The neuropeptide PACAP promotes ?‐secretase pathway for processing Alzheimer amyloid precursor protein

A new generation of Ca2+ indicators with greatly improved fluorescence properties.

Grynkiewicz, G., Poenie, M., & Tsien, R. Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83641-4 · Cited by 21,722 · see citing works

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 · see citing works

Differential signal transduction by five splice variants of the PACAP receptor

Spengler, D., Waeber, C., Pantaloni, C., Holsboer, F., Bockaert, J., Seeburg, P. H., & Journot, L. (1993) · Nature · doi:10.1038/365170a0 · Cited by 1,182 · see citing works

Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., & Fahrenholz, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3922 · Cited by 1,132 · see citing works

Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: From Structure to Functions

Vaudry, D., Gonzalez, B. J., Basille, M., Yon, L., Fournier, A., & Vaudry, H. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01449-2 · Cited by 1,120 · see citing works

Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein Precursor

Buxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27765 · Cited by 933 · see citing works

Release of Alzheimer Amyloid Precursor Derivatives Stimulated by Activation of Muscarinic Acetylcholine Receptors

Nitsch, R. M., Slack, B. E., Wurtman, R. J., & Growdon, J. H. (1992) · Science · doi:10.1126/science.1411529 · Cited by 898 · see citing works

Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein

Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I. M., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 795 · see citing works

The Origin and Function of the Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP)/Glucagon Superfamily

Sherwood, N. M., Krueckl, S. L., & McRory, J. E. (2000) · Endocrine Reviews · doi:10.1210/edrv.21.6.0414 · Cited by 727 · see citing works

The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion

Hundhausen, C., Misztela, D., Berkhout, T. A., BROADWAY, N. M., Säftig, P., Reiß, K., Hartmann, D., Fahrenholz, F., Postina, R., Matthews, V. B., et al. (2003) · Blood · doi:10.1182/blood-2002-12-3775 · Cited by 714 · see citing works

Structure and function of phosphoinositide 3-kinases

Wymann, M. P., & Pirola, L. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s0005-2760(98)00139-8 · Cited by 662 · see citing works

A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model

Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638 · see citing works

Perspectives on Pituitary Adenylate Cyclase Activating Polypeptide (PACAP) in the Neuroendocrine, Endocrine, and Nervous Systems

Arimura, A. (1998) · The Japanese Journal of Physiology · doi:10.2170/jjphysiol.48.301 · Cited by 512 · see citing works

Phosphoinositide 3-kinase signalling – which way to target?

Wymann, M. P., Zvelebil, M., & Laffargue, M. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00163-9 · Cited by 410 · see citing works

Diverse Cell Surface Protein Ectodomains Are Shed by a System Sensitive to Metalloprotease Inhibitors

Arribas, J., Coodly, L. R., Vollmer, P., Kishimoto, T., Rose‐John, S., & Massagué, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11376 · Cited by 391 · see citing works

Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone

Caillé, I., Allinquant, B., Dupont, E., Bouillot, C., Langer, A., Müller, U., & Prochiantz, A. (2004) · Development · doi:10.1242/dev.01103 · Cited by 388 · see citing works

Transmembrane-4 Superfamily Proteins Associate with Activated Protein Kinase C (PKC) and Link PKC to Specific β1 Integrins

Zhang, X. A., Bontrager, A. L., & Hemler, M. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102156200 · Cited by 361 · see citing works

Metalloproteinase Inhibitors for the Disintegrin-Like Metalloproteinases ADAM10 and ADAM17 that Differentially Block Constitutive and Phorbol Ester-Inducible Shedding of Cell Surface Molecules

Ludwig, A., Hundhausen, C., Lambert, M. H., BROADWAY, N. M., Andrews, R. K., Bickett, D. M., Leesnitzer, M. A., & Becherer, J. D. (2005) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207053258488 · Cited by 356 · see citing works

Two High Affinity Binding Sites for Pituitary Adenylate Cyclase-Activating Polypeptide Have Different Tissue Distributions*

Shivers, B. D., Görcs, T. J., Gottschall, P. E., & Arimura, A. (1991) · Endocrinology · doi:10.1210/endo-128-6-3055 · Cited by 321 · see citing works

The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein–coupled receptors

Yan, Y., Shirakabe, K., & Werb, Z. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200112026 · Cited by 317 · see citing works

A Neuropeptide Gene Defined by the Drosophila Memory Mutant amnesiac

Feany, M. Β., & Quinn, W. G. (1995) · Science · doi:10.1126/science.7754370 · Cited by 269 · see citing works

ADAM10‐mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles

Gutwein, P., Mechtersheimer, S., Riedle, S., Stoeck, A., Gast, D., Joumaa, S., Zentgraf, H., Fogel, M., & Altevogt, P. (2002) · The FASEB Journal · doi:10.1096/fj.02-0430fje · Cited by 225 · see citing works

Alternative Splicing in the N-terminal Extracellular Domain of the Pituitary Adenylate Cyclase-activating Polypeptide (PACAP) Receptor Modulates Receptor Selectivity and Relative Potencies of PACAP-27 and PACAP-38 in Phospholipase C Activation

Pantaloni, C., Brabet, P., Bilanges, B., Dumuis, A., Houssami, S., Spengler, D., Bockaert, J., & Journot, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.22146 · Cited by 223 · see citing works

Prevention of ischemia-induced death of hippocampal neurons by pituitary adenylate cyclase activating polypeptide

Uchida, D., Arimura, A., Somogyvári-Vigh, A., Shioda, S., & Banks, W. A. (1996) · Brain Research · doi:10.1016/0006-8993(96)00716-0 · Cited by 215 · see citing works

The Non-Amyloidogenic Pathway: Structure and Function of α-Secretases

Kojro, E., & Fahrenholz, F. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_5 · Cited by 211 · see citing works

Dynamic Regulation of a GPCR-Tetraspanin-G Protein Complex on Intact Cells: Central Role of CD81 in Facilitating GPR56-Gα_q/11Association

Little, K. D., Hemler, M. E., & Stipp, C. S. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-12-0886 · Cited by 211 · see citing works

Cleavage of Alzheimer's Amyloid Precursor Protein by α-Secretase Occurs at the Surface of Neuronal Cells

Parvathy, S., Hussain, I., Karran, E. H., Turner, A. J., & Hooper, N. M. (1999) · Biochemistry · doi:10.1021/bi9906827 · Cited by 200 · see citing works

A Novel Role for Phosphatidylinositol 3-Kinase β in Signaling from G Protein-coupled Receptors to Akt

Murga, C., Fukuhara, S., & Gutkind, J. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12069 · Cited by 199 · see citing works

Secreted β-Amyloid Precursor Protein Counteracts the Proapoptotic Action of Mutant Presenilin-1 by Activation of NF-κB and Stabilization of Calcium Homeostasis

Guo, Q., Robinson, N., & Mattson, M. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12341 · Cited by 196 · see citing works

Impairment of Mossy Fiber Long-Term Potentiation and Associative Learning in Pituitary Adenylate Cyclase Activating Polypeptide Type I Receptor-Deficient Mice

Otto, C., Kovalchuk, Y., Wolfer, D. P., Gass, P., Martin, M., Zuschratter, W., Gröne, H. J., Kellendonk, C., Tronche, F., Maldonado, R. J., et al. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-15-05520.2001 · Cited by 191 · see citing works

Cloning and Characterization of the Signal Transduction of Four Splice Variants of the Human Pituitary Adenylate Cyclase Activating Polypeptide Receptor

Pisegna, J. R., & Wank, S. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17267 · Cited by 187 · see citing works

Distribution of vasoactive intestinal peptide and pituitary adenylate cyclase‐activating polypeptide receptors (VPAC1, VPAC2, and PAC1 receptor) in the rat brain

Joo, K. M., Chung, Y. H., Kim, M., Nam, R. H., Lee, B. L., Lee, K. H., & Ik, C. (2004) · The Journal of Comparative Neurology · doi:10.1002/cne.20231 · Cited by 186 · see citing works

Molecular Cloning of a Novel Variant of the Pituitary Adenylate Cyclase-activating Polypeptide (PACAP) Receptor That Stimulates Calcium Influx by Activation of L-type Calcium Channels

Chatterjee, T. K., Sharma, R. V., & Fisher, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.32226 · Cited by 160 · see citing works

Binding sites for pituitary adenyloate cyclase activating polypeptide (PACAP): comparison with vasoactive intestinal polypeptide (VIP) binding site localization in rat brain sections

Masuo, Y., Ohtaki, T., Masuda, Y., Tsuda, M., & Fujino, M. (1992) · Brain Research · doi:10.1016/0006-8993(92)90430-h · Cited by 160 · see citing works

Tetraspanin proteins as organisers of membrane microdomains and signalling complexes

Yunta, M., & Lazo, P. A. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00147-x · Cited by 149 · see citing works

Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines

Zimmermann, M., Gardoni, F., Marcello, E. E., Colciaghi, F., Borroni, B., Padovani, A., Cattabeni, F., & Luca, M. D. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02680.x · Cited by 132 · see citing works

The Search for α-Secretase and its Potential as a Therapeutic Approach to Alzheimer's Disease

Hooper, N. M., & Turner, A. J. (2002) · Current Medicinal Chemistry · doi:10.2174/0929867023370121 · Cited by 127 · see citing works

ADAM10 Mediates Ectodomain Shedding of the Betacellulin Precursor Activated by p-Aminophenylmercuric Acetate and Extracellular Calcium Influx

Sanderson, M. P., Erickson, S. N., Gough, P. J., Garton, K. J., Wille, P. T., Raines, E. W., Dunbar, A. J., & Dempsey, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408804200 · Cited by 107 · see citing works

Passage of VIP / PACAP / Secretin Family Across the Blood-Brain Barrier: Therapeutic Effects

Doğrukol‐Ak, D., Töre, F., & Tunçel, N. (2004) · Current Pharmaceutical Design · doi:10.2174/1381612043384934 · Cited by 106 · see citing works

Human oxytocin receptors in cholesterol‐rich vs. cholesterol‐poor microdomains of the plasma membrane

Gimpl, G., & Fahrenholz, F. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01280.x · Cited by 95 · see citing works

Properties and distribution of receptors for pituitary adenylate cyclase activating peptide (PACAP) in rat brain and spinal cord

Cauvin, A. J., Robberecht, P., NEEF, P. D., Gourlet, P., Vandermeers, A., Vandermeers‐Piret, M., & Christophe, J. (1991) · Regulatory Peptides · doi:10.1016/0167-0115(91)90478-y · Cited by 93 · see citing works

The 38-Amino-Acid Form of Pituitary Adenylate Cyclase-Activating Polypeptide Induces Neurite Outgrowth in PC12 Cells that Is Dependent on Protein Kinase C and Extracellular Signal-Regulated Kinase but not on Protein Kinase A, Nerve Growth Factor Receptor Tyrosine Kinase, p21ras G protein, and pp60c-srcCytoplasmic Tyrosine Kinase

Lazarovici, P., Jiang, H., & Fink, D. W. (1998) · Molecular Pharmacology · doi:10.1124/mol.54.3.547 · Cited by 91 · see citing works

Neurotrophic and Neuroprotective Effects of hAPP in Transgenic Micea

Mucke, L., Abraham, C. R., & Masliah, E. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34405.x · Cited by 87 · see citing works

Metabolism of Alzheimer beta-amyloid precursor protein: regulation by protein kinase A in intact cells and in a cell-free system.

Xu, H., Sweeney, D. A., Greengard, P., & Gandy, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4081 · Cited by 84 · see citing works

Pituitary Adenylate Cyclase‐Activating Polypeptide (PACAP) Stimulates Adenylyl Cyclase and Phospholipase C Activity in Rat Cerebellar Neuroblasts

Basille, M., Gonzalez, B. J., Desrues, L., Demas, M., Fournier, A., & Vaudry, H. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65031318.x · Cited by 76 · see citing works

Recombinant human amyloid precursor‐like protein 2 (APLP2) expressed in the yeast Pichia pastoris can stimulate neurite outgrowth

Cappai, R., Mok, S. S., Galatis, D., Tucker, D. F., Henry, A., Beyreuther, K. T., Small, D. H., & Masters, C. L. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01635-4 · Cited by 64 · see citing works

Pituitary Adenylate Cyclase-Activating Polypeptide Hormone (PACAP) at Very Low Dosages Improves Memory in the Rat

Sacchetti, B., Lorenzini, C. A., Baldi, E., Bucherelli, C., Roberto, M., Tassoni, G., & Brunelli, M. (2001) · Neurobiology of Learning and Memory · doi:10.1006/nlme.2001.4014 · Cited by 63 · see citing works

Investigation and Characterization of Receptors for Pituitary Adenylate Cyclase-Activating Polypeptide in Human Brain by Radioligand Binding and Chemical Cross-Linking

Suda, K., Smith, D. M., Ghatei, M. A., Murphy, J. K., & Bloom, S. R. (1991) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-72-5-958 · Cited by 58 · see citing works

The Phosphatidylinositol 3‐Kinase Inhibitor Wortmannin Alters the Metabolism of the Alzheimer's Amyloid Precursor Protein

Petanceska, S. S., & Gandy, S. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0732316.x · Cited by 57 · see citing works

Pituitary adenylate cyclase activating polypeptide (PACAP) stimulates mitogen-activated protein kinase (MAPK) in cultured rat astrocytes

Moroo, I., Tatsuno, I., Uchida, D., Tanaka, T., Saito, J., Saito, Y., & Hirai, A. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00291-1 · Cited by 56 · see citing works

Receptor occupancy and adenylate cyclase activation in AR 4-2J rat pancreatic acinar cell membranes by analogs of pituitary adenylate cyclase-activating peptides amino-terminally shortened or modified at position 1, 2, 3, 20, or 21.

Robberecht, P., Gourlet, P., NEEF, P. D., Woussen-Colle, M. C., Vandermeers-Piret, M.-C., Vandermeers, A., & Christophe, J. (1992) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)08921-7 · Cited by 54 · see citing works

Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase Cα, src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C

Canet-Aviles, R., Anderton, M. J., Hooper, N. M., Turner, A. J., & Vaughan, P. F. T. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(02)00184-5 · Cited by 52 · see citing works

Structure−Activity Relationship of Hydroxamate-Based Inhibitors on the Secretases that Cleave the Amyloid Precursor Protein, Angiotensin Converting Enzyme, CD23, and Pro-Tumor Necrosis Factor-α

Parkin, E. T., Trew, A. J., Christie, G., Faller, A., Mayer, R. J., Turner, A. J., & Hooper, N. M. (2002) · Biochemistry · doi:10.1021/bi015936e · Cited by 52 · see citing works

Neuroprotective Effects of PACAP38 in a Rat Model of Transient Focal Ischemia under Various Experimental Conditions

Reglődi, D., Somogyvári-Vigh, A., Vigh, S., Maderdrut, J. L., & Arimura, A. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06958.x · Cited by 47 · see citing works

Intracellular Cyclic AMP Inhibits Constitutive and Phorbol Ester‐Stimulated Secretory Cleavage of Amyloid Precursor Protein

Efthimiopoulos, S., Punj, S., Manolopoulos, V. G., Pangalos, M. N., Wang, G. P., Refolo, L. M., & Robakis, N. K. R. K. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67020872.x · Cited by 45 · see citing works

A Dominant Role for the Raf-MEK Pathway in Forskolin, 12-O-Tetradecanoyl-phorbol Acetate, and Platelet-Derived Growth Factor-Induced CREB (cAMP-Responsive Element-Binding Protein) Activation, Uncoupled from Serine 133 Phosphorylation in NIH 3T3 Cells

Seternes, O. M., Johansen, B., & Moens, U. L. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.7.0293 · Cited by 42 · see citing works

Phosphatidylinositol 3′‐OH kinase and protein kinase A pathways mediate the anti‐apoptotic effect of pituitary adenylyl cyclase‐activating polypeptide in cultured cerebellar granule neurons: modulation by ethanol

Bhave, S. V., & Hoffman, P. L. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02167.x · Cited by 40 · see citing works

Metabotropic Glutamate Receptors Increase Amyloid Precursor Protein Processing in Astrocytes: Inhibition by Cyclic AMP

Lee, R. K. K., & Wurtman, R. J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68051830.x · Cited by 40 · see citing works

Activity of α‐Secretase as the Common Final Effector of Protein Kinase C‐Dependent and ‐Independent Modulation of Amyloid Precursor Protein Metabolism

Racchi, M., Solano, D. C., Sironi, M., & Govoni, S. M. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722464.x · Cited by 37 · see citing works

PACAP activates PKA, PKC and Ca2+ signaling cascades in rat neuroepithelial cells

Zhou, C. J., Yada, T., Kohno, D., Kikuyama, S., Suzuki, R., Mizushima, H., & Shioda, S. (2001) · Peptides · doi:10.1016/s0196-9781(01)00437-5 · Cited by 34 · see citing works

PACAP activates Rac1 and synergizes with NGF to activate ERK1/2, thereby inducing neurite outgrowth in PC12 cells

Sakai, Y., Hashimoto, H., Shintani, N., Katoh, H., Negishi, M., Kawaguchi, C., Kasai, A., & Baba, A. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2003.12.013 · Cited by 32 · see citing works

PACAP promotes sensory neuron differentiation: blockade by neurotrophic factors

Nielsen, K. M., Chaverra, M., Hapner, S. J., Nelson, B. R., Todd, V. J., Zigmond, R. E., & Lefcort, F. B. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2003.12.004 · Cited by 29 · see citing works

Maxadilan interacts with receptors for pituitary adenylyl cyclase activating peptide in human SH-SY5Y and SK-N-MC neuroblastoma cells

Eggenberger, M., Born, W., Zimmermann, U., Lerner, E. A., Ja, F., & Muff, R. (1999) · Neuropeptides · doi:10.1054/npep.1999.0004 · Cited by 14 · see citing works

Activation of MAPKs by G Protein-Coupled Receptors

Crespo, P., & Gutkind, J. S. (2004) · Humana Press eBooks · doi:10.1385/1-59259-671-1:203 · Cited by 9 · see citing works

Untitled work

(2000) · doi:10.1002/1531-8249(200012)48:6

Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery

Vaudry, D., Falluel‐Morel, A., Bourgault, S., Basille, M., Burel, D., Wurtz, O., Fournier, A., Chow, B., Hashimoto, H., Galas, L., et al. (2009) · Pharmacological Reviews · doi:10.1124/pr.109.001370 · Cited by 1,060 · see citing works

ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons

Kuhn, 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 · see citing works

ADAM-17: the enzyme that does it all

Gooz, M. B. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003628015 · Cited by 413 · see citing works

Serotonin signaling is associated with lower amyloid-β levels and plaques in transgenic mice and humans

Cirrito, J. R., Disabato, B. M., Restivo, J. L., Verges, D. K., Goebel, W. D., Sathyan, A., Hayreh, D., D'Angelo, G., Benzinger, T., Yoon, H., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107411108 · Cited by 370 · see citing works

Oxidative stress activates a positive feedback between the γ‐ and β‐secretase cleavages of the β‐amyloid precursor protein

Tamagno, E., Guglielmotto, M., Aragno, M., Borghi, R., Autelli, R., Giliberto, L., Muraca, G., Danni, O., Zhu, X., Smith, M. A., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05072.x · Cited by 338 · see citing works

The role of G protein-coupled receptors in the pathology of Alzheimer's disease

Thathiah, A., & De Strooper, B. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2977 · Cited by 288 · see citing works

Receptor for Advanced Glycation End Products Is Subjected to Protein Ectodomain Shedding by Metalloproteinases

Zhang, L., Bukulin, M., Kojro, E., Roth, A., Metz, V. V., Fahrenholz, F., Nawroth, P. P., Bierhaus, A., & Postina, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806948200 · Cited by 285 · see citing works

Docosahexaenoic Acid-Derived Neuroprotectin D1 Induces Neuronal Survival via Secretase- and PPARγ-Mediated Mechanisms in Alzheimer's Disease Models

Zhao, Y., Calon, F., Julien, C., Winkler, J. W., Petasis, N. A., Lukiw, W. J., & Bazan, N. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015816 · Cited by 243 · see citing works

Regulated intramembrane proteolysis - lessons from amyloid precursor protein processing

Lichtenthaler, S. F., Haass, C., & Steiner, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07248.x · Cited by 230 · see citing works

Concerted changes in transcripts in the prefrontal cortex precede neuropathology in Alzheimer's disease

Bossers, K., Wirz, K. T. S., Meerhoff, G. F., Essing, A. H. W., van Dongen, J. W., Houba, P., Kruse, C. G., Verhaagen, J., & Swaab, D. F. (2010) · Brain · doi:10.1093/brain/awq258 · Cited by 230 · see citing works

The alpha secretase ADAM10: A metalloprotease with multiple functions in the brain

Säftig, P., & Lichtenthaler, S. F. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.10.003 · Cited by 209 · see citing works

Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development

Robichaux, W. G., & Cheng, X. (2018) · Physiological Reviews · doi:10.1152/physrev.00025.2017 · Cited by 208 · see citing works

Alpha-secretase in Alzheimer’s disease: molecular identity, regulation and therapeutic potential

Lichtenthaler, S. F. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07081.x · Cited by 207 · see citing works

Age-dependent Accumulation of Soluble Amyloid β (Aβ) Oligomers Reverses the Neuroprotective Effect of Soluble Amyloid Precursor Protein-α (sAPPα) by Modulating Phosphatidylinositol 3-Kinase (PI3K)/Akt-GSK-3β Pathway in Alzheimer Mouse Model

Jiménez, S., Torres, M., Vizuete, M., Sanchez-Varo, R. M., Sánchez‐Mejías, E., Trujillo‐Estrada, L., Carmona‐Cuenca, I., Caballero, C., Ruano, D., Gutiérrez, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209718 · Cited by 190 · see citing works

The Role of ADAM10 in Alzheimer’s Disease

Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160 · see citing works

Etazolate, a neuroprotective drug linking GABAA receptor pharmacology to amyloid precursor protein processing

Marcade, M., Bourdin, J., Loiseau, N., Peillon, H., Rayer, A., Drouin, D., Schweighoffer, F., & Désiré, L. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05396.x · Cited by 155 · see citing works

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Zussy, C., Brureau, A., Delair, B., Marchal, S., Keller, E., IXART, G., Naert, G., Meunier, J., Chevallier, N., Maurice, T., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.03.021 · Cited by 151 · see citing works

Neuropeptide pituitary adenylate cyclase‐activating polypeptide (PACAP) slows down Alzheimer's disease‐like pathology in amyloid precursor protein‐transgenic mice

Rat, D., Schmitt, U., Tippmann, F., Dewachter, I., Theunis, C., Wieczerzak, E., Postina, R., LEUVEN, F. V., Fahrenholz, F., & Kojro, E. (2011) · The FASEB Journal · doi:10.1096/fj.10-180133 · Cited by 148 · see citing works

Synaptic Therapy in Alzheimer's Disease: A CREB-centric Approach

Teich, A. F., Nicholls, R. E., Puzzo, D., Fiorito, J., Purgatorio, R., Fà, M., & Arancio, O. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0327-5 · Cited by 147 · see citing works

The metalloproteinase ADAM10: A useful therapeutic target?

Wetzel, S., Seipold, L., & Säftig, P. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.06.005 · Cited by 130 · see citing works

Neuropeptides Exert Neuroprotective Effects in Alzheimer's Disease

Chen, X., Du, Y., & Chen, L. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00493 · Cited by 131 · see citing works

Obesity, leptin, and Alzheimer's disease

Lee, E. B. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06274.x · Cited by 126 · 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

Gintonin, a Ginseng-Derived Lysophosphatidic Acid Receptor Ligand, Attenuates Alzheimer's Disease-Related Neuropathies: Involvement of Non-Amyloidogenic Processing

Hwang, S. H., Shin, E., Shin, T., Lee, B., Choi, S.-H., Kang, J., Kim, H., Kwon, S., Jang, C., Lee, J., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120439 · Cited by 115 · see citing works

Activation of α‐secretase cleavage

Postina, R. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07459.x · Cited by 109 · see citing works

G Protein-Coupled Receptors (GPCRs) in Alzheimer’s Disease: A Focus on BACE1 Related GPCRs

Zhao, J., Deng, Y., Jiang, Z., & Qing, H. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00058 · Cited by 108 · see citing works

The Purinergic Receptor P2X7 Triggers α-Secretase-dependent Processing of the Amyloid Precursor Protein

Delarasse, C., Auger, R., Gonnord, P., Fontaine, B., & Kanellopoulos, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.200618 · Cited by 108 · see citing works

5-HT4Receptors Constitutively Promote the Non-Amyloidogenic Pathway of APP Cleavage and Interact with ADAM10

Cochet, M., Donneger, R., Cassier, E., Gaven, F., Lichtenthaler, S. F., Marin, P., Bockaert, J., Dumuis, A., & Claeysen, S. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300095t · Cited by 105 · see citing works

Alternative Splicing of the Pituitary Adenylate Cyclase-Activating Polypeptide Receptor PAC1: Mechanisms of Fine Tuning of Brain Activity

Blechman, J., & Levkowitz, G. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00055 · Cited by 101 · see citing works

Exogenous Administration of PACAP Alleviates Traumatic Brain Injury in Rats through a Mechanism Involving the TLR4/MyD88/NF-κB Pathway

Mao, S., Hua, R., Zhao, X., Qin, X., Sun, Z.-Q., Zhang, Y., Wu, Y.-Q., Jia, M., Cao, J., & Zhang, Y.-M. (2012) · Journal of Neurotrauma · doi:10.1089/neu.2011.2244 · Cited by 93 · see citing works

Alzheimer culprits: Cellular crossroads and interplay

Claeysen, S., Cochet, M., Donneger, R., Dumuis, A., Bockaert, J., & Giannoni, P. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.05.008 · Cited by 79 · see citing works

Regulation of alpha-secretase ADAM10 expression and activity

Endres, K., & Fahrenholz, F. (2011) · Experimental Brain Research · doi:10.1007/s00221-011-2885-7 · Cited by 79 · see citing works

Upregulation of the α‐secretase ADAM10 – risk or reason for hope?

Endres, K., & Fahrenholz, F. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07566.x · Cited by 79 · see citing works

Redundant Gs-coupled serotonin receptors regulate amyloid-β metabolism in vivo

Fisher, J. R., Wallace, C. E., Tripoli, D. L., Sheline, Y. I., & Cirrito, J. R. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0112-5 · Cited by 79 · see citing works

Identification and biology of α‐secretase

Vingtdeux, V., & Marambaud, P. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07477.x · Cited by 81 · see citing works

Neuroprotective roles of pituitary adenylate cyclase-activating polypeptide in neurodegenerative diseases

Lee, E. H., & Seo, S. R. (2014) · BMB Reports · doi:10.5483/bmbrep.2014.47.7.086 · Cited by 75 · see citing works

Opposing Synaptic Regulation of Amyloid-β Metabolism by NMDA Receptors <i>In Vivo</i>

Verges, D. K., Restivo, J. L., Goebel, W. D., Holtzman, D. M., & Cirrito, J. R. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0607-11.2011 · Cited by 74 · see citing works

Amyloid Cascade Hypothesis for the Treatment of Alzheimer’s Disease: Progress and Challenges

Wu, T., Ding, L., Cheng, Y., Jiang, S., Riaz, M. W., Fu, N., Mou, C., Ye, M., & Zheng, Y. (2022) · Aging and Disease · doi:10.14336/ad.2022.0412 · Cited by 75 · see citing works

Protective effects of pituitary adenylate cyclase activating polypeptide in endothelial cells against oxidative stress-induced apoptosis

Rácz, B., Gasz, B., Borsiczky, B., Gallyas, F., Tamás, A., Józsa, R., Lubics, A., Kiss, P., Rőth, E., Ferencz, A., et al. (2006) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2006.12.006 · Cited by 71 · see citing works

The Distinct Role of ADAM17 in APP Proteolysis and Microglial Activation Related to Alzheimer’s Disease

Qian, M., Shen, X., & Wang, H. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0232-4 · Cited by 69 · see citing works

Interleukin‐1α stimulates non‐amyloidogenic pathway by α‐secretase (ADAM‐10 and ADAM‐17) cleavage of APP in human astrocytic cells involving p38 MAP kinase

Bandyopadhyay, S., Hartley, D. M., Cahill, C. M., Lahiri, D. K., Chattopadhyay, N., & Rogers, J. T. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20864 · Cited by 65 · see citing works

Induction of RAGE Shedding by Activation of G Protein-Coupled Receptors

Metz, V. V., Kojro, E., Rat, D., & Postina, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041823 · Cited by 61 · see citing works

Huperzine a alleviates synaptic deficits and modulates amyloidogenic and nonamyloidogenic pathways in APPswe/PS1dE9 transgenic mice

Wang, Y., Tang, X. C., & Zhang, H. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22775 · Cited by 60 · see citing works

α-Secretase Activation – An Approach to Alzheimer’s Disease Therapy

Fahrenholz, F., & Postina, R. (2006) · Neurodegenerative Diseases · doi:10.1159/000095264 · Cited by 59 · see citing works

MEK1/2 inhibition rescues neurodegeneration by TFEB-mediated activation of autophagic lysosomal function in a model of Alzheimer’s Disease

Chun, Y. S., Kim, M., Lee, S., Kim, M. J., Hong, T.-J., Jeon, J. K., Ganbat, D., Kim, H. T., Kim, S. S., Kam, T., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01713-5 · Cited by 56 · see citing works

Potential Enzymatic Targets in Alzheimer's: A Comprehensive Review.

Alam, J., & Sharma, L. (2019) · Current Drug Targets · doi:10.2174/1389450119666180820104723 · Cited by 43 · see citing works

Pituitary Adenylate Cyclase-Activating Polypeptide: 30 Years in Research Spotlight and 600 Million Years in Service

Dénes, V., Geck, P., Mester, A., & Gabriel, R. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8091488 · Cited by 58 · see citing works

Neurobiology of Memory and Anxiety: From Genes to Behavior

Kalueff, A. V. (2007) · Neural Plasticity · doi:10.1155/2007/78171 · Cited by 52 · see citing works

Light-Triggerable Liposomes for Enhanced Endolysosomal Escape and Gene Silencing in PC12 Cells

Chen, W., Deng, W., & Goldys, E. M. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.04.015 · Cited by 53 · see citing works

New insights into the function and pathophysiology of the ectodomain sheddase A Disintegrin And Metalloproteinase 10 (ADAM10)

Rosenbaum, D., & Säftig, P. (2023) · FEBS Journal · doi:10.1111/febs.16870 · Cited by 53 · see citing works

Pharmacological Treatment of Depression in Alzheimer’s Disease: A Challenging Task

Cassano, T., Calcagnini, S., Carbone, A., Bukke, V. N., Orkisz, S., Villani, R., Romano, A., Avolio, C., & Gaetani, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01067 · Cited by 51 · see citing works

Activation of the α-Secretase Processing of AβPP as a Therapeutic Approach in Alzheimer's Disease

Vincent, B., & Govitrapong, P. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110218 · Cited by 45 · see citing works

Regulation of the α-secretase ADAM10 at transcriptional, translational and post-translational levels

Vincent, B. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.03.020 · Cited by 45 · see citing works

Statins and the Squalene Synthase Inhibitor Zaragozic Acid Stimulate the Non-Amyloidogenic Pathway of Amyloid-β Protein Precursor Processing by Suppression of Cholesterol Synthesis

Kojro, E., Füger, P., Prinzen, C., Kanarek, A. M., Rat, D., Endres, K., Fahrenholz, F., & Postina, R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091621 · Cited by 45 · see citing works

Promoter polymorphisms which regulate ADAM9 transcription are protective against sporadic Alzheimer's disease

Cong, L., & Jia, J. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.01.001 · Cited by 43 · see citing works

Therapeutic potential of PACAP for neurodegenerative diseases

Yang, R., Jiang, X. M., Ji, R., Meng, L., Liu, F., Chen, X., & Xin, Y. (2015) · Cellular & Molecular Biology Letters · doi:10.1515/cmble-2015-0008 · Cited by 43 · see citing works

Role of pituitary adenylate cyclase-activating polypeptide (PACAP) in the action of ginsenoside Rh2 against beta-amyloid-induced inhibition of rat brain astrocytes

Shieh, P.-C., Tsao, C.-W., Li, J.-S., Wu, H., Wen, Y.-J., Kou, D., & Cheng, J. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.12.032 · Cited by 43 · see citing works

BACE and γ-Secretase Characterization and Their Sorting as Therapeutic Targets to Reduce Amyloidogenesis

Marks, N., & Berg, M. J. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0054-1 · Cited by 38 · see citing works

Ectodomain shedding of the receptor for advanced glycation end products: a novel therapeutic target for Alzheimer’s disease

Zhang, L., Postina, R., & Wang, Y.-Q. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0121-4 · Cited by 44 · see citing works

Regulated Proteolysis of RAGE and AβPP as Possible Link Between Type 2 Diabetes Mellitus and Alzheimer's Disease

Kojro, E., & Postina, R. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0998 · Cited by 40 · see citing works

The Cytoplasmic Domain of A Disintegrin and Metalloproteinase 10 (ADAM10) Regulates Its Constitutive Activity but Is Dispensable for Stimulated ADAM10-dependent Shedding

Maretzky, T., Evers, A., Gall, S. M. L., Alabi, R. O., Speck, N., Reiß, K., & Blobel, C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.603753 · Cited by 39 · see citing works

Coordination between proteasome impairment and caspase activation leading to TAU pathology: neuroprotection by cAMP

Metcalfe, M., Huang, Q., & Figueiredo‐Pereira, M. E. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.70 · Cited by 38 · see citing works

Accelerated pre‐senile systemic amyloidosis in PACAP knockout mice – a protective role of PACAP in age‐related degenerative processes

Reglődi, D., Jüngling, A., Longuespée, R., Kriegsmann, J., Casadonte, R., Kriegsmann, M., Juhász, T., Bardosi, S., Tamás, A., Fulop, B. D., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5100 · Cited by 38 · see citing works

The neuropeptidePACAP38induces dendritic spine remodeling through ADAM10/N-Cadherin signaling pathway

Gardoni, F., Luca, M. D., Malinverno, M., Marcello, E. E., Verpelli, C., Sala, C., & Luca, M. D. (2012) · Journal of Cell Science · doi:10.1242/jcs.097576 · Cited by 33 · see citing works

Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity

Bajor, M., & Kaczmarek, L. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0919-6 · Cited by 33 · see citing works

Leptin inhibits amyloid β‐protein fibrillogenesis by decreasing GM1 gangliosides on the neuronal cell surface through PI3K/Akt/mTOR pathway

Yamamoto, N., Tanida, M., Kasahara, R., Sobue, K., & Suzuki, K. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12828 · Cited by 30 · see citing works

Neurosecretases provide strategies to treat sporadic and familial Alzheimer disorders

Marks, N., & Berg, M. J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.06.020 · Cited by 29 · see citing works

Trafficking in neurons: Searching for new targets for Alzheimer's disease future therapies

Musardo, S., Saraceno, C., Pelucchi, S., & Marcello, E. E. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.07.019 · Cited by 29 · see citing works

A Two Decade Contribution of Molecular Cell Biology to the Centennial of Alzheimer's Disease: Are We Progressing Toward Therapy?

Dillen, K., & Annaert, W. G. (2006) · International review of cytology · doi:10.1016/s0074-7696(06)54005-7 · Cited by 29 · see citing works

Pituitary Adenylate Cyclase-Activating Polypeptide Modulates Hippocampal Synaptic Transmission and Plasticity: New Therapeutic Suggestions for Fragile X Syndrome

Ciranna, L., & Costa, L. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00524 · Cited by 28 · see citing works

Substance P activates ADAM9 mRNA expression and induces α-secretase-mediated amyloid precursor protein cleavage

Marolda, R., Ciotti, M. T., Matrone, C., Possenti, R., Calissano, P., Cavallaro, S., & Severini, C. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.12.025 · Cited by 27 · see citing works

Nonamyloidogenic processing of amyloid beta precursor protein is associated with retinal function improvement in aging male APPswe/PS1ΔE9 mice

Joly, S., Lamoureux, S., & Pernet, V. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.02.004 · Cited by 24 · see citing works

GSK3β modulates PACAP-induced neuritogenesis in PC12 cells by acting downstream of Rap1 in a caveolae-dependent manner

Zhang, W., Smith, A. D., Liu, J., Cheung, N. S., Zhou, S., Liu, K., Li, Q., & Duan, W. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.10.008 · Cited by 24 · see citing works

Design and Synthesis of Brain Penetrant Glycopeptide Analogues of PACAP With Neuroprotective Potential for Traumatic Brain Injury and Parkinsonism

Apostol, C. R., Bernard, K., Tanguturi, P., Molnar, G., Bartlett, M. J., Szabó, L., Liu, C., Ortiz, J. B., Saber, M., Giordano, K. R., et al. (2022) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2021.818003 · Cited by 20 · see citing works

PACAP38 protects rat cortical neurons against the neurotoxicity evoked by sodium nitroprusside and thrombin

Sanchez, A. C., Rao, H. V., & Grammas, P. (2008) · Regulatory Peptides · doi:10.1016/j.regpep.2008.07.004 · Cited by 19 · see citing works

STC1 Induction by PACAP is Mediated Through cAMP and ERK1/2 but not PKA in Cultured Cortical Neurons

Holighaus, Y., Weihe, E., & Eiden, L. E. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9653-9 · Cited by 17 · see citing works

Bioinformatic Analysis Reveals Phosphodiesterase 4D-Interacting Protein as a Key Frontal Cortex Dementia Switch Gene

Potashkin, J. A., Bottero, V., Santiago, J. A., & Quinn, J. P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113787 · Cited by 16 · see citing works

New highly sensitive rodent and human tests for soluble amyloid precursor protein alpha quantification: preclinical and clinical applications in Alzheimer’s disease

Rose, C., Peoc’h, K., Chasseigneaux, S., Paquet, C., Dumurgier, J., Bourasset, F., Calon, F., Laplanche, J., Hugon, J., & Allinquant, B. (2012) · BMC Neuroscience · doi:10.1186/1471-2202-13-84 · Cited by 13 · see citing works

Regulation of the Soluble Amyloid Precursor Protein α (sAPPα) Levels by Acetylcholinesterase and Brain-Derived Neurotrophic Factor in Lung Cancer Cell Media

Khashali, H. A., Ray, R., Coleman, K.-L., Atali, S., Haddad, B., Wareham, J., Guthrie, J. W., Heyl, D., & Evans, H. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810746 · Cited by 13 · see citing works

A subnanomolar concentration of Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP) pre-synaptically modulates glutamatergic transmission in the rat hippocampus acting through acetylcholine

Pecoraro, V., Sardone, L. M., Chisari, M., Licata, F., Volsi, G. L., Perciavalle, V., Ciranna, L., & Costa, L. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.10.061 · Cited by 12 · see citing works

Grape powder consumption affects the expression of neurodegeneration-related brain proteins in rats chronically fed a high-fructose–high-fat diet

Liao, H., Chou, L.-M., Chien, Y., Wu, C., Chang, J., Lin, C.-I., & Lin, S. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2017.02.013 · Cited by 12 · see citing works

Viable mouse gene ablations that robustly alter brain Aβ levels are rare

Toyn, J. H., Lin, X.-A., Thompson, M. W., Guss, V. L., Meredith, J. E., Sankaranarayanan, S., Barrezueta, N. X., Corradi, J., Majumdar, A., Small, D. L., et al. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-143 · Cited by 11 · see citing works

Pharmacological Treatment of Alzheimer`s Disease: Is it Progressing Adequately?

Robles, A. (2009) · The Open Neurology Journal · doi:10.2174/1874205x00903010027 · Cited by 11 · see citing works

Age-Related Decrease in Glucagon-Like Peptide-1 in Mouse Prefrontal Cortex but Not in Hippocampus Despite the Preservation of Its Receptor

Ohshima, R. (2015) · American Journal of BioScience · doi:10.11648/j.ajbio.20150301.13 · Cited by 10 · see citing works

Mechanisms for PACAP-induced prolactin gene expression in grass carp pituitary cells

Lin, C., Jiang, X. X., He, M., Zhao, L., Huang, T., Bian, Z., & Wong, A. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0433 · Cited by 10 · see citing works

Pituitary adenylate cyclase-activating polypeptide (PACAP) protects against mitoxantrone-induced cardiac injury in mice

Subramaniam, V., Chuang, G. C., Xia, H., Burn, B. R., Bradley, J., Maderdrut, J. L., Coy, D. H., & Varner, K. J. (2017) · Peptides · doi:10.1016/j.peptides.2017.07.007 · Cited by 10 · see citing works

Crossing Barriers: Advancements in Macromolecular Therapeutics for Neurodegenerative Diseases and Strategies to Overcome the Blood–Brain Barrier

Alo, B., & Lamers, C. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00153 · Cited by 10 · see citing works

Crosstalk between angiotensin and the nonamyloidogenic pathway of Alzheimer's amyloid precursor protein

Kanarek, A. M., Wagner, A., Küppers, J., Gütschow, M., Postina, R., & Kojro, E. (2017) · FEBS Journal · doi:10.1111/febs.14015 · Cited by 8 · see citing works

Alternative Pharmacological Strategies for the Treatment of Alzheimer’s Disease: Focus on Neuromodulator Function

Cunliffe, G., Lim, Y. T., Chae, W., & Jung, S. (2022) · Biomedicines · doi:10.3390/biomedicines10123064 · Cited by 5 · see citing works

A Bioengineering Strategy to Control ADAM10 Activity in Living Cells

Pastore, F., Battistoni, M., Sollazzo, R., Renna, P., Paciello, F., Puma, D. D. L., Barone, E., Dağliyan, O., Ripoli, C., & Grassi, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020917 · Cited by 6 · see citing works

ADAM10: Function insights, disease implications, and promise of therapeutic targeting

Zhang, W., Xu, Y., & Fu, J. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104414 · Cited by 5 · see citing works

Inhibition of PACAP/PAC1/VPAC2 signaling impairs the consolidation of social recognition memory and nitric oxide prevents this deficit

Schmidt, S. D., Zinn, C. G., Behling, J. A. K., Furian, A. F., Furini, C. R. G., Myskiw, J. D. C., & Izquierdo, I. (2021) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2021.107423 · Cited by 5 · see citing works

Microglial Physiology

Watters, J. J., & Pocock, J. M. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1429-6_3 · Cited by 5 · see citing works

From circadian sleep disruption to Neuroprotection: The potential of VIP/PACAP in Alzheimer’s disease treatment

Galushkin, A., & Gozes, I. (2024) · Current Research in Biotechnology · doi:10.1016/j.crbiot.2024.100254 · Cited by 4 · see citing works

Proteases in the Nervous System

Cynis, H., Lichtenthaler, S., Wagner, L., & Demuth, H. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_10 · Cited by 1 · see citing works

LncRNA ENST00000440246.1 Promotes Alzheimer’s Disease Progression by Targeting PP2A

Gao, S., Chang, F., Wang, Y., Yang, W., & Jiang, H. (2023) · Biochemical Genetics · doi:10.1007/s10528-023-10552-0 · Cited by 4 · see citing works

The role of leptin in regulation of the soluble amyloid precursor protein α (sAPPα) levels in lung cancer cell media

Haddad, B., Khalil, J., Khashali, H. A., Ray, R., Goel, S., Darweesh, B., Coleman, K.-L., Wozniak, C., Ranzenberger, R., Lopo, B., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-55717-y · Cited by 4 · see citing works

Mechanisms of PACAP in PTSD and Stress-Related Disorders in Humans

Lebois, L. A. M., & Ressler, K. J. (2016) · Current topics in neurotoxicity · doi:10.1007/978-3-319-35135-3_45 · Cited by 4 · see citing works

Neuroprotective Effects of Pituitary Adenylate Cyclase-Activating Polypeptide

Meng, R. J. L. (2014) · International Journal of Advance Innovations Thoughts & Ideas · doi:10.4172/2277-1891.1000156 · Cited by 3 · see citing works

Synthesis and In Vitro Characterization of Glycopeptide Drug Candidates Related to PACAP1–23

Apostol, C. R., Tanguturi, P., Szabó, L., Varela, D., Gilmartin, T., Streicher, J. M., & Polt, R. L. (2021) · Molecules · doi:10.3390/molecules26164932 · Cited by 3 · see citing works

P4–256: PACAP peptides as new α–secretase activators

Kojro, E., Postina, R., Gehrig‐Burger, K., & Fahrenholz, F. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1995

Neuropeptide pituitary adenylate cyclase‐activating polypeptide (PACAP) slows down Alzheimer's disease‐like pathology in amyloid precursor protein‐transgenic mice

Rat, D., Schmitt, U., Tippmann, F., Dewachter, I., Theunis, C., Wieczerzak, E., Postina, R., LEUVEN, F. V., Fahrenholz, F., & Kojro, E. (2011) · The FASEB Journal · doi:10.1096/fj.10-180133 · Cited by 148 · see citing works

Alpha-Secretase As a Therapeutic Target

Fahrenholz, F. (2007) · Current Alzheimer Research · doi:10.2174/156720507781788837 · Cited by 111 · see citing works

New protein kinase C activator regulates amyloid precursor protein processing in vitro by increasing α‐secretase activity

Yang, H., Pan, J., Ba, M., Sun, Z., Ma, G., Lü, G., Xiao, Q., & Chen, S. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05648.x · Cited by 40 · see citing works

Regulation of Secretion of Alzheimer Amyloid Precursor Protein by the Mitogen‐Activated Protein Kinase Cascade

Desdouits‐Magnen, J., Desdouits, F., Takeda, S., Syu, L.-J., Saltiel, A. R., Buxbaum, J. D., Czernik, A. J., Nairn, A. C., & Greengard, P. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70020524.x · Cited by 109 · see citing works