maeso, J., Logothetis, D. E., & Levitz, J. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.07.008 · Cited by 102 · see citing works

Brain foods - the role of diet in brain performance and health

Ekstrand, B., Scheers, N., Rasmussen, M. K., Young, J. F., Ross, A. B., & Landberg, R. (2020) · Nutrition Reviews · doi:10.1093/nutrit/nuaa091 · Cited by 110 · see citing works

The Role of the GABAergic System in Diseases of the Central Nervous System

Zhang, W., Xiong, B., Zhang, L.-Q., Huang, X., Yuan, X., Tian, Y., & Tian, X. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.06.037 · Cited by 96 · see citing works

Trafficking and proteolytic processing of amyloid precursor protein and secretases in Alzheimer's disease development: An up-to-date review

Yuksel, M., & Tacal, Ö. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172415 · Cited by 94 · see citing works

Modulation of Brain Hyperexcitability: Potential New Therapeutic Approaches in Alzheimer’s Disease

Toniolo, S., Sen, A., & Husain, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239318 · Cited by 94 · see citing works

Small heat shock proteins in neurodegenerative diseases

Vendredy, L., Adriaenssens, E., & Timmerman, V. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01101-4 · Cited by 96 · see citing works

Neurophysiological biomarkers using transcranial magnetic stimulation in Alzheimer’s disease and mild cognitive impairment: A systematic review and meta-analysis

Mimura, Y., Nishida, H., Nakajima, S., Tsugawa, S., Morita, S., Yoshida, K., Tarumi, R., Ogyu, K., Wada, M., Kurose, S., et al. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.12.003 · Cited by 85 · see citing works

Synaptic dysfunction in early phases of Alzheimer's Disease

Pelucchi, S., Gardoni, F., Luca, M. D., & Marcello, E. E. (2022) · Handbook of clinical neurology · doi:10.1016/b978-0-12-819410-2.00022-9 · Cited by 88 · see citing works

Neuropathological assessment of the Alzheimer spectrum

Jellinger, K. A. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02232-9 · Cited by 82 · see citing works

Proteotoxicity and Neurodegenerative Diseases

Ruz, C., Alcantud, J. L., Montero, F. V., Durán, R., & Bandrés‐Ciga, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165646 · Cited by 81 · see citing works

Physiological Roles of β-amyloid in Regulating Synaptic Function: Implications for AD Pathophysiology

Cai, W., Li, L., Sang, S., Pan, X., & Zhong, C. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-022-00985-9 · Cited by 83 · see citing works

An Insight into Cellular and Molecular Mechanisms Underlying the Pathogenesis of Neurodegeneration in Alzheimer’s Disease

Ratan, Y., Rajput, A., Maleysm, S., Pareek, A., Jain, V. K., Pareek, A., Kaur, R., & Singh, G. (2023) · Biomedicines · doi:10.3390/biomedicines11051398 · Cited by 87 · see citing works

Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP

García‐González, L., Piłat, D., Baranger, K., & Rivera, S. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00244 · Cited by 81 · see citing works

Modeling the β-secretase cleavage site and humanizing amyloid-beta precursor protein in rat and mouse to study Alzheimer’s disease

Serneels, L., T’Syen, D., Pérez‐Benito, L., Theys, T., Holt, M. G., & Strooper, B. D. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00399-z · Cited by 78 · see citing works

Targeting receptor complexes: a new dimension in drug discovery

Ishoey, M., Clemmensen, L. S., Bredt, D. S., Bettler, B., & Strømgaard, K. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0086-4 · Cited by 78 · see citing works

Knock-in models related to Alzheimer’s disease: synaptic transmission, plaques and the role of microglia

Benítez, D. P., Jiang, S., Wood, J. I., Wang, R., Hall, C. M., Peerboom, C., Wong, N. S. M., Stringer, K. M., Vitanova, K. S., Smith, V. C., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00457-0 · Cited by 79 · see citing works

Amyloid, APP, and Electrical Activity of the Brain

Hefter, D., Ludewig, S., Draguhn, A., & Körte, M. (2019) · The Neuroscientist · doi:10.1177/1073858419882619 · Cited by 76 · see citing works

Dissociation of somatostatin and parvalbumin interneurons circuit dysfunctions underlying hippocampal theta and gamma oscillations impaired by amyloid β oligomers in vivo

Chung, H., Park, K., Jang, H. J., Kohl, M. M., & Kwag, J. (2020) · Brain Structure and Function · doi:10.1007/s00429-020-02044-3 · Cited by 80 · see citing works

Deciphering the neuroprotective and neurogenic potential of soluble amyloid precursor protein alpha (sAPPα)

Dar, N. J., & Glazner, G. W. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03404-x · Cited by 74 · see citing works

Presynaptic failure in Alzheimer's disease

Barthet, G., & Mulle, C. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101801 · Cited by 74 · see citing works

An Expanded Narrative Review of Neurotransmitters on Alzheimer’s Disease: The Role of Therapeutic Interventions on Neurotransmission

Akyuz, E., Arulsamy, A., Aslan, F. S., Sarisözen, B., Guney, B., Hekimoglu, A., Yilmaz, B. N., Retinasamy, T., & Shaikh, M. F. (2025) · Molecular Neurobiology · doi:10.1007/s12035-024-04333-y · Cited by 69 · see citing works

Amyloid-β Peptide Impact on Synaptic Function and Neuroepigenetic Gene Control Reveal New Therapeutic Strategies for Alzheimer’s Disease

Karisetty, B. C., Bhatnagar, A., Armour, E. M., Beaver, M., Zhang, H., & Elefant, F. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.577622 · Cited by 67 · see citing works

Beyond the Ligand: Extracellular and Transcellular G Protein–Coupled Receptor Complexes in Physiology and Pharmacology

Dunn, H. A., Orlandi, C., & Martemyanov, K. A. (2019) · Pharmacological Reviews · doi:10.1124/pr.119.018044 · Cited by 66 · see citing works

Amyloid-β plaque formation and reactive gliosis are required for induction of cognitive deficits in App knock-in mouse models of Alzheimer’s disease

Sakakibara, Y., Sekiya, M., Saito, T., Saido, T. C., & Iijima, K. M. (2019) · BMC Neuroscience · doi:10.1186/s12868-019-0496-6 · Cited by 65 · see citing works

Glia: A major player in glutamate–GABA dysregulation‐mediated neurodegeneration

Sood, A., Kumari, P., Fernandes, V., Khatri, D. K., & Singh, S. B. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24977 · Cited by 60 · see citing works

Functional and Phenotypic Diversity of Microglia: Implication for Microglia-Based Therapies for Alzheimer’s Disease

Xu, Y., Au, N. P. B., & Ma, C. H. E. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.896852 · Cited by 63 · see citing works

Super-resolution microscopy: a closer look at synaptic dysfunction in Alzheimer disease

Padmanabhan, P., Kneynsberg, A., & Götz, J. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00531-y · Cited by 55 · see citing works

Does HIV infection contribute to increased beta-amyloid synthesis and plaque formation leading to neurodegeneration and Alzheimer’s disease?

Fülöp, T., Witkowski, J. M., Larbi, A., Khalil, A., Herbein, G., & Frost, E. H. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-019-00732-3 · Cited by 58 · see citing works

Reversible GABAergic dysfunction involved in hippocampal hyperactivity predicts early-stage Alzheimer disease in a mouse model

Li, Y., Zhu, K., Li, N., Wang, X., Xiao, X., Li, L., Li, L., He, Y., Zhang, J., Wo, J., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00859-8 · Cited by 50 · see citing works

Long-term voluntary exercise inhibited AGE/RAGE and microglial activation and reduced the loss of dendritic spines in the hippocampi of APP/PS1 transgenic mice

Wang, Y., Zhou, Y., Jiang, L. H., Wang, S., Zhu, L., Zhang, S., Yang, H., He, Q., Liu, L., Xie, Y., et al. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114371 · Cited by 55 · see citing works

Symptomatic, Genetic, and Mechanistic Overlaps between Autism and Alzheimer’s Disease

Nadeem, M. S., Hosawi, S. B. I., Alshehri, S., Ghoneim, M. M., Imam, S. S., Murtaza, B. N., & Kazmi, I. A. (2021) · Biomolecules · doi:10.3390/biom11111635 · Cited by 56 · see citing works

Evaluation and targeting of amyloid precursor protein (APP)/amyloid beta (Aβ) axis in amyloidogenic and non-amyloidogenic pathways: A time outside the tunnel

Al-Kuraishy, H. M., Jabir, M. S., Al-Gareeb, A. I., Albuhadily, A. K., Albukhaty, S., Sulaiman, G. M., & Batiha, G. E. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102119 · Cited by 53 · see citing works

Contribution of GABAergic interneurons to amyloid-β plaque pathology in an APP knock-in mouse model

Rice, H. C., Marcassa, G., Chrysidou, I., Horré, K., Young‐Pearse, T. L., Müller, U., Saito, T., Saido, T. C., Vassar, R. J., de Wit, J., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0356-y · Cited by 53 · see citing works

Loss of all three APP family members during development impairs synaptic function and plasticity, disrupts learning, and causes an autism‐like phenotype

Steubler, V., Erdinger, S., Back, M. K., Ludewig, S., Fässler, D., Richter, M., Han, K., Slomianka, L., Amrein, I., von Engelhardt, J., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020107471 · Cited by 52 · see citing works

Differential microRNA expression analyses across two brain regions in Alzheimer’s disease

Dobričić, V., Schilling, M., Schulz, J., Zhu, L., Zhou, C.-W., Fuß, J., Franzenburg, S., Zhu, L., Parkkinen, L., Lill, C. M., et al. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02108-4 · Cited by 52 · see citing works

Amyloid-Beta Mediates Homeostatic Synaptic Plasticity

Galanis, C., Fellenz, M., Becker, D., Bold, C., Lichtenthaler, S., Müller, U. C., Deller, T., & Vlachos, A. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1820-20.2021 · Cited by 38 · see citing works

Opposite changes in APP processing and human Aβ levels in rats carrying either a protective or a pathogenic APP mutation

Tambini, M. D., Norris, K. A., & D'adamio, L. (2020) · eLife · doi:10.7554/elife.52612 · Cited by 47 · see citing works

Neurexins regulate presynaptic GABAB-receptors at central synapses

Luo, F., Sclip, A., Merrill, S. A., & Südhof, T. C. (2021) · Nature Communications · doi:10.1038/s41467-021-22753-5 · Cited by 49 · see citing works

Reduction in the neuronal surface of post and presynaptic GABABreceptors in the hippocampus in a mouse model of Alzheimer's disease

Martín‐Belmonte, A., Aguado, C., Alfaro‐Ruiz, R., Moreno‐Martínez, A. E., de la Ossa, L., Hernández, J. M., Buisson, A., Früh, S., Bettler, B., Shigemoto, R., et al. (2019) · Brain Pathology · doi:10.1111/bpa.12802 · Cited by 48 · see citing works

Brothers in Arms: ProBDNF/BDNF and sAPPα/Aβ-Signaling and Their Common Interplay with ADAM10, TrkB, p75NTR, Sortilin, and sorLA in the Progression of Alzheimer’s Disease

Eggert, S., Kins, S., Endres, K., & Brigadski, T. (2022) · Biological Chemistry · doi:10.1515/hsz-2021-0330 · Cited by 46 · see citing works

ELFN2 is a postsynaptic cell adhesion molecule with essential roles in controlling group III mGluRs in the brain and neuropsychiatric behavior

Dunn, H. A., Zucca, S., Dao, M. T., Orlandi, C., & Martemyanov, K. A. (2019) · Molecular Psychiatry · doi:10.1038/s41380-019-0512-3 · Cited by 45 · see citing works

Knockdown of Amyloid Precursor Protein: Biological Consequences and Clinical Opportunities

Gabriele, R. M. C., Abel, E., Fox, N. C., Wray, S., & Arber, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.835645 · Cited by 44 · see citing works

Neuropathology of the Alzheimer's continuum: an update

Jellinger, K. A. (2020) · Free Neuropathology · doi:10.17879/freeneuropathology-2020-3050 · Cited by 45 · see citing works

Morphological and Molecular Profiling of Amyloid-β Species in Alzheimer’s Pathogenesis

Almeida, Z. L., Vaz, D. C., & Brito, R. M. M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04543-4 · Cited by 45 · see citing works

Next Generation Precision Medicine: CRISPR-mediated Genome Editing for the Treatment of Neurodegenerative Disorders

Raikwar, S. P., Kikkeri, N. S., Sakuru, R. C., Saeed, D., Zahoor, H., Premkumar, K., Mentor, S., Thangavel, R., Dubova, I., Ahmed, M. E., et al. (2019) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-019-09849-y · Cited by 47 · see citing works

The Interaction Between Contactin and Amyloid Precursor Protein and Its Role in Alzheimer's Disease.

Bamford, R., Widagdo, J., Takamura, N., Eve, M., Anggono, V., & Oguro-Ando, A. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.10.006 · Cited by 37 · see citing works

The fusiform gyrus exhibits an epigenetic signature for Alzheimer’s disease

Ma, D., Fetahu, I. S., Wang, M., Fang, R., Li, J., Liu, H., Gramyk, T., Iwanicki, I. J., Gu, S., Xu, W., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-020-00916-3 · Cited by 43 · see citing works

Acteoside exerts neuroprotection effects in the model of Parkinson's disease via inducing autophagy: Network pharmacology and experimental study

Aimaiti, M., Wumaier, A., Aisa, Y., Zhang, Y., Xirepu, X., Aibaidula, Y., Lei, X., Chen, Q., Feng, X., & Mi, N. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174136 · Cited by 43 · see citing works

GABAB Receptor Chemistry and Pharmacology: Agonists, Antagonists, and Allosteric Modulators

Nieto, A., Bailey, T., Kaczanowska, K., & McDonald, P. H. (2021) · Current topics in behavioral neurosciences · doi:10.1007/7854_2021_232 · Cited by 43 · see citing works

Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterolPreprint

Wang, H., Kulas, J. A., Ferris, H. A., & Hansen, S. B. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.18.159632 · Cited by 43 · see citing works

The organizing principle of GABAB receptor complexes: Physiological and pharmacological implications

Fritzius, T., & Bettler, B. (2019) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13241 · Cited by 41 · see citing works

Therapeutic effects of phlorotannins in the treatment of neurodegenerative disorders

Kwon, S. Y., Kwon, O. I., Hwang, H. J., Shin, H., & Yang, S. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1193590 · Cited by 43 · see citing works

Density of GABAB Receptors Is Reduced in Granule Cells of the Hippocampus in a Mouse Model of Alzheimer’s Disease

Martín‐Belmonte, A., Aguado, C., Alfaro‐Ruiz, R., Moreno‐Martínez, A. E., de la Ossa, L., Hernández, J. M., Buisson, A., Shigemoto, R., Fukazawa, Y., & Luján, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072459 · Cited by 38 · see citing works

Hydrogen-rich water ameliorates neuropathological impairments in a mouse model of Alzheimer's disease through reducing neuroinflammation and modulating intestinal microbiota

Lin, Y., Shi, Q., Zhang, L., Yue, C.-P., He, Z.-J., Li, X.-X., He, Q., Liu, Q., & Du, X. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.317992 · Cited by 39 · see citing works

Finding memo: versatile interactions of the VPS10p-Domain receptors in Alzheimer’s disease

Salašová, A., Monti, G., Andersen, O. M., & Nykjær, A. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00576-2 · Cited by 35 · see citing works

Novel Therapeutic Strategies in Alzheimer’s Disease: Pitfalls and Challenges of Anti-Amyloid Therapies and Beyond

Tondo, G., Marchi, F. D., Bonardi, F., Menegon, F., Verrini, G., Aprile, D., Anselmi, M., Mazzini, L., & Comi, C. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13113098 · Cited by 43 · see citing works

An agnostic reevaluation of the amyloid cascade hypothesis of Alzheimer's disease pathogenesis: The role of APP homeostasis

Caselli, R. J., Knopman, D. S., & Bu, G. (2020) · Alzheimer s & Dementia · doi:10.1002/alz.12124 · Cited by 36 · see citing works

The Expression and Localisation of G-Protein-Coupled Inwardly Rectifying Potassium (GIRK) Channels Is Differentially Altered in the Hippocampus of Two Mouse Models of Alzheimer’s Disease

Alfaro‐Ruiz, R., Martín‐Belmonte, A., Aguado, C., Hernández, F., Moreno‐Martínez, A. E., Ávila, J., & Luján, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011106 · Cited by 36 · see citing works

The vexing complexity of the amyloidogenic pathway

Castro, M., Hadziselimovic, A., & Sanders, C. R. (2019) · Protein Science · doi:10.1002/pro.3606 · Cited by 36 · see citing works

Amyloidosis is associated with thicker myelin and increased oligodendrogenesis in the adult mouse brain

Ferreira, S., Pitman, K. A., Wang, S., Summers, B. S., Bye, N., Young, K. M., & Cullen, C. L. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24672 · Cited by 36 · see citing works

Amyloid Precursor Protein (APP) Controls the Expression of the Transcriptional Activator Neuronal PAS Domain Protein 4 (NPAS4) and Synaptic GABA Release

Opsomer, R., Contino, S., Perrin, F., Gualdani, R., Tasiaux, B., Doyen, P. J., Vergouts, M., Vrancx, C., Doshina, A., Pierrot, N., et al. (2020) · eNeuro · doi:10.1523/eneuro.0322-19.2020 · Cited by 34 · see citing works

Herpes Zoster virus infection and the risk of developing dementia: A systematic review and meta-analysis

Elhalag, R. H., Motawea, K. R., Talat, N. E., Rouzan, S. S., Reyad, S. M., Elsayed, S. M., Chèbl, P., Abowafia, M., & Shah, J. (2023) · Medicine · doi:10.1097/md.0000000000034503 · Cited by 34 · see citing works

A Novel CCK Receptor GPR173 Mediates Potentiation of GABAergic Inhibition

He, L. S., Shi, H., Zhang, G., Peng, Y., Ghosh, A., Zhang, M., Hu, X., Liu, C., Shao, Y., Wang, S., et al. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.2035-22.2023 · Cited by 32 · see citing works

GABA and glutamate moderate beta-amyloid related functional connectivity in cognitively unimpaired old-aged adults

Quevenco, F. C., Schreiner, S. J., Preti, M. G., Bergen, J. M. G. V., Kirchner, T., Wyss, M. T., Steininger, S. C., Gietl, A. F., Leh, S. E., Buck, A., et al. (2019) · NeuroImage Clinical · doi:10.1016/j.nicl.2019.101776 · Cited by 32 · see citing works

Amyloid precursor protein and its interacting proteins in neurodevelopment

Chau, D. D., Ng, L. L.-H., Zhai, Y., & Lau, K. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221527 · Cited by 31 · see citing works

Amyloid Precursor Protein (APP) and GABAergic Neurotransmission

Tang, B. L. (2019) · Cells · doi:10.3390/cells8060550 · Cited by 31 · see citing works

Controversial Properties of Amyloidogenic Proteins and Peptides: New Data in the COVID Era

Surguchov, A. P., Emamzadeh, F. N., Titova, M., & Surguchev, A. A. (2023) · Biomedicines · doi:10.3390/biomedicines11041215 · Cited by 31 · see citing works

Family C G-Protein-Coupled Receptors in Alzheimer’s Disease and Therapeutic Implications

Prà, I. D., Armato, U., & Chiarini, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01282 · Cited by 31 · see citing works

Somatostatin and the pathophysiology of Alzheimer’s disease

Almeida, V. N. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102270 · Cited by 30 · see citing works

APP-Mediated Signaling Prevents Memory Decline in Alzheimer’s Disease Mouse Model

Deyts, C., Clutter, M., Pierce, N., Chakrabarty, P., Ladd, T. B., GODDI, A. A., Rosario, A. M., Cruz, P. E., Vetrivel, K. S., Wagner, S. L., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.087 · Cited by 30 · see citing works

Disrupted neural correlates of anesthesia and sleep reveal early circuit dysfunctions in Alzheimer models

Zarhin, D., Atsmon, R., Ruggiero, A., Baeloha, H., Shoob, S., Scharf, O., Heim, L. R., Buchbinder, N., Shinikamin, O., Shapira, I., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110268 · Cited by 30 · see citing works

Lack of APP and APLP2 in GABAergic Forebrain Neurons Impairs Synaptic Plasticity and Cognition

Mehr, A., Hick, M., Ludewig, S., Müller, M., Herrmann, U., von Engelhardt, J., Wolfer, D. P., Körte, M., & Müller, U. (2020) · Cerebral Cortex · doi:10.1093/cercor/bhaa025 · Cited by 27 · see citing works

Overexpression of wild-type human amyloid precursor protein alters GABAergic transmission

Kreis, A., Desloovere, J., Suelves, N., Pierrot, N., Yerna, X., Issa, F., Schakman, O., Gualdani, R., de Clippele, M., Tajeddine, N., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-97144-3 · Cited by 29 · see citing works

Infection‐induced endothelial amyloids impair memory

Balczon, R., Pittet, J., Wagener, B., Moser, S., Voth, S., Vorhees, C., Williams, M. T., Bridges, J. P., Alvarez, D., Koloteva, A., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900322r · Cited by 25 · see citing works

Amyloid-β1–43 cerebrospinal fluid levels and the interpretation of APP, PSEN1 and PSEN2 mutations

Perrone, F., Bjerke, M., Hens, E., Sieben, A., Timmers, M., Roeck, A. D., Vandenberghe, R. R., Sleegers, K., Martin, J., Deyn, P. P. D., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00676-5 · Cited by 28 · see citing works

MDGA1 negatively regulates amyloid precursor protein–mediated synapse inhibition in the hippocampus

Kim, J., Kim, S., Kim, H., Hwang, I.-W., Bae, S., Karki, S., Kim, D., Ogelman, R., Bang, G., Kim, J. Y., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2115326119 · Cited by 28 · see citing works

Intercellular signaling by ectodomain shedding at the synapse

Martin‐de‐Saavedra, M. D., Santos, M. D., & Penzes, P. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.03.004 · Cited by 24 · see citing works

Reduction of Dendritic Inhibition in CA1 Pyramidal Neurons in Amyloidosis Models of Early Alzheimer’s Disease

Ruiter, M., Herstel, L. J., & Wierenga, C. J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200527 · Cited by 25 · see citing works

A physiological function for sAPP?

Hurtley, S. M. (2019) · Science · doi:10.1126/science.363.6423.137-m

Secreted APP Modulates Synaptic Activity: A Novel Target for Therapeutic Intervention?

Haass, C., & Willem, M. (2019) · Neuron · doi:10.1016/j.neuron.2019.01.058 · Cited by 18 · see citing works

Molecular mechanism of secreted amyloid-β precursor protein in binding and modulating GABA B R1a

Feng, M., Song, Y., Chen, S. H., Zhang, Y., & Zhou, R. (2021) · Chemical Science · doi:10.1039/d0sc06946a · Cited by 13 · see citing works

[O1–07–06]: SOLUBLE AMYLOID PRECURSOR PROTEIN IS AN ISOFORM‐SPECIFIC GABA(B) RECEPTOR LIGAND THAT SUPPRESSES SYNAPTIC RELEASE PROBABILITY

Rice, H. C., Wierda, K. D. B., Frère, S. G. A., Vertkin, I., Molle, I. V., Ranaivoson, F. M., Comoletti, D., Savas, J. N., Slutsky, I., Strooper, B. D., et al. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.07.075 · Cited by 2 · see citing works

P1‐185: SECRETED AMYLOID PRECURSOR PROTEIN IS A GABABR1A LIGAND THAT SUPPRESSES SYNAPTIC VESICLE RELEASE

Rice, H. C., Wierda, K. D. B., Frère, S. G. A., Vertkin, I., Molle, I. V., Ranaivoson, F. M., Comoletti, D., Savas, J. N., Slutsky, I., Strooper, B. D., et al. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.06.189 · Cited by 1 · see citing works