Cited by 588Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchCholinesterase and Neurodegenerative Diseases

The DOI matches its Crossref record; 365 of the 371 references it cites were found in a registry or an index.

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Barage, Sagar H., Sonawane, Kailas D.·2015·Neuropeptides

DOI 10.1016/j.npep.2015.06.008

Open this paper in CoChat — free account

Abstract

Alzheimer's disease is an irreversible, progressive neurodegenerative disorder. Various therapeutic approaches are being used to improve the cholinergic neurotransmission, but their role in AD pathogenesis is still unknown. Although, an increase in tau protein concentration in CSF has been described in AD, but several issues remains unclear. Extensive and accurate analysis of CSF could be helpful to define presence of tau proteins in physiological conditions, or released during the progression of neurodegenerative disease. The amyloid cascade hypothesis postulates that the neurodegeneration in AD caused by abnormal accumulation of amyloid beta (Aβ) plaques in various areas of the brain. The amyloid hypothesis has continued to gain support over the last two decades, particularly from genetic studies. Therefore, current research progress in several areas of therapies shall provide an effective treatment to cure this devastating disease. This review critically evaluates general biochemical and physiological functions of Aβ directed therapeutics and their relevance.

Integrity signals

Registry

Crossref · 10.1016/j.npep.2015.06.008

Cites

365 of 365 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Items 201–365 of 365

Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer’s disease
Ling, Y., Morgan, K., & Kalsheker, N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00133-x · Cited by 224
Nicotine Inhibits Amyloid Formation by the β-Peptide
Salomon, A. R., Marcinowski, K. J., Friedland, R. P., & Zagorski, M. G. (1996) · Biochemistry · doi:10.1021/bi9617264 · Cited by 220
Current advances in using neurotrophic factors to treat neurodegenerative disorders
Weissmiller, A. M., & Wu, C. (2012) · Translational Neurodegeneration · doi:10.1186/2047-9158-1-14 · Cited by 219
β-Secretase (BACE) as a drug target for alzheimer’s disease
Vassar, R. J. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00157-6 · Cited by 212
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
Aβ-degrading enzymes: modulators of Alzheimer's disease pathogenesis and targets for therapeutic intervention
Eckman, C. B., & Eckman, E. A. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051101 · Cited by 211
Substrate and Inhibitor Profile of BACE (β-Secretase) and Comparison with Other Mammalian Aspartic Proteases
Grüninger-Leitch, F., Schlatter, D., Küng, E., Nelböck, P., & Döbeli, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109266200 · Cited by 211
Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation
Dayanandan, R., van Slegtenhorst, M., Mack, T. G. A., Ko, L., Yen, S. H., Leroy, K., Brion, J., Anderton, B. H., Hutton, M. L., & Lovestone, S. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00222-7 · Cited by 210
What the evolution of the amyloid protein precursor supergene family tells us about its function
Coulson, E. J., Paliga, K., Beyreuther, K. T., & Masters, C. L. (2000) · Neurochemistry International · doi:10.1016/s0197-0186(99)00125-4 · Cited by 209
Second Kininase in Human Blood Plasma
Yang, H., & Erdös, E. G. (1967) · Nature · doi:10.1038/2151402a0 · Cited by 208
Recognition Sequence Design for Peptidyl Modulators of β-Amyloid Aggregation and Toxicity
Pallitto, M. M., Ghanta, J., Heinzelman, P., Kiessling, L. L., & Murphy, R. M. (1999) · Biochemistry · doi:10.1021/bi982119e · Cited by 208
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
Neutral endopeptidase can hydrolyze β-amyloid(1–40) but shows no effect on β-amyloid precursor protein metabolism
Howell, S. W., Nalbantoglu, J. N., & Crine, P. (1995) · Peptides · doi:10.1016/0196-9781(95)00021-b · Cited by 205
Interaction of the anthracycline 4'-iodo-4'-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis.
Merlini, G., Ascari, E., Amboldi, N., Bellotti, V., Arbustini, E., Perfetti, V., Ferrari, M., Zorzoli, I., Marinone, M. G., & Garini, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2959 · Cited by 204
Transcription of Testicular Angiotensin-Converting Enzyme (ACE) Is Initiated within the 12th Intron of the Somatic ACE Gene
Howard, T. E., Shai, S., Langford, K. G., Martin, B. M., & Bernstein, K. E. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4294 · Cited by 201
Membrane Topology of the C. elegans SEL-12 Presenilin
Li, X., & Greenwald, I. (1996) · Neuron · doi:10.1016/s0896-6273(00)80231-7 · Cited by 201
Plasma Aβ in Alzheimer's disease—up or down?
Zetterberg, H., & Blennow, K. (2006) · The Lancet Neurology · doi:10.1016/s1474-4422(06)70503-8 · Cited by 200
β-Secretase inhibition for the treatment of Alzheimer's disease – promise and challenge
Citron, M. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2003.12.004 · Cited by 199
Evidence for high affinity choline transport in synaptosomes prepared from hippocampus and neocortex of patients with Alzheimer's disease
Rylett, R. J., Ball, M. J., & Colhoun, E. H. (1983) · Brain Research · doi:10.1016/0006-8993(83)90017-3 · Cited by 198
Regulation of Steady-state β-Amyloid Levels in the Brain by Neprilysin and Endothelin-converting Enzyme but Not Angiotensin-converting Enzyme
Eckman, E. A., Adams, S. K., Troendle, F. J., Stodola, B. A., Kahn, M. A., Fauq, A. H., Xiao, H. D., Bernstein, K. E., & Eckman, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605827200 · Cited by 196 · cited 2×
“Few studies have shown that inactivation of themouse ACE gene or inhibition of ACE in mice does not affect Aβ peptide level (Eckman et al., 2006; Hemming et al., 2007).”
β ‐Amyloid Degradation and Alzheimer′s Disease
Wang, D.-S., Dickson, D. W., & Malter, J. S. (2006) · BioMed Research International · doi:10.1155/jbb/2006/58406 · Cited by 195
Angiotensin-Converting Enzyme Converts Amyloid β-Protein 1–42 (Aβ 1–42 ) to Aβ 1–40 , and Its Inhibition Enhances Brain Aβ Deposition
Zou, K., Yamaguchi, H., Akatsu, H., Sakamoto, T., Ko, M.-H., Mizoguchi, K., Gong, J.-S., Yu, W., Yamamoto, T., Kosaka, K., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1549-07.2007 · Cited by 193
β-Amyloid peptides as direct cholinergic neuromodulators: a missing link?
Auld, D. S., Kar, S., & Quirion, R. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01144-2 · Cited by 192
Gleevec inhibits β-amyloid production but not Notch cleavage
Netzer, W. J., Dou, F., Cai, D., Veach, D. R., Jean, S., Li, Y., Bornmann, W. G., Clarkson, B., Xu, H., & Greengard, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1534745100 · Cited by 192
Reduction in p140-TrkA receptor protein within the nucleus basalis and cortex in Alzheimer's disease.
Mufson, E., Lavine, N., Jaffar, S., Kordower, J., Quirion, R., & Saragovi, H. (1997) · Experimental Neurology · doi:10.1006/exnr.1997.6504 · Cited by 188
Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease
Cataldo, A. M., Hamilton, D. J., & Nixon, R. A. (1994) · Brain Research · doi:10.1016/0006-8993(94)91858-9 · Cited by 185
Degradation of Alzheimer's ß-Amyloid Protein by Human and Rat Brain Peptidases: Involvement of Insulin-Degrading Enzyme
MCDERMOTT, J. R., & GIBSON, A. M. (1997) · Neurochemical Research · doi:10.1023/a:1027325304203 · Cited by 184
The neuropathogenic contributions of lysosomal dysfunction
Bahr, B. A., & Bendiske, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01192.x · Cited by 183
β-Secretase as a Therapeutic Target for Alzheimer's Disease
Ghosh, A. K., Gemma, S., & Tang, J. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.007 · Cited by 183
Morphological criteria for the recognition of Alzheimer's disease and the distribution pattern of cortical changes related to this disorder
Braak, H., & Braak, E. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90032-9 · Cited by 181
Molecular genetic analysis of familial early-onset Alzheimer's disease linked to chromosome 14q24.3
Cruts, M., Backhovens, H., Wang, S., Gassen, G. V., Theuns, J., Jonghe, C. D., Wehnert, A., Voecht, J. D., Winter, G. D., Cras, P. P., et al. (1995) · Human Molecular Genetics · doi:10.1093/hmg/4.12.2363 · Cited by 180
Biogenesis and metabolism of Alzheimer’s disease Aβ amyloid peptides
Evin, G. M., & Weidemann, A. (2002) · Peptides · doi:10.1016/s0196-9781(02)00063-3 · Cited by 179
A Single Ascending Dose Study of Bapineuzumab in Patients With Alzheimer Disease
Black, R. S., Sperling, R. A., Safirstein, B., Motter, R. N., Pallay, A., Nichols, A., & Grundman, M. (2010) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e3181c53b00 · Cited by 170
Aβ-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer's disease
Huang, Y. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.04.004 · Cited by 170
Protein Phosphatase 2A Is the Major Enzyme in Brain that Dephosphorylates τ Protein Phosphorylated by Proline‐Directed Protein Kinases or Cyclic AMP‐Dependent Protein Kinase
Goedert, M., Jakes, R., Qi, R. Z., Wang, J. H.-C., & Cohen, P. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65062804.x · Cited by 170
Amyloid β‐Peptide Inhibits High‐Affinity Choline Uptake and Acetylcholine Release in Rat Hippocampal Slices
Kar, S., Issa, A. M., Seto, D., Auld, D. S., Collier, B., & Quirion, R. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70052179.x · Cited by 167
Angiotensin I‐converting Enzyme
Grönhagen-Riska, C., Fyhrquist, F., & von Willebrand, E. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb18500.x · Cited by 165
Angiotensins in Alzheimer's disease – friend or foe?
Kehoe, P. G., Miners, J. S., & Love, S. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.07.006 · Cited by 164
Disrupting β-Amyloid Aggregation for Alzheimer Disease Treatment
Estrada, L. D., & Soto, C. A. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607779318262 · Cited by 164
Rivastigmine in the treatment of Alzheimer's disease: an update
Onor, M. L., Trevisiol, M., & Aguglia, E. (2007) · Clinical Interventions in Aging · doi:10.2147/ciia.2007.2.1.17 · Cited by 162
The cell biology of Alzheimer's disease: uncovering the secrets of secretases
Walter, J., Kaether, C., Steiner, H., & Haass, C. (2001) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00253-1 · Cited by 160
Anterior pituitary hormones, stress, and immune system homeostasis
Dorshkind, K. A., & Horseman, N. D. (2001) · BioEssays · doi:10.1002/1521-1878(200103)23:3 · Cited by 157
Neprilysin Regulates Amyloid β Peptide Levels
Marr, R. A., Guan, H., Rockenstein, E. M., Kindy, M. S., Gage, F. H., Verma, I. M., Masliah, E., & Hersh, L. B. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:22:1-2:5 · Cited by 157
Role of Serine/Threonine Protein Phosphatase in Alzheimer’s Disease
Tian, Q., & Wang, J. (2002) · Neurosignals · doi:10.1159/000067425 · Cited by 156
Design and characterization of a membrane permeable N‐methyl amino acid‐containing peptide that inhibits Aβ1–40 fibrillogenesis
Gordon, D. J., Tappe, R., & Meredith, S. C. (2002) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2002.11002.x · Cited by 156
Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions.
L’Hernault, S. W., & Arduengo, P. M. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.1.55 · Cited by 155
Hydrolysis of Peptide Hormones by Endothelin-converting Enzyme-1
Johnson, G. D., Stevenson, T. I., & Ahn, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4053 · Cited by 147
Apolipoprotein E and Alzheimer Disease: An Update on Genetic and Functional Analyses
Saunders, A. M. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.9.751 · Cited by 147
Inhibition and Modulation of γ-Secretase for Alzheimer's Disease
Wolfe, M. S. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.010 · Cited by 146
Tau Therapeutic Strategies for the Treatment of Alzheimers Disease
Churcher, I. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776743057 · Cited by 142
Reductions in Acetylcholine and Nicotine Binding in Several Degenerative Diseases
Whitehouse, P. J., Martino, A. M., Marcus, K. A., Zweig, R. M., Singer, H. S., Price, D. L., & Kellar, K. J. (1988) · Archives of Neurology · doi:10.1001/archneur.1988.00520310028012 · Cited by 141
Proteolytic mechanisms in amyloid-β metabolism: therapeutic implications for Alzheimer's disease
Vardy, E. R. L. C., Catto, A. J., & Hooper, N. M. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.08.004 · Cited by 135
Concentration-Dependent Modulation of Amyloid-β in Vivo and in Vitro Using the γ-Secretase Inhibitor, LY-450139
Lanz, T. A., Karmilowicz, M. J., Wood, K. M., Pozdnyakov, N., Du, P., Piotrowski, M. A., Brown, T. M., Nolan, C. E., Richter, K. E. G., Finley, J. E., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110700 · Cited by 130
Design of Potent Peptide Mimetics of Brain-derived Neurotrophic Factor
O’Leary, P. D., & Hughes, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303209200 · Cited by 129
Corticotropin-Releasing Hormone-Mediated Neuroprotection against Oxidative Stress Is Associated with the Increased Release of Non-amyloidogenic Amyloid Precursor Protein and with the Suppression of Nuclear Factor- B
Lezoualc’h, F., Engert, S., Berning, B., & Behl, C. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.1.0403 · Cited by 124
Characterization of human presenilin 1 using N‐terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing
Mercken, M. H., Takahashi, H., Honda, T., Sato, K., Murayama, M., Nakazato, Y., Noguchi, K., Imahori, K., & Takashima, A. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00608-4 · Cited by 124
Neuropeptide Y and its role in CNS disease and repair
Decressac, M., & Barker, R. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.09.004 · Cited by 123
Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues.
Kuo, W. L., MONTAG, A. G., & Rosner, M. R. (1993) · Endocrinology · doi:10.1210/endo.132.2.7678795 · Cited by 122
Cholinesterase Inhibitors Stabilize Alzheimer's Disease
Giacobini, E. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06942.x · Cited by 122
Non-amyloidogenic cleavage of the beta-amyloid precursor protein by an integral membrane metalloendopeptidase.
Roberts, S. B., Ripellino, J. A., Ingalls, K. M., Robakis, N. K. R. K., & Felsenstein, K. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42055-2 · Cited by 120
Evaluating triggers and enhancers of tau fibrillization
Kuret, J., Congdon, E. E., Li, G., Yin, H., Yu, X., & Zhong, Q. (2005) · Microscopy Research and Technique · doi:10.1002/jemt.20187 · Cited by 119
State of the art of the neurotrophin hypothesis in psychiatric disorders: implications and limitations
Lang, U. E., Jockers-Scherübl, M. C., & Hellweg, R. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-003-0100-0 · Cited by 119
Effects of prolonged angiotensin-converting enzyme inhibitor treatment on amyloid β-protein metabolism in mouse models of Alzheimer disease
Hemming, M. L., Selkoe, D. J., & Farris, W. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.01.004 · Cited by 119
PKCε increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice
Choi, D., Wang, D., Yu, G.-Q., Zhu, G., Kharazia, V., Paredes, J. P., Chang, W. S., Deitchman, J. K., Mucke, L., & Messing, R. O. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509725103 · Cited by 119
Role of neurotrophins in cholinergic-neurone function in the adult and aged CNS
Rylett, R. J., & Williams, L. R. (1994) · Trends in Neurosciences · doi:10.1016/0166-2236(94)90138-4 · Cited by 118
The neuronal endosomal-lysosomal system in Alzheimer's disease
Nixon, R. A., Mathews, P. M., & Cataldo, A. M. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3114 · Cited by 114
Physostigmine restores3H-acetylcholine efflux from Alzheimer brain slices to normal level
Nilsson, L. M., Nordberg, A. K., Hardy, J., Wester, P. O., & Winblad, B. G. (1986) · Journal of Neural Transmission · doi:10.1007/bf01243353 · Cited by 114
Recent advances in knowledge of the structure and function of the angiotensin I converting enzyme
Corvol, P. L., Michaud, A., Soubrier, F., & Williams, T. A. (1995) · Journal of Hypertension · doi:10.1097/00004872-199509003-00002 · Cited by 114
Central Angiotensin II Stimulation Promotes β Amyloid Production in Sprague Dawley Rats
Zhu, D., Shi, J., Zhang, Y., Wang, B., Liu, W., Chen, Z., & Tong, Q. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016037 · Cited by 112
Cathepsin B Degrades Amyloid-β in Mice Expressing Wild-type Human Amyloid Precursor Protein
Wang, C., Sun, B., Zhou, Y., GRUBB, A. O., & Gan, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371641 · Cited by 112
Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto
Hsu, R., Lee, K., Wang, J.-H., Lee, L. Y.-L., & Chen, R. P. ‐. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf803072r · Cited by 112
Alpha-Secretase As a Therapeutic Target
Fahrenholz, F. (2007) · Current Alzheimer Research · doi:10.2174/156720507781788837 · Cited by 111
Shift in the ratio of three‐repeat tau and four‐repeat tau mRNAs in individual cholinergic basal forebrain neurons in mild cognitive impairment and Alzheimer's disease
Ginsberg, S. D., Che, S., Counts, S. E., & Mufson, E. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03641.x · Cited by 111
Alterations in immunological and neurological gene expression patterns in Alzheimer's disease tissues
Weeraratna, A. T., Kalehua, A. N., DeLeon, I., Bertak, D., Maher, G., Wade, M. S., Lustig, A., Becker, K. G., Wood, W. W., Walker, D. G., et al. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.10.028 · Cited by 109
An upstream enhancer and a negative element in the 5' flanking region of the human urokinase plasminogen activator gene
Verde, P., Boast, S., Franzè, A., Robbiati, F., & Blasi, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10699 · Cited by 108
Alzheimer disease risk and genetic variation in ACE
Elkins, J. S., Douglas, V. C., & Johnston, S. C. (2004) · Neurology · doi:10.1212/01.wnl.0000106823.72493.ff · Cited by 108
Aminopeptidase A contributes to the N‐terminal truncation of amyloid β‐peptide
Sévalle, J., Amoyel, A., Robert, P. H., Fournié‐Zaluski, M., Roques, B. P., & Checler, F. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05950.x · Cited by 108
Microheterogeneity of Micro tubule‐Associated τ Proteins Is Due to Differences in Phosphorylation
Butler, M., & Shelanski, M. L. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00788.x · Cited by 106
Examination of the Clinicopathologic Continuum of Alzheimer Disease in the Autopsy Cohort of the National Alzheimer Coordinating Center
Serrano‐Pozo, A., Qian, J., Monsell, S. E., Frosch, M. P., Betensky, R. A., & Hyman, B. T. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000016 · Cited by 106
Current advances in the treatment of Alzheimer's disease: focused on considerations targeting Aβ and tau
Yang, H., Sun, Z., & Chen, S. (2012) · Translational Neurodegeneration · doi:10.1186/2047-9158-1-21 · Cited by 105
Recent Advances in the Identification of γ-Secretase Inhibitors To Clinically Test the Aβ Oligomer Hypothesis of Alzheimer’s Disease
Kreft, A. F., Martone, R. L., & Porte, A. M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900188z · Cited by 105
Endothelin-Converting Enzyme-2 Is Increased in Alzheimer’s Disease and Up-Regulated by Aβ
Palmer, J. C., Baig, S., Kehoe, P. G., & Love, S. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.081054 · Cited by 103
Degradation of Amyloid β-Protein by a Serine Protease-α2-Macroglobulin Complex
Qiu, W. Q., Borth, W., Ye, Z., Haass, C., Teplow, D. B., & Selkoe, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.8443 · Cited by 98
Corticotropin-releasing hormone physiology
Majzoub, J. A. (2006) · European Journal of Endocrinology · doi:10.1530/eje.1.02247 · Cited by 97
Somatostatin: the neuroendocrine story
Gillies, G. E. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(96)01032-2 · Cited by 95
Somatostatin, Alzheimer's disease and cognition: An old story coming of age?
Epelbaum, J., Guillou, J., Gastambide, F., Hoyer, D., Duron, E., & Viollet, C. (2009) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2009.07.002 · Cited by 94
Neuropeptide Y Fragments Derived from Neprilysin Processing Are Neuroprotective in a Transgenic Model of Alzheimer's Disease
Rose, J. B., Crews, L. A., Rockenstein, E. M., Adame, A., Mante, M., Hersh, L. B., Gage, F. H., Spencer, B. J., Potkar, R., Marr, R. A., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4220-08.2009 · Cited by 94
Effect of human endopeptidase 24.11 ("enkephalinase") on IL-1-induced thymocyte proliferation activity.
Pierart, M. E., Najdovski, T., Appelboom, T., & Deschodt-Lanckman, M. M. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.140.11.3808 · Cited by 94
Vacuolar/lysosomal proteolysis: proteases, substrates mechanisms
Knop, M., Schiffer, H. H., Rupp, S., & Wolf, D. H. (1993) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(93)90082-2 · Cited by 93
Endothelin-converting Enzymes Degrade Intracellular β-Amyloid Produced within the Endosomal/Lysosomal Pathway and Autophagosomes*
Pacheco‐Quinto, J., & Eckman, E. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422964 · Cited by 92
Long-term stabilizing effect of cholinesterase inhibitors in the therapy of Alzheimer’ disease
Giacobini, E. (2002) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6139-5_17 · Cited by 91
Dynamics of Aβ Turnover and Deposition in Different β-Amyloid Precursor Protein Transgenic Mouse Models Following γ-Secretase Inhibition
Abramowski, D., Wiederhold, K.-H., Furrer, U., Jaton, A.-L., Neuenschwander, A., Runser, M.-J., Danner, S., Reichwald, J., Ammaturo, D., Staab, D., et al. (2008) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.140327 · Cited by 89
Somatostatin and Alzheimer's disease
Burgos‐Ramos, E., Hervás‐Aguilar, A., Aguado‐Llera, D., Puebla‐Jiménez, L., Hernández‐Pinto, A. M., Barrios, V., & Arilla, E. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.01.014 · Cited by 88
Targeting the Prodromal Stage of Alzheimer's Disease: Bioenergetic and Mitochondrial Opportunities
Caldwell, C. C., Yao, J., & Brinton, R. D. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0324-8 · Cited by 86
Amyloid Clearance as a Treatment Target Against Alzheimer's Disease
Kurz, A., & Perneczky, R. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-102139 · Cited by 84
Structural analysis of neprilysin with various specific and potent inhibitors
Oefner, C., Roques, B. P., Fournie-Zaluski, M.-C., & Dale, G. E. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903027410 · Cited by 81
Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants
Wang, S. S. ‐., Chen, Y., & Chou, S. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.05.004 · Cited by 81
Comparison of Aβ levels in the brain of familial and sporadic Alzheimer's disease
Hellström‐Lindahl, E., Viitanen, M. H., & Marutle, A. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.03.007 · Cited by 78
Cerebrospinal fluid concentrations of corticotropin‐releasing hormone (CRH) and corticotropin (ACTH) are reduced in patients with Alzheimer's disease
May, C., Рапопорт, С. И., Tomai, T. P., Chrousos, G. P., & Gold, P. W. (1987) · Neurology · doi:10.1212/wnl.37.3.535 · Cited by 76
‘Prodromal Alzheimerʼs disease’: a more useful concept than mild cognitive impairment?
Dubois, B. (2000) · Current Opinion in Neurology · doi:10.1097/00019052-200008000-00001 · Cited by 76
β-Amyloid Production, Aggregation, and Clearance as Targets for Therapy in Alzheimer's Disease
Felice, F. G. D., & Ferreira, S. T. (2002) · Cellular and Molecular Neurobiology · doi:10.1023/a:1021832302524 · Cited by 75
Presynaptic protein synthesis required for NT-3-induced long-term synaptic modulation
Je, H. S., Ji, Y., Wang, Y., Yang, F., Wu, W., & Lu, B. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-1 · Cited by 74
Endothelin-converting enzymes and endothelin receptor B messenger RNAs are expressed in different neural cell species and these messenger RNAs are coordinately induced in neurons and astrocytes respectively following nerve injury
Nakagomi, S., Kiryu‐Seo, S., & Kiyama, H. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00345-6 · Cited by 74
Optimization of environmental and nutritional conditions for the production of alkaline protease by a newly isolated bacterium Bacillus cereus strain 146
Shafee, N., Aris, S. N. A. M., Rahman, R. N. Z. R. A., Basri, M., & Salleh, A. B. (2005) · Universiti Putra Malaysia Institutional Repository (Universiti Putra Malaysia) · Cited by 73
Do Cholinesterase Inhibitors Have Disease-Modifying Effects in Alzheimer??s Disease?
Giacobini, E. (2001) · CNS Drugs · doi:10.2165/00023210-200115020-00001 · Cited by 72
CSF somatostatin in Alzheimer's disease
Serby, M., Richardson, S. B., Twente, S., Siekierski, J., Corwin, J., & Rotrosen, J. (1984) · Neurobiology of Aging · doi:10.1016/0197-4580(84)90061-7 · Cited by 71
Functions of corticotropin‐releasing hormone in anthropoid primates: From brain to placenta
Power, M. L., & Schulkin, J. A. (2006) · American Journal of Human Biology · doi:10.1002/ajhb.20521 · Cited by 69
Endothelin-converting enzyme-1 is expressed in human cerebral cortex and protects against Alzheimer's disease
Funalot, B., Ouimet, T., Clapéron, A., Fallet‐Bianco, C., Delacourte, A., Epelbaum, J., Subkowski, T., Léonard, N., Codron, V., David, J. P., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001584 · Cited by 65
Estrogen blocks neurotoxic effects of β-amyloid (1–42) and induces neurite extension on B103 cells
Mook‐Jung, I., Joo, I.-S., Sohn, S., Kwon, H. J., Huh, K., & Jung, M. W. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00632-0 · Cited by 64
Neuropeptide Y receptor binding sites in human brain. Possible alteration in Alzheimer's disease
Martel, J., Alagar, R., Robitaille, Y., & Quirion, R. (1990) · Brain Research · doi:10.1016/0006-8993(90)90082-m · Cited by 61
Degradation of β-Amyloid by Proteolytic Antibody Light Chains
Rangan, S. K., Liu, R., Brune, D. C., Planque, S. A., Paul, S., & Sierks, M. R. (2003) · Biochemistry · doi:10.1021/bi035038d · Cited by 61
Identification of γ-Secretase Inhibitor Potency Determinants on Presenilin
Zhao, B., Yu, M., Neitzel, M. L., Marugg, J. L., Jagodzinski, J. J., Lee, M., Hu, K., Schenk, D., Yednock, T. A., & Basi, G. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708870200 · Cited by 61
Molecular Dynamics Simulation and Molecular Docking Studies of Angiotensin Converting Enzyme with Inhibitor Lisinopril and Amyloid Beta Peptide
Jalkute, C. B., Barage, S. H., Dhanavade, M. J., & Sonawane, K. D. (2013) · The Protein Journal · doi:10.1007/s10930-013-9492-3 · Cited by 60
Self-citation
Alzheimer's disease with spastic paraparesis and 'cotton wool' plaques: two pedigrees with PS-1 exon 9 deletions
Brooks, W. S. (2003) · Brain · doi:10.1093/brain/awg084 · Cited by 59
Alterations in Trk A, Trk B and Trk C Receptor Immunoreactivities in Parietal Cortex and Cerebellum in Alzheimer’s Disease
Savaskan, E., Müller-Spahn, F., Olivieri, G., Bruttel, S., Otten, U., Rosenberg, C., Hulette, C., & Höck, C. (2000) · European Neurology · doi:10.1159/000008229 · Cited by 58
Homology modeling, molecular docking and MD simulation studies to investigate role of cysteine protease from Xanthomonas campestris in degradation of Aβ peptide
Dhanavade, M. J., Jalkute, C. B., Barage, S. H., & Sonawane, K. D. (2013) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2013.09.021 · Cited by 58
Self-citation
Corticotropin‐Releasing Factor (CRF), CRF‐Binding Protein (CRF‐BP), and CRF/CRF‐BP Complex in Alzheimer's Disease and Control Postmortem Human Brain
Behan, D., Khongsaly, O., Owens, M. J., Chung, H., Nemeroff, C., & de Souza, E. D. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68052053.x · Cited by 57
Adeno-Associated Viral Vector Mediated Gene Delivery of Endothelin Converting Enzyme Reduces Aβ Deposits in APP+PS-1 Transgenic Mice
Carty, N. C., Nash, K., Lee, D. C., Mercer, M., Gottschall, P. E., Meyers, C., Muzyczka, N., Gordon, M. N., & Morgan, D. (2008) · Molecular Therapy · doi:10.1038/mt.2008.148 · Cited by 55
Structure of human Endothelin-converting Enzyme I Complexed with Phosphoramidon
Schulz, H., Dale, G. E., Karimi‐Nejad, Y., & Oefner, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.052 · Cited by 55
Apolipoprotein E immunoreactivity within neurofibrillary tangles: relationship to tau and PHF in Alzheimer's disease
Benzing, W. C., & Mufson, E. J. (1995) · Experimental Neurology · doi:10.1016/0014-4886(95)90021-7 · Cited by 53
Spinal fluid CRF reduction in Alzheimer's disease
Mouradian, M. M., Farah, J. M., Mohr, E., Fabbrini, G., O’Donohue, T. L., & Chase, T. N. (1986) · Neuropeptides · doi:10.1016/0143-4179(86)90010-7 · Cited by 53
Overview of Protein Aggregation in Single, Double, and Triple Neurodegenerative Brain Amyloidoses
Trojanowski, J. Q., & Mattson, M. P. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:1 · Cited by 53
Endothelin converting enzyme-1-, endothelin-1-, and endothelin-3-like immunoreactivity in the rat brain
Sluck, J. M., Lin, R. C. S., Katolik, L. I., Jeng, A. Y., & Lehmann, J. C. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00692-7 · Cited by 52
Inflammation in Alzheimer’s disease: insights from immunotherapy
Schott, J. M., & Révész, T. (2013) · Brain · doi:10.1093/brain/awt231 · Cited by 51
Selective localization of gelatinase A, an enzyme degrading ?-amyloid protein, in white matter microglia and in Schwann cells
Yamada, T., Miyazaki, K., Koshikawa, N., Takahashi, M., Akatsu, H., & Yamamoto, T. (1995) · Acta Neuropathologica · doi:10.1007/bf00309334 · Cited by 45
Endothelin-Converting Enzymes and Related Metalloproteases in Alzheimer's Disease
Pacheco‐Quinto, J., Herdt, A. R., Eckman, C. B., & Eckman, E. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129043 · Cited by 45
Brain choline acetyltransferase activity and neuropeptide Y concentrations in Alzheimer's disease
Foster, N. L., Tamminga, C. A., O’Donohue, T. L., Tanimoto, K., Bird, E. D., & Chase, T. N. (1986) · Neuroscience Letters · doi:10.1016/0304-3940(86)90015-7 · Cited by 45
Alzheimer's Disease: Presenilin 2-Sparing γ-Secretase Inhibition Is a Tolerable Aβ Peptide-Lowering Strategy
Borgegård, T., Gustavsson, S., Nilsson, C. B., Parpal, S., Klintenberg, R., Berg, A., Rosqvist, S., Serneels, L., Svensson, S., Olsson, F., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1451-12.2012 · Cited by 43
Physiological Roles of Corticotropin-Releasing Hormone Receptor Type 2.
Hashimoto, K., Makino, S., Asaba, K., & Nishiyama, M. (2001) · Endocrine Journal · doi:10.1507/endocrj.48.1 · Cited by 43
Insights into the molecular interactions between aminopeptidase and amyloid beta peptide using molecular modeling techniques
Dhanavade, M. J., & Sonawane, K. D. (2014) · Amino Acids · doi:10.1007/s00726-014-1740-0 · Cited by 41
Self-citation
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
O3-06-07 Multi-compartmental pharmacodynamic assessment of the functional gamma-secretase inhibitor LY450139 in PDAPP transgenic mice and non-transgenic mice
May, P. C., Yang, Z., Li, W., Hyslop, P. A., Siemers, E., & Boggs, L. N. (2004) · Neurobiology of Aging · doi:10.1016/s0197-4580(04)80220-3 · Cited by 39
Spotlight on BACE: The secretases as targets for treatment in Alzheimer disease
Dingwall, C. (2001) · Journal of Clinical Investigation · doi:10.1172/jci14402 · Cited by 38
Analysis of the Subsite Specificity of Rat Insulysin Using Fluorogenic Peptide Substrates
Song, E.-S., Mukherjee, A., Juliano, M. A., Pyrek, J. S., Goodman, J. P., Juliano, L., & Hersh, L. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008702200 · Cited by 38
Expression of Endothelin‐Converting Enzyme in Both Neuroblastoma and Glial Cell Lines and Its Localization in Rat Hippocampus
Barnes, K., Walkden, B. J., Wilkinson, T. C., & Turner, A. J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68020570.x · Cited by 38
The Search for γ-Secretase and Development of Inhibitors
Tsai, J.-Y., Wolfe, M. S., & Xia, W. (2002) · Current Medicinal Chemistry · doi:10.2174/0929867023370185 · Cited by 37
Coagulation Factor XIa Cleaves the RHDS Sequence and Abolishes the Cell Adhesive Properties of the Amyloid β-Protein
Saporito-Irwin, S. M., & Nostrand, W. E. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26265 · Cited by 34
Frontiers in Alzheimer’s disease therapeutics
Stone, J. G., Casadesús, G., Rothenberg, K. G., Siedlak, S. L., Wang, X., Zhu, X., Perry, G. L., Castellani, R. J., & Smith, M. A. (2010) · Therapeutic Advances in Chronic Disease · doi:10.1177/2040622310382817 · Cited by 32
Pathological and clinical heterogeneity of presenilin 1 gene mutations
Menéndez‐González, M. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6503 · Cited by 29
BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease
John, V. (2010) · doi:10.1002/9780470594087 · Cited by 27
Structural analysis of membrane-bound hECE-1 dimer using molecular modeling techniques: insights into conformational changes and Aβ1–42 peptide binding
Sonawane, K. D., & Barage, S. H. (2014) · Amino Acids · doi:10.1007/s00726-014-1887-8 · Cited by 25
Self-citation
Endothelin-Converting Enzyme in the Human Vasculature: Evidence for Differential Conversion of Big Endothelin-3 by Endothelial and Smooth-Muscle Cells
Davenport, A. P., Kuc, R. E., & Mockridge, J. W. (1998) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199800001-00002 · Cited by 23
Insight into molecular interactions of Aβ peptide and gelatinase from Enterococcus faecalis: a molecular modeling approach
Jalkute, C. B., Barage, S. H., & Sonawane, K. D. (2015) · RSC Advances · doi:10.1039/c4ra09354b · Cited by 23
Self-citation
Neuropeptides in Alzheimer`s Disease: From Pathophysiological Mechanisms to Therapeutic Opportunities
Dam, D. V., Dijck, A. V., Janssen, L., & Deyn, P. P. D. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310050001 · Cited by 21
Trophic Factor Effects on Septal Cholinergic Neuronsa
Svendsen, C. N., Cooper, J. D., & Sofroniew, M. V. (1991) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1991.tb00197.x · Cited by 21
Cellular basis of Alzheimer′s disease
Rajendran, L., Bali, J., Halima, S. B., Felmy, B., Goodger, Z. V., & Zurbriggen, S. (2010) · Annals of Indian Academy of Neurology · doi:10.4103/0972-2327.74251 · Cited by 20
A Polymorphic Microsatellite Repeat within the ECE-1c Promoter Is Involved in Transcriptional Start Site Determination, Human Evolution, and Alzheimer's Disease
Li, Y.-S., Seidel, K., Marschall, P., Klein, M. L., Hope, A., Schacherl, J., Schmitz, J., Menk, M., Schefe, J., Reinemund, J., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2636-12.2012 · Cited by 20
Dissecting the telomere region of barley chromosome 5HL using rice genomic sequences as references: new markers for tracking a complex region in breeding
Zhang, X., Li, C., Panozzo, J., Westcott, S., Zhang, G., Tay, A., Appels, R., Jones, M., & Lance, R. (2010) · Molecular Breeding · doi:10.1007/s11032-010-9408-2 · Cited by 20
An aminopeptidase from Streptomyces sp. KK565 degrades beta amyloid monomers, oligomers and fibrils
Yoo, C., Ahn, K., Park, J., Kim, M.-J., & Jo, S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.08.048 · Cited by 20
Contributions of Degradation and Brain-to-blood Elimination Across the Blood—Brain Barrier to Cerebral Clearance of Human Amyloid-β Peptide(1-40) in Mouse Brain
Ito, S., Matsumiya, K., Ohtsuki, S., Kamiie, J., & Terasaki, T. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.125 · Cited by 19
Caspases land on APP: One small step for apoptosis, one giant leap for amyloidosis?
Tanzi, R. E. (1999) · Nature Neuroscience · doi:10.1038/10133 · Cited by 17
Mapping the Active Site of Endothelin-Converting Enzyme-1 through Subsite Specificity and Mutagenesis Studies: A Comparison with Neprilysin
Johnson, G. D., Swenson, H. R., Ramage, R., & Ahn, K. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2708 · Cited by 17
Effects of 4-Hydroxy-Nonenal and Amyloid-β on Expression and Activity of Endothelin Converting Enzyme and Insulin Degrading Enzyme in SH-SY5Y Cells
Wang, R., Wang, S., Malter, J. S., & Wang, D.-S. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1066 · Cited by 16
Simulated Interactions between Endothelin Converting Enzyme and Aβ Peptide: Insights into Subsite Recognition and Cleavage Mechanism
Barage, S. H., Jalkute, C. B., Dhanavade, M. J., & Sonawane, K. D. (2014) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-014-9403-2 · Cited by 16
Self-citation
Dementia: from muddled diagnoses to treatable mechanisms
Hachinski, V., & Sposato, L. A. (2013) · Brain · doi:10.1093/brain/awt230 · Cited by 15
And four equals one: Presenilin takes the γ-secretase role by itself
Lessard, C. B., Wagner, S. L., & Koo, E. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016284108 · Cited by 14
Human Neutral Endopeptidase 24.11 (NEP, Enkephalinase) ; Function, Distribution and Release
Erdös, E. G., & Skidgel, R. A. (1988) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-1057-0_2 · Cited by 14
Exploring Mode of Phosphoramidon and Aβ Peptide Binding to hECE-1 by Molecular Dynamics and Docking Studies
Barage, S. H., & Sonawane, K. D. (2013) · Protein and Peptide Letters · doi:10.2174/09298665113209990091 · Cited by 13
Self-citation
Fibrillogenesis of β-amyloid
Allsop, D., Howlett, D. R., Christie, G., & Karran, E. H. (1998) · Biochemical Society Transactions · doi:10.1042/bst0260459 · Cited by 13
Neuropeptide signalling and cell-surface peptidases.
Turner, A. J. (1990) · PubMed · Cited by 10
Endothelin-converting enzyme-1 is expressed in human cerebral cortex and protects against Alzheimer's disease
Funalot, B., Ouimet, T., Clapéron, A., Fallet‐Bianco, C., Delacourte, A., Epelbaum, J., Subkowski, T., Léonard, N., Codron, V., David, J. P., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001612 · Cited by 10
Nucleotide sequence of the tissue-type plasminogen activator cDNA from human fetal lung cells
Sasaki, H., Saito, Y., Hayashi, M., Otsuka, K., & Niwa, M. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.12.5695 · Cited by 9
Evaluation of a Possible Role of Stigmatella aurantiaca ACE in Aβ Peptide Degradation: A Molecular Modeling Approach
Jalkute, C. B., & Sonawane, K. D. (2015) · Microbial Physiology · doi:10.1159/000370114 · Cited by 8
Self-citation
Clinical Trials for Disease‐Modifying Drugs Such as BACE Inhibitors
Hsu, H. H. (2010) · Wiley eBooks · doi:10.1002/9780470594087.ch9 · Cited by 6
Untitled work
(1998) · doi:10.1002/(sici)1097-4547(19980615)52:6

Flagged first, then by citations

6 of the 371 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Kehoe, 2009, 1, 3

Sorted by citations

Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease
Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820
“The Aβ plaque comprises of Aβ peptides obtained from amyloid precursor protein (APP) by the enzymatic cleavage via secretases (α, β and γ) [2].”
Background
Pathophysiologic relationship between Alzheimer's disease, cerebrovascular disease, and cardiovascular risk: A review and synthesis
Santos, C. Y., Snyder, P. J., Wu, W., Zhang, M., Echeverria, A., & Alber, J. (2017) · Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring · doi:10.1016/j.dadm.2017.01.005 · Cited by 431
Early long-term administration of the CSF1R inhibitor PLX3397 ablates microglia and reduces accumulation of intraneuronal amyloid, neuritic plaque deposition and pre-fibrillar oligomers in 5XFAD mouse model of Alzheimer’s disease
Sosna, J., Philipp, S., Albay, R., Reyes-Ruiz, J. M., Baglietto-Vargas, D., LaFerla, F. M., & Glabe, C. G. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0244-x · Cited by 406
Shaping the Nrf2-ARE-related pathways in Alzheimer’s and Parkinson’s diseases
Fão, L., Mota, S. I., & Rego, A. C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100942 · Cited by 281
Plasma neuronal exosomes serve as biomarkers of cognitive impairment in HIV infection and Alzheimer’s disease
Pulliam, L., Sun, B., Mustapić, M., Chawla, S., & Kapogiannis, D. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-018-0695-4 · Cited by 246

See all 588

Authors: Barage, S. H., & Sonawane, K. D.
Affiliations: Shivaji University (IN)
Corresponding author: Sonawane, Kailas D.
ORCID: Barage, Sagar H.
Sonawane, Kailas D.
Venue: Neuropeptides
Publisher: Elsevier BV
Published: 2015-08
Volume: 52
Pages: 1-18
ISSN: 0143-4179 (ISSN-L)
DOI: 10.1016/j.npep.2015.06.008
OpenAlex: W2099751992
Cited by: 579
References: 371
Citations by year: 2026: 22 · 2025: 57 · 2024: 75 · 2023: 69 · 2022: 58 · 2021: 67 · 2020: 59 · 2019: 58 · 2018: 51 · 2017: 33 · 2016: 24 · 2015: 5
FWCI: 4.66
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuropeptides (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
Keywords: Alzheimer's disease, amyloid hypothesis, amyloid-beta, amyloid plaques, tau protein, cerebrospinal fluid biomarkers, cholinergic neurotransmission, neurodegeneration, Alzheimer's disease therapeutics, genetic risk factors
MeSH terms: Acetylcholine, Alzheimer Disease, Animals, Brain, Humans, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Neurofibrillary Tangles, tau Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks