Cited by 20

The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.

MicroRNA-Target Interaction Regulatory Network in Alzheimer’s Disease

Turk, Aleksander, Kunej, Tanja, Peterlin, Borut·2021·Journal of Personalized Medicine

Abstract

Alzheimer’s Disease (AD) is a progressive neurodegenerative disorder and the most common cause of dementia; however, early diagnosis of the disease is challenging. Research suggests that biomarkers found in blood, such as microRNAs (miRNA), may be promising for AD diagnostics. Experimental data on miRNA–target interactions (MTI) associated with AD are scattered across databases and publications, thus making the identification of promising miRNA biomarkers for AD difficult. In response to this, a list of experimentally validated AD-associated MTIs was obtained from miRTarBase. Cytoscape was used to create a visual MTI network. STRING software was used for protein–protein interaction analysis and mirPath was used for pathway enrichment analysis. Several targets regulated by multiple miRNAs were identified, including: BACE1, APP, NCSTN, SP1, SIRT1, and PTEN. The miRNA with the highest numbers of interactions in the network were: miR-9, miR-16, miR-34a, miR-106a, miR-107, miR-125b, miR-146, and miR-181c. The analysis revealed seven subnetworks, representing disease modules which have a potential for further biomarker development. The obtained MTI network is not yet complete, and additional studies are needed for the comprehensive understanding of the AD-associated miRNA targetome.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/jpm11121275

Cites

10 of 10 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Network of experimentally validated MTIs associated with AD visualized using the Cytoscape software. Orange-colored nodes represent target genes while blue-colored nodes represent miRNAs. Each edge represents an experimentally validated interaction between a miRNA and its target. (a) The largest subnetwork identified in the data set, consisting of 18 miRNAs and 15 target genes, with a total of 37 MTIs. (b) Smaller subnetworks and miRNA–target pairs identified in the data set.
Figure 1 Network of experimentally validated MTIs associated with AD visualized using the Cytoscape software. Orange-colored nodes represent target genes while blue-colored nodes represent miRNAs. Each edge represents an experimentally validated interaction between a miRNA and its target. (a) The largest subnetwork identified in the data set, consisting of 18 miRNAs and 15 target genes, with a total of 37 MTIs. (b) Smaller subnetworks and miRNA–target pairs identified in the data set.CC BY · PubMed Central
Figure 2 Protein–protein interaction network of 43 AD-associated miRNA targets using STRING software. The colors of connections between nodes represent the type interaction between the two proteins. The most reliable of these connections are “known interactions” from curated databases and experiments. Common gene neighborhoods, fusions, and co-occurrences as well as textmining, co-expression, and protein homology are considered less reliable connections and tend to require independent verification.
Figure 2 Protein–protein interaction network of 43 AD-associated miRNA targets using STRING software. The colors of connections between nodes represent the type interaction between the two proteins. The most reliable of these connections are “known interactions” from curated databases and experiments. Common gene neighborhoods, fusions, and co-occurrences as well as textmining, co-expression, and protein homology are considered less reliable connections and tend to require independent verification.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 10 references

Research works printed but not linked: 130

  1. Zhao, 2020, microRNA-Based Biomarkers in Alzheimer’s Disease (AD), Front. Neurosci., 14, 585432, 10.3389/fnins.2020.585432 · DOI
  2. Blennow, 2018, Biomarkers for Alzheimer’s disease: Current status and prospects for the future, J. Intern. Med., 284, 643, 10.1111/joim.12816 · DOI · Paper page
  3. Vos, 2016, GBD 2015 Disease and Injury Incidence and Prevalence Collaborators, Global, regional, and national incidence, prevalence, and years lived with disability for 310 diseases and injuries, 1990–2015: A systematic analysis for the Global Burden of Disease Study 2015, Lancet, 388, 1545, 10.1016/S0140-6736(16)31678-6 · DOI · Paper page
  4. Dubois, 2014, Advancing research diagnostic criteria for Alzheimer’s disease: The IWG-2 criteria, Lancet Neurol., 13, 614, 10.1016/S1474-4422(14)70090-0 · DOI · Paper page
  5. Palmqvist, 2019, Performance of Fully Automated Plasma Assays as Screening Tests for Alzheimer Disease–Related β-Amyloid Status, JAMA Neurol., 76, 1060, 10.1001/jamaneurol.2019.1632 · DOI · Paper page
  6. Brickman, 2021, Plasma p-tau181, p-tau217, and other blood-based Alzheimer’s disease biomarkers in a multi-ethnic, community study, Alzheimer’s Dement., 17, 1353, 10.1002/alz.12301 · DOI · Paper page
  7. Ossenkoppele, 2021, Tau PET correlates with different Alzheimer’s disease-related features compared to CSF and plasma p-tau biomarkers, EMBO Mol. Med., 13, e14398, 10.15252/emmm.202114398 · DOI
  8. Cullen, 2021, Plasma biomarkers of Alzheimer’s disease improve prediction of cognitive decline in cognitively unimpaired elderly populations, Nat. Commun., 12, 3555, 10.1038/s41467-021-23746-0 · DOI
  9. Karikari, 2020, Blood phosphorylated tau 181 as a biomarker for Alzheimer’s disease: A diagnostic performance and prediction modelling study using data from four prospective cohorts, Lancet Neurol., 19, 422, 10.1016/S1474-4422(20)30071-5 · DOI · Paper page
  10. Hrovatin, 2018, Classification of miRNA-related sequence variations, Epigenomics, 10, 463, 10.2217/epi-2017-0126 · DOI
  11. Friedman, 2008, Most mammalian mRNAs are conserved targets of microRNAs, Genome Res., 19, 92, 10.1101/gr.082701.108 · DOI · Paper page
  12. Hammond, 2015, An overview of microRNAs, Adv. Drug Deliv. Rev., 87, 3, 10.1016/j.addr.2015.05.001 · DOI
  13. Wang, 2019, MicroRNAs in Alzheimer’s Disease, Front. Genet., 10, 153, 10.3389/fgene.2019.00153 · DOI
  14. Vergallo, 2021, MiRNA-15b and miRNA-125b are associated with regional Aβ-PET and FDG-PET uptake in cognitively normal individuals with subjective memory complaints, Transl. Psychiatry, 11, 78, 10.1038/s41398-020-01184-8 · DOI
  15. Ballard, 2011, Alzheimer’s disease, Lancet, 377, 1019, 10.1016/S0140-6736(10)61349-9 · DOI · Paper page
  16. Ansari, 2019, miR-146a and miR-181a are involved in the progression of mild cognitive impairment to Alzheimer’s disease, Neurobiol. Aging, 82, 102, 10.1016/j.neurobiolaging.2019.06.005 · DOI
  17. Xie, 2016, Increased Serum miR-206 Level Predicts Conversion from Amnestic Mild Cognitive Impairment to Alzheimer’s Disease: A 5-Year Follow-up Study, J. Alzheimer’s Dis., 55, 509, 10.3233/JAD-160468 · DOI
  18. Henry, 2018, Inhibition of miR-155 Limits Neuroinflammation and Improves Functional Recovery After Experimental Traumatic Brain Injury in Mice, Neurotherapeutics, 16, 216, 10.1007/s13311-018-0665-9 · DOI
  19. Lukiw, 2012, NF-ĸB-regulated micro RNAs (miRNAs) in primary human brain cells, Exp. Neurol., 235, 484, 10.1016/j.expneurol.2011.11.022 · DOI · Paper page
  20. Jaber, 2019, Addressing Alzheimer’s Disease (AD) Neuropathology Using Anti-microRNA (AM) Strategies, Mol. Neurobiol., 56, 8101, 10.1007/s12035-019-1632-0 · DOI
  21. Abuelezz, 2021, MicroRNAs as Potential Orchestrators of Alzheimer’s Disease-Related Pathologies: Insights on Current Status and Future Possibilities, Front. Aging Neurosci., 13, 743573, 10.3389/fnagi.2021.743573 · DOI
  22. Chou, 2017, miRTarBase update 2018: A resource for experimentally validated microRNA-target interactions, Nucleic Acids Res., 46, D296, 10.1093/nar/gkx1067 · DOI
  23. Shannon, 2003, Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks, Genome Res., 13, 2498, 10.1101/gr.1239303 · DOI · Paper page
  24. Szklarczyk, 2020, The STRING database in 2021: Customizable protein–protein networks, and functional characterization of user-uploaded gene/measurement sets, Nucleic Acids Res., 49, D605, 10.1093/nar/gkaa1074 · DOI · Paper page
  25. Vlachos, 2015, DIANA-miRPath v3.0: Deciphering microRNA function with experimental support, Nucleic Acids Res., 43, W460, 10.1093/nar/gkv403 · DOI
  26. Shioya, 2010, Aberrant microRNA expression in the brains of neurodegenerative diseases: miR-29a decreased in Alzheimer disease brains targets neurone navigator 3, Neuropathol. Appl. Neurobiol., 36, 320, 10.1111/j.1365-2990.2010.01076.x · DOI · Paper page
  27. Li, 2016, miR-98-5p Acts as a Target for Alzheimer’s Disease by Regulating Aβ Production Through Modulating SNX6 Expression, J. Mol. Neurosci., 60, 413, 10.1007/s12031-016-0815-7 · DOI
  28. Lei, 2015, Downregulated miR-29c correlates with increased BACE1 expression in sporadic Alzheimer’s disease, Int. J. Clin. Exp. Pathol., 8, 1565
  29. Zhang, 2013, Regulation of STAT3 by miR-106a is linked to cognitive impairment in ovariectomized mice, Brain Res., 1503, 43, 10.1016/j.brainres.2013.01.052 · DOI
  30. Villa, 2013, Expression of the Transcription Factor Sp1 and its Regulatory hsa-miR-29b in Peripheral Blood Mononuclear Cells from Patients with Alzheimer’s Disease, J. Alzheimer’s Dis., 35, 487, 10.3233/JAD-122263 · DOI
  31. Absalon, 2013, MiR-26b, Upregulated in Alzheimer’s Disease, Activates Cell Cycle Entry, Tau-Phosphorylation, and Apoptosis in Postmitotic Neurons, J. Neurosci., 33, 14645, 10.1523/JNEUROSCI.1327-13.2013 · DOI · Paper page
  32. Benito, 2014, Micro RNA-125b induces tau hyperphosphorylation and cognitive deficits in Alzheimer’s disease, EMBO J., 33, 1667, 10.15252/embj.201387576 · DOI · Paper page
  33. Yan, H., Xu, T., Zhao, H., Lee, K.-C., Wang, H.-Y., and Zhang, Y. (2013). Isoflurane Increases Neuronal Cell Death Vulnerability by Downregulating miR-214. PLoS ONE, 8. · DOI
  34. Ghanbari, 2016, Genome-wide identification of microRNA-related variants associated with risk of Alzheimer’s disease, Sci. Rep., 6, 28387, 10.1038/srep28387 · DOI
  35. Schonrock, 2011, Target Gene Repression Mediated by miRNAs miR-181c and miR-9 Both of Which Are Down-regulated by Amyloid-β, J. Mol. Neurosci., 46, 324, 10.1007/s12031-011-9587-2 · DOI
  36. Zhang, 2016, MicroRNA-146a represses LRP2 translation and leads to cell apoptosis in Alzheimer’s disease, FEBS Lett., 590, 2190, 10.1002/1873-3468.12229 · DOI
  37. Hebert, 2009, MicroRNA regulation of Alzheimer’s Amyloid precursor protein expression, Neurobiol. Dis., 33, 422, 10.1016/j.nbd.2008.11.009 · DOI · Paper page
  38. Song, 2009, MicroRNA-205 inhibits tumor cell migration through down-regulating the expression of the LDL receptor-related protein 1, Biochem. Biophys. Res. Commun., 388, 400, 10.1016/j.bbrc.2009.08.020 · DOI
  39. Li, 2016, miR-302 Attenuates Amyloid-β-Induced Neurotoxicity through Activation of Akt Signaling, J. Alzheimer’s Dis., 50, 1083, 10.3233/JAD-150741 · DOI
  40. Wang, 2010, miR-107 Regulates Granulin/Progranulin with Implications for Traumatic Brain Injury and Neurodegenerative Disease, Am. J. Pathol., 177, 334, 10.2353/ajpath.2010.091202 · DOI
  41. Jayadev, 2013, Presenilin 2 influences miR146 level and activity in microglia, J. Neurochem., 127, 592, 10.1111/jnc.12400 · DOI · Paper page
  42. Li, 2016, MicroRNA-613 regulates the expression of brain-derived neurotrophic factor in Alzheimer’s disease, Biosci. Trends, 10, 372, 10.5582/bst.2016.01127 · DOI
  43. Li, 2016, Neuroprotective Effect of Osthole on Neuron Synapses in an Alzheimer’s Disease Cell Model via Upregulation of MicroRNA-9, J. Mol. Neurosci., 60, 71, 10.1007/s12031-016-0793-9 · DOI · Paper page
  44. Parsi, 2015, Preclinical Evaluation of miR-15/107 Family Members as Multifactorial Drug Targets for Alzheimer’s Disease, Mol. Ther. Nucleic Acids, 4, e256, 10.1038/mtna.2015.33 · DOI · Paper page
  45. Jovicic, A., Jolissaint, J.F.Z., Moser, R., Santos, M.D.F.S.S., and Luthi-Carter, R. (2013). MicroRNA-22 (miR-22) Overexpression Is Neuroprotective via General Anti-Apoptotic Effects and May also Target Specific Huntington’s Disease-Related Mechanisms. PLoS ONE, 8. · DOI
  46. Wang, 2016, MicroRNA-146a suppresses ROCK1 allowing hyperphosphorylation of tau in Alzheimer’s disease, Sci. Rep., 6, 26697, 10.1038/srep26697 · DOI
  47. Pogue, 2010, Micro RNA-125b (miRNA-125b) function in astrogliosis and glial cell proliferation, Neurosci. Lett., 476, 18, 10.1016/j.neulet.2010.03.054 · DOI
  48. Zhang, 2016, MiR-299-5p regulates apoptosis through autophagy in neurons and ameliorates cognitive capacity in APPswe/PS1dE9 mice, Sci. Rep., 6, 24566, 10.1038/srep24566 · DOI
  49. Lau, 2013, Alteration of the micro RNA network during the progression of Alzheimer’s disease, EMBO Mol. Med., 5, 1613, 10.1002/emmm.201201974 · DOI · Paper page
  50. Agostini, 2011, Neuronal differentiation by TAp73 is mediated by microRNA-34a regulation of synaptic protein targets, Proc. Natl. Acad. Sci. USA, 108, 21093, 10.1073/pnas.1112061109 · DOI
  51. Liu, 2016, MicroRNA-26b is upregulated in a double transgenic mouse model of Alzheimer’s disease and promotes the expression of amyloid-β by targeting insulin-like growth factor 1, Mol. Med. Rep., 13, 2809, 10.3892/mmr.2016.4860 · DOI
  52. Ubhi, 2013, Widespread microRNA dysregulation in multiple system atrophy-disease-related alteration in miR-96, Eur. J. Neurosci., 39, 1026, 10.1111/ejn.12444 · DOI
  53. Wang, 2008, The Expression of MicroRNA miR-107 Decreases Early in Alzheimer’s Disease and May Accelerate Disease Progression through Regulation of β-Site Amyloid Precursor Protein-Cleaving Enzyme 1, J. Neurosci., 28, 1213, 10.1523/JNEUROSCI.5065-07.2008 · DOI · Paper page
  54. Liu, 2016, miR-106b inhibits tau phosphorylation at Tyr18 by targeting Fyn in a model of Alzheimer’s disease, Biochem. Biophys. Res. Commun., 478, 852, 10.1016/j.bbrc.2016.08.037 · DOI
  55. Vilardo, 2010, MicroRNA-101 Regulates Amyloid Precursor Protein Expression in Hippocampal Neurons, J. Biol. Chem., 285, 18344, 10.1074/jbc.M110.112664 · DOI
  56. Papadopoulou, 2008, Loss of microRNA cluster miR-29a/b-1 in sporadic Alzheimer’s disease correlates with increased BACE1/β-secretase expression, Proc. Natl. Acad. Sci. USA, 105, 6415, 10.1073/pnas.0710263105 · DOI · Paper page
  57. Zhao, Y., Alexandrov, P.N., Jaber, V., and Lukiw, W.J. (2016). Deficiency in the Ubiquitin Conjugating Enzyme UBE2A in Alzheimer’s Disease (AD) is Linked to Deficits in a Natural Circular miRNA-7 Sponge (circRNA; ciRS-7). Genes, 7. · DOI
  58. Pereira, 2016, Recombinant pre-miR-29b for Alzheimer’s disease therapeutics, Sci. Rep., 6, 19946, 10.1038/srep19946 · DOI
  59. Patel, 2008, MicroRNAs can regulate human APP levels, Mol. Neurodegener., 3, 10, 10.1186/1750-1326-3-10 · DOI
  60. Wang, 2015, MicroRNA-138 promotes tau phosphorylation by targeting retinoic acid receptor alpha, FEBS Lett., 589, 726, 10.1016/j.febslet.2015.02.001 · DOI
  61. Liu, 2016, MicroRNA-107 prevents amyloid-beta induced blood-brain barrier disruption and endothelial cell dysfunction by targeting Endophilin-1, Exp. Cell Res., 343, 248, 10.1016/j.yexcr.2016.03.026 · DOI
  62. Zheng, 2016, MicroRNA-511 Binds to FKBP5 mRNA, Which Encodes a Chaperone Protein, and Regulates Neuronal Differentiation, J. Biol. Chem., 291, 17897, 10.1074/jbc.M116.727941 · DOI
  63. Long, 2011, MicroRNA-101 downregulates Alzheimer’s amyloid-β precursor protein levels in human cell cultures and is differentially expressed, Biochem. Biophys. Res. Commun., 404, 889, 10.1016/j.bbrc.2010.12.053 · DOI
  64. Wu, 2016, The Protective Role of microRNA-200c in Alzheimer’s Disease Pathologies Is Induced by Beta Amyloid-Triggered Endoplasmic Reticulum Stress, Front. Mol. Neurosci., 9, 140, 10.3389/fnmol.2016.00140 · DOI
  65. Long, 2014, MicroRNA-339-5p Down-regulates Protein Expression of β-Site Amyloid Precursor Protein-Cleaving Enzyme 1 (BACE1) in Human Primary Brain Cultures and Is Reduced in Brain Tissue Specimens of Alzheimer Disease Subjects, J. Biol. Chem., 289, 5184, 10.1074/jbc.M113.518241 · DOI · Paper page
  66. Zong, 2011, miR-29c regulates BACE1 protein expression, Brain Res., 1395, 108, 10.1016/j.brainres.2011.04.035 · DOI · Paper page
  67. Zhang, 2016, MiR-195 dependent roles of mitofusin2 in the mitochondrial dysfunction of hippocampal neurons in SAMP8 mice, Brain Res., 1652, 135, 10.1016/j.brainres.2016.09.047 · DOI
  68. Stutzmann, 2005, Calcium Dysregulation, IP3 Signaling, and Alzheimer’s Disease, Neuroscientist, 11, 110, 10.1177/1073858404270899 · DOI
  69. Chang, 2012, Role of p53 in Neurodegenerative Diseases, Neurodegener. Dis., 9, 68, 10.1159/000329999 · DOI
  70. Zhang, 2014, Towards Understanding the Roles of Heparan Sulfate Proteoglycans in Alzheimer’s Disease, BioMed Res. Int., 2014, 516028
  71. Lehrer, 2018, Glioma and Alzheimer’s Disease, J. Alzheimer’s Dis. Rep., 2, 213, 10.3233/ADR-180084 · DOI
  72. Penzes, 2011, Impaired regulation of synaptic actin cytoskeleton in Alzheimer’s disease, Brain Res. Rev., 67, 184, 10.1016/j.brainresrev.2011.01.003 · DOI
  73. Vasco, 2018, The Phosphoinositide Signal Transduction Pathway in the Pathogenesis of Alzheimer’s Disease, Curr. Alzheimer Res., 15, 355, 10.2174/1567205014666170829100230 · DOI
  74. Greene, 2016, Tight junction modulation of the blood brain barrier: CNS delivery of small molecules, Tissue Barriers, 4, e1138017, 10.1080/21688370.2015.1138017 · DOI
  75. Berezin, 2014, Targeting of ECM molecules and their metabolizing enzymes and receptors for the treatment of CNS diseases, Prog. Brain Res., 214, 353, 10.1016/B978-0-444-63486-3.00015-3 · DOI
  76. Caltagarone, 2007, Focal adhesions regulate Aβ signaling and cell death in Alzheimer’s disease, Biochim. Biophys. Acta (BBA)—Mol. Basis Dis., 1772, 438, 10.1016/j.bbadis.2006.11.007 · DOI · Paper page
  77. Jayaraman, 2014, Alzheimer’s Disease and Type 2 Diabetes: Multiple Mechanisms Contribute to Interactions, Curr. Diabetes Rep., 14, 476, 10.1007/s11892-014-0476-2 · DOI
  78. Maiese, 2018, Forkhead Transcription Factors: Formulating a FOXO Target for Cognitive Loss, Curr. Neurovasc. Res., 14, 415, 10.2174/1567202614666171116102911 · DOI
  79. Frank, 1999, Increased cerebrospinal fluid cAMP levels in Alzheimer’s disease, Brain Res., 846, 265, 10.1016/S0006-8993(99)01981-2 · DOI
  80. Haase, 2013, Amyloid- Peptides Activate 1-Adrenergic Cardiovascular Receptors, Hypertension, 62, 966, 10.1161/HYPERTENSIONAHA.113.01348 · DOI
  81. Sevush, 1998, Platelet Activation in Alzheimer Disease, Arch. Neurol., 55, 530, 10.1001/archneur.55.4.530 · DOI
  82. Pereira, 2014, The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: Implications for Alzheimer’s disease, Biochim. Biophys. Acta (BBA)—Mol. Basis Dis., 1842, 1444, 10.1016/j.bbadis.2014.05.003 · DOI
  83. Mielke, 2010, Alterations of the Sphingolipid Pathway in Alzheimer’s Disease: New Biomarkers and Treatment Targets?, NeuroMol. Med., 12, 331, 10.1007/s12017-010-8121-y · DOI
  84. Akasaka-Manya, K., and Manya, H. (2020). The Role of APP O-Glycosylation in Alzheimer’s Disease. Biomolecules, 10. · DOI
  85. Zhu, 2002, The Role of Mitogen-Activated Protein Kinase Pathways in Alzheimer’s Disease, Neurosignals, 11, 270, 10.1159/000067426 · DOI
  86. McKay, 2019, Peri-Infarct Upregulation of the Oxytocin Receptor in Vascular Dementia, J. Neuropathol. Exp. Neurol., 78, 436, 10.1093/jnen/nlz023 · DOI
  87. Malik, 2015, Genetics of CD33 in Alzheimer’s disease and acute myeloid leukemia, Hum. Mol. Genet., 24, 3557, 10.1093/hmg/ddv092 · DOI
  88. Oddo, 2012, The role of mTOR signaling in Alzheimer disease, Front. Biosci., 4, 941, 10.2741/s310 · DOI
  89. Angeli, 2020, Altered Expression of Glial Gap Junction Proteins Cx43, Cx30, and Cx47 in the 5XFAD Model of Alzheimer’s Disease, Front. Neurosci., 14, 582934, 10.3389/fnins.2020.582934 · DOI
  90. Woo, 2011, Expression of ErbB4 in the neurons of Alzheimer’s disease brain and APP/PS1 mice, a model of Alzheimer’s disease, Anat. Cell Biol., 44, 116, 10.5115/acb.2011.44.2.116 · DOI
  91. Curtis, 2020, Mini-review: Role of the PI3K/Akt pathway and tyrosine phosphatases in Alzheimer’s disease susceptibility, Ann. Hum. Genet., 85, 1, 10.1111/ahg.12410 · DOI
  92. Monsonego, 2013, CD4 T cells in immunity and immunotherapy of Alzheimer’s disease, Immunology, 139, 438, 10.1111/imm.12103 · DOI
  93. Watson, 2011, The Neurotrophins and Their Role in Alzheimers Disease, Curr. Neuropharmacol., 9, 559, 10.2174/157015911798376190 · DOI
  94. Bernhardi, 2015, Role of TGFβ signaling in the pathogenesis of Alzheimer’s disease, Front. Cell. Neurosci., 9, 426
  95. Uddin, 2020, Estrogen Signaling in Alzheimer’s Disease: Molecular Insights and Therapeutic Targets for Alzheimer’s Dementia, Mol. Neurobiol., 57, 2654, 10.1007/s12035-020-01911-8 · DOI · Paper page
  96. Choi, 2021, Association between dementia and hepatitis B and C virus infection, Medicine, 100, e26476, 10.1097/MD.0000000000026476 · DOI
  97. Zhang, 2021, Roles and Mechanisms of Axon-Guidance Molecules in Alzheimer’s Disease, Mol. Neurobiol., 58, 3290, 10.1007/s12035-021-02311-2 · DOI
  98. Yamazaki, 2019, Selective loss of cortical endothelial tight junction proteins during Alzheimer’s disease progression, Brain, 142, 1077, 10.1093/brain/awz011 · DOI · Paper page
  99. Hong, 2020, TRP Channels as Emerging Therapeutic Targets for Neurodegenerative Diseases, Front. Physiol., 11, 238, 10.3389/fphys.2020.00238 · DOI
  100. Huh, 2016, The reemergence of long-term potentiation in aged Alzheimer’s disease mouse model, Sci. Rep., 6, 29152, 10.1038/srep29152 · DOI
  101. Nixon, 2005, Endosome function and dysfunction in Alzheimer’s disease and other neurodegenerative diseases, Neurobiol. Aging, 26, 373, 10.1016/j.neurobiolaging.2004.09.018 · DOI
  102. Wang, 2019, Therapeutic Potential of AMP-Activated Protein Kinase in Alzheimer’s Disease, J. Alzheimer’s Dis., 68, 33, 10.3233/JAD-181043 · DOI
  103. Sanders, 2020, Phosphodiesterase Inhibitors for Alzheimer’s Disease: A Systematic Review of Clinical Trials and Epidemiology with a Mechanistic Rationale, J. Alzheimer’s Dis. Rep., 4, 185, 10.3233/ADR-200191 · DOI
  104. Irwin, 2020, A Positive Feedback Loop of Hippo- and c-Jun-Amino-Terminal Kinase Signaling Pathways Regulates Amyloid-Beta-Mediated Neurodegeneration, Front. Cell Dev. Biol., 8, 117, 10.3389/fcell.2020.00117 · DOI
  105. Park, 2019, Dysregulated Fc gamma receptor–mediated phagocytosis pathway in Alzheimer’s disease: Network-based gene expression analysis, Neurobiol. Aging, 88, 24, 10.1016/j.neurobiolaging.2019.12.001 · DOI
  106. Maillet, 2003, Crosstalk between Rap1 and Rac regulates secretion of sAPPα, Nature, 5, 633
  107. Vogrinc, D., Goričar, K., Kunej, T., and Dolžan, V. (2021). Systematic Search for Novel Circulating Biomarkers Associated with Extracellular Vesicles in Alzheimer’s Disease: Combining Literature Screening and Database Mining Approaches. J. Pers. Med., 11. · DOI
  108. Das, 2017, Role of BACE1 in Alzheimer’s synaptic function, Transl. Neurodegener., 6, 23, 10.1186/s40035-017-0093-5 · DOI
  109. Wong, 2011, Amyloid Precursor Protein Processing and Alzheimer’s Disease, Annu. Rev. Neurosci., 34, 185, 10.1146/annurev-neuro-061010-113613 · DOI · Paper page
  110. Kaether, 2006, Assembly, Trafficking and Function of γ-Secretase, Neurodegener. Dis., 3, 275, 10.1159/000095267 · DOI
  111. Yoon, 2014, Differential roles of Sirt1 in HIF-1α and HIF-2α mediated hypoxic responses, Biochem. Biophys. Res. Commun., 444, 36, 10.1016/j.bbrc.2014.01.001 · DOI
  112. Kleszka, 2020, Hypoxia-inducible factor-2α is crucial for proper brain development, Sci. Rep., 10, 19146, 10.1038/s41598-020-75838-4 · DOI
  113. Elalla, 2013, The role of sirtuins in Alzheimer’s disease, Front. Aging Neurosci., 5, 16
  114. Citron, 2008, Transcription factor Sp1 dysregulation in Alzheimer’s disease, J. Neurosci. Res., 86, 2499, 10.1002/jnr.21695 · DOI · Paper page
  115. Knafo, 2016, PTEN recruitment controls synaptic and cognitive function in Alzheimer’s models, Nat. Neurosci., 19, 443, 10.1038/nn.4225 · DOI
  116. Frere, 2016, Targeting PTEN interactions for Alzheimer’s disease, Nat. Neurosci., 19, 416, 10.1038/nn.4248 · DOI
  117. Chen, 2021, Revisiting the Relationship between Alzheimer’s Disease and Cancer with a circRNA Perspective, Front. Cell Dev. Biol., 9, 647197, 10.3389/fcell.2021.647197 · DOI
  118. Ou, 2013, Does Alzheimer’s Disease Protect against Cancers? A Nationwide Population-Based Study, Neuroepidemiology, 40, 42, 10.1159/000341411 · DOI
  119. Liu, 2013, Transcriptional signaling pathways inversely regulated in Alzheimer’s disease and glioblastoma multiform, Sci. Rep., 3, 3467, 10.1038/srep03467 · DOI
  120. Musicco, 2013, Inverse occurrence of cancer and Alzheimer disease: A population-based incidence study, Neurology, 81, 322, 10.1212/WNL.0b013e31829c5ec1 · DOI · Paper page
  121. Rinaldi, 2021, The biological pathways of Alzheimer disease: A review, AIMS Neurosci., 8, 86, 10.3934/Neuroscience.2021005 · DOI
  122. Caruana, 2015, Longitudinal studies, J. Thorac. Dis., 7, E537
  123. Wang, 2018, The microRNA-1908 up-regulation in the peripheral blood cells impairs amyloid clearance by targeting ApoE, Int. J. Geriatr. Psychiatry, 33, 980, 10.1002/gps.4881 · DOI
  124. Deng, 2014, The miR-193a-3p regulated PSEN1 gene suppresses the multi-chemoresistance of bladder cancer, Biochim. Biophys. Acta (BBA)—Mol. Basis Dis., 1852, 520, 10.1016/j.bbadis.2014.12.014 · DOI
  125. Robinson, 2017, Multiplexing Biomarker Methods, Proteomics and Considerations for Alzheimer’s Disease, Proteom. Methods Neuropsychiatry Res., 974, 21, 10.1007/978-3-319-52479-5_2 · DOI
  126. Maoz, 2017, Alzheimer’s Disease and ncRNAs, Neuroepigenom. Aging Dis., 978, 337, 10.1007/978-3-319-53889-1_18 · DOI
  127. Lugli, G., Cohen, A.M., Bennett, D.A., Shah, R., Fields, C., Hernandez, A.G., and Smalheiser, N.R. (2015). Plasma Exosomal miRNAs in Persons with and without Alzheimer Disease: Altered Expression and Prospects for Biomarkers. PLoS ONE, 10. · DOI · Paper page
  128. Leidinger, 2013, A blood based 12-miRNA signature of Alzheimer disease patients, Genome Biol., 14, R78, 10.1186/gb-2013-14-7-r78 · DOI
  129. Zetterberg, 2019, Blood-based molecular biomarkers for Alzheimer’s disease, Mol. Brain, 12, 26, 10.1186/s13041-019-0448-1 · DOI
  130. Zhao, 2013, Regulation of TREM2 expression by an NF-ĸB-sensitive miRNA-34a, NeuroReport, 24, 318, 10.1097/WNR.0b013e32835fb6b0 · DOI

Cited by

Sorted by citations

Metadata

Authors
Turk, A., Kunej, T., & Peterlin, B.
Affiliations
  • Department of Animal Science, Biotechnical Faculty, University of Ljubljana, 1230 Domžale, Slovenia
  • Clinical Institute of Genomic Medicine, University Medical Centre Ljubljana, 1000 Ljubljana, Slovenia
Venue
Journal of Personalized Medicine
Publisher
MDPI AG
Published
2021-12-02
Volume
11
Issue
12
Pages
1275
ISSN
2075-4426
Cited by
20
References
10
Language
en
Funders
Slovenian Research Agency (P4-0220)

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