본문 바로가기
KERD
논문KCI 등재

Emerging roles of 14-3-3γ in the brain disorder

2

조회

0

다운로드

0

인용

0

참고문헌

키워드

주제분류화학

초록

14-3-3 proteins are mostly expressed in the brain and are closely involved in numerous brain functions and various brain disorders. Among the isotypes of the 14-3-3 proteins, 14-3-3γ is mainly expressed in neurons and is highly produced during brain development, which could indicate that it has a significance in neural development. Furthermore, the distinctive levels of temporally and locally regulated 14-3-3γ expression in various brain disorders suggest that it could play a substantial role in brain plasticity of the diseased states. In this review, we introduce the various brain disorders reported to be involved with 14-3-3γ, and summarize the changes of 14-3-3γ expression in each brain disease. We also discuss the potential of 14-3-3γ for treatment and the importance of research on specific 14-3-3 isotypes for an effective therapeutic approach.

Abstract

14-3-3 proteins are mostly expressed in the brain and are closely involved in numerous brain functions and various brain disorders. Among the isotypes of the 14-3-3 proteins, 14-3-3γ is mainly expressed in neurons and is highly produced during brain development, which could indicate that it has a significance in neural development. Furthermore, the distinctive levels of temporally and locally regulated 14-3-3γ expression in various brain disorders suggest that it could play a substantial role in brain plasticity of the diseased states. In this review, we introduce the various brain disorders reported to be involved with 14-3-3γ, and summarize the changes of 14-3-3γ expression in each brain disease. We also discuss the potential of 14-3-3γ for treatment and the importance of research on specific 14-3-3 isotypes for an effective therapeutic approach.

참고문헌 (135)

  1. Moore BE, "Physiological and Biochemical aspects of Nervous integration. A symposium", pp.343~359 (1967), Prentice Hall
  2. Ichimura T, "Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+, calmodulindependent protein kinase II", FEBS Letts, 219, pp.79~82 (1987)
  3. Jones DH, "Isoforms of 14-3-3protein can form homo-and heterodimers in vivo and in vitro : implications for function as adapter proteins", FEBS Lett, 368, pp.55~58 (1995)
  4. Jin J, "Proteomic, functional, and domain-based analysis of in vivo 14-3-3binding proteins involved in cytoskeletal regulation and cellular organization", Curr Biol, 14, pp.1436~1450 (2004)
  5. Darling DL, "Role of 14-3-3 Proteins in Eukaryotic Signaling and Development", Curr Top Dev Biol, 68, pp.281~315 (2005)
  6. Wang W, "Molecular evolution of the 14-3-3 protein family", J Mol Evol, 43, pp.384~398 (1996)
  7. Rosenquist M, "Data mining the arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes", Plant Physiol, 127, pp.142~149 (2001)
  8. Su TT, "Cell cycle roles for two 14-3-3proteins during drosophila development", J Cell Sci, 114, pp.3445~3454 (2001)
  9. Aitken A, "14-3-3 alpha and delta are the phosphorylated forms of Raf-activating 14-3-3 beta and zeta", J Biol Chem, 270, pp.5706~5709 (1995)
  10. Dougherty MK, "Unlocking the code of 14-3-3", J Cell Sci, 117, pp.1875~1884 (2004)
  11. van Heusden GP, "14-3-3 proteins : regulators of numerous eukaryotic proteins", IUBMB Life, 57, pp.623~629 (2005)
  12. Bridges D, "14-3-3 proteins : a number of functions for a numbered protein", Sci STKE, 296, pp.re10~ (2004)
  13. Sluchanko NN, "Moonlighting chaperone-like activity of the universal regulatory 14-3-3proteins", FEBS J, 284, pp.1279~1295 (2017)
  14. Fan X, "14-3-3 proteins are on the crossroads of cancer, aging, and age-related neurodegenerative disease", Int J Mol Sci, 20, pp.3518~ (2019)
  15. Muslin AJ, "14-3-3 proteins : regulation of subcellular localization by molecular interference", Cell Signal, 12, pp.703~709 (2000)
  16. Obsil T, "Structural basis of 14-3-3protein functions", Semin Cell Dev Biol, 22, pp.663~672 (2011)
  17. Fu H, "14-3-3proteins : structure, function, and regulation", Annu Rev Pharmacol Toxicol, 40, pp.617~647 (2000)
  18. Yaffe MB, "The Structural basis for 14-3-3 : phosphopeptide Binding Specificity", Cell, 91, pp.961~971 (1997)
  19. Wilker EW, "14-3-3 proteins : a family of versatile molecular regulators", J Biol Chem, 280, pp.18891~18898 (2005)
  20. Chaudhri M, "Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo", Biochem Biophys Res Commun, 300, pp.679~685 (2003)
  21. Gardino AK, "Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes : a comparison of the X-ray crystal structures of all human 14-3-3 isoforms", Semin Cancer Biol, 16, pp.173~182 (2006)
  22. Yang X, "Structural basis for protein-protein interactions in the 14-3-3 protein family", Proc Natl Acad Sci U S A, 103, pp.17237~17242 (2006)
  23. Tzivion G, "A Dimeric 14-3-3protein is an essential cofactor for Raf Kinase Activity", Nature, 394, pp.88~92 (1998)
  24. Zhou Y, "Monomeric 14-3-3 protein is sufficient to modulate the activity of the drosophila slowpoke calcium-dependent potassium channel", J Biol Chem, 278, pp.10073~10080 (2003)
  25. Xiao B, "Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways", Nature, 376, pp.188~191 (1995)
  26. Liu D, "Crystal structure of the zeta isoform of the 14-3-3 protein", Nature, 376, pp.191~194 (1995)
  27. Rittinger K, "Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding", Mol Cell, 4, pp.153~166 (1999)
  28. Coblitz B, "C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors", J Biol Chem, 280, pp.36263~36272 (2005)
  29. Coblitz B, "C-terminal binding : an expanded repertoire and function of 14-3-3proteins", FEBS Lett, 580, pp.1531~1535 (2006)
  30. Petosa C, "14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove", J Biol Chem, 273, pp.16305~16310 (1998)
  31. Masters SC, "Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa", Biochemistry, 38, pp.5216~5221 (1999)
  32. Zhai J, "Identification of a novel interaction of 14-3-3 with p190RhoGEF", J Biol Chem, 276, pp.41318~41324 (2001)
  33. Wang B, "Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display", Biochemistry, 38, pp.12499~12504 (1999)
  34. Aitken A, "Specificity of 14-3-3 isoform dimer interactions and phosphorylation", Biochem Soc Trans, 30, pp.351~360 (2002)
  35. Aitken A, "Post-translational modification of 14-3-3isoforms and regulation of cellular function", Semin Cell Dev Biol, 22, pp.673~680 (2011)
  36. Truong AB, "Role of the 14-3-3 C-terminal loop in ligand interaction", Proteins, 49, pp.321~325 (2002)
  37. Silhan J, "14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding", J Biol Chem, 279, pp.49113~49119 (2004)
  38. Pennington KL, "The Dynamic and stress-adaptive signaling hub of 14-3-3 : Emerging mechanisms of regulation and contextdependent protein-protein interactions", Oncogene, 37, pp.5587~5604 (2018)
  39. Boston PF, "Human 14-3-3 protein : radioimmunoassay, tissue distribution, and cerebrospinal fluid levels in patients with neurological disorders", J Neurochem, 38, pp.1466~1474 (1982)
  40. Aghazadeh V, "The role of the 14-3-3 protein family in health, disease, and drug development", Drug Discov Today, 21, pp.278~287 (2016)
  41. Leffers H, "Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway", J Mol Biol, 231, pp.982~998 (1993)
  42. Watanabe M, "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3 protein and developmental changes in expression of their mRNAs in the nervous system", Brain Res Mol Brain Res, 17, pp.135~146 (1993)
  43. Xiong XX, "Selective 14-3-3 upregulation promotes Beclin-1-LC3-Autophagic Influx via β-catenin interaction in starved neurons in vitro and in vivo", Neurochem Res, 44, pp.849~858 (2019)
  44. Gerber KJ, "14-3-3 binds regulator of G protein signaling 14(RGS14)at distinct sites to inhibit the RGS14 : Gαi-AlF4− signaling complex and RGS14 nuclear localization", J Biol Chem, 293, pp.14616~14631 (2018)
  45. Civiero L, "PAK6Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2", Front Mol Neurosci, 10, pp.417~ (2017)
  46. Lee YS, "Suppression of 14-3-3γ-mediated surface expression of ANO1 inhibits cancer progression of glioblastoma cells", Sci Rep, 6, pp.26413~ (2016)
  47. Oh SJ, "Direct interaction with 14-3-3γ promotes surface expression of Best1 channel in astrocyte", Mol Brain, 10, pp.51~ (2016)
  48. Cho CH, "Depletion of 14-3-3γ reduces the surface expression of Transient Receptor Potential Melastatin 4b (TRPM4b) channels and attenuates TRPM4b-mediated glutamate-induced neuronal cell death", Mol Brain, 7, pp.52~ (2014)
  49. Cornell B, "14-3-3 proteins in brain development : neurogenesis, neuronal migration and neuromorphogenesis", Front Mol Neurosci, 10, pp.318~ (2017)
  50. Wachi T, "Ablation of the 14-3-3gamma protein results in neuronal migration delay and morphological defects in the developing cerebral cortex", Dev Neurobiol, 76, pp.600~614 (2016)
  51. JC Yoo, "14-3-3γ regulates Copine1-mediated neuronal differentiation in HiB5hippocampal progenitor cells", Exp Cell Res, 356, pp.85~92 (2017)
  52. Cornell B, "Overexpression of the 14-3-3γ protein in embryonic mice results in neuronal migration delay in the developing cerebral cortex", Neurosci Lett, 628, pp.40~46 (2016)
  53. Hillier L, "The DNA sequence of chromosome 7", Nature, 424, pp.157~164 (2003)
  54. Ramocki MB, "Recurrent distal 7q11. 23 deletion including HIP1 and YWHAG identified in patients with intellectual disabilities, epilepsy, and neurobehavioral problems", Am J Hum Genet, 87, pp.857~865 (2010)
  55. Fusco C, "Smaller and larger deletions of the Williams Beuren syndrome region implicate genes involved in mild facial phenotype, epilepsy and autistic traits", Eur J Hum Genet, 22, pp.64~70 (2014)
  56. Nicita F, "Epilepsy is a possible feature in Williams-Beuren syndrome patients harboring typical deletions of the 7q11. 23 critical region", Am J Med Genet A, 170A, pp.148~155 (2016)
  57. Morris CM, "Osborne 7q11. 23 duplication syndrome : physical characteristics and natural history", Am J Med Genet A, 167A, pp.2916~2935 (2015)
  58. Schindler CK, "Isoform-and subcellular fraction-specific differences in hippocampal 14-3-3 levels following experimentally evoked seizures and in human temporal lobe epilepsy", J Neurochem, 99, pp.561~569 (2016)
  59. Smani D, "Downregulation of 14-3-3 proteins in a kainic acid-induced neurotoxicity model", Mol Neurobiol, 55, pp.122~129 (2018)
  60. Guella I, "De Novo mutations in YWHAG cause early-onset epilepsy", Am J Hum Genet, 101, pp.300~310 (2017)
  61. Bull MJ, "Down syndrome", N Engl J Med, 382, pp.2344~2352 (2020)
  62. Fountoulakis M, "Increased levels of 14-3-3γ and ε proteins in brain of patients with Alzheimer’s disease and Down syndrome", J Neural Transm Suppl, 57, pp.323~335 (1999)
  63. Peyril A, "Aberrant expression of signalingrelated proteins 14-3-3γ and RACK1 in fetal Down syndrome brain(trisomy 21)", Electrophoresis, 23, pp.152~157 (2002)
  64. Hughes AJ, "What features improve the accuracy of clinical diagnosis in Parkinson’s disease : a clinicopathologic study", Neurology, 42, pp.1142~1146 (1992)
  65. Chen H, "Research on the premotor symptoms of Parkinson’s disease : clinical and etiological implications. Environ", Health Perspect, 121, pp.11~12 (2013)
  66. Sveinbjornsdottir S, "The clinical symptoms of Parkinson’s disease", J Neurochemistry, 139, pp.318~324 (2016)
  67. Jellinger KA, "Formation and development of Lewy pathology : a critical update", J Neurology, 256, pp.270~279 (2009)
  68. Goedert M, "100 years of Lewy pathology", Nat Rev Neurol, 9, pp.13~24 (2013)
  69. Wong YC, "α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies", Nat Med, 23, pp.1~13 (2017)
  70. Ostrerova N, "alpha-Synuclein shares physical and functional homology with 14-3-3 proteins", J Neurosci, 19, pp.5782~5791 (1999)
  71. Kawamoto Y, "14-3-3 proteins in Lewy bodies in Parkinson disease and diffuse Lewy body disease brains", J Neuropathol Exp Neurol, 61, pp.245~253 (2002)
  72. Berg D, "Specification of 14-3–3 proteins in Lewy bodies", Ann Neurol, 53, pp.135~ (2003)
  73. Yacoubian TA, "Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson’s disease", Death Dis, 1, pp.e2~ (2010)
  74. Ding H, "14-3-3 inhibition promotes dopaminergic neuron loss and 14-3-3θ overexpression promotes recovery in the MPTP mouse model of Parkinson’s disease", Neuroscience, 307, pp.73~82 (2015)
  75. Xu Z, "14-3-3 protein targets misfolded chaperone-associated proteins to aggresomes", J Cell Sci, 126, pp.4173~4186 (2013)
  76. Jia B, "14-3-3 and aggresome formation : implications in neurodegenerative diseases", Prion, 8, pp.173~177 (2014)
  77. Plotegher N, "The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity", Hum Mol Genet, 23, pp.5615~5629 (2014)
  78. Sato S, "14-3-3eta is a novel regulator of parkin ubiquitin ligase", EMBO J, 25, pp.211~221 (2006)
  79. Wang J, "14-3-3zeta contributes to tyrosine hydroxylase activity in MN9D cells : localization of dopamine regulatory proteins to mitochondria", J Biol Chem, 284, pp.14011~14019 (2009)
  80. Scheltens P, "Alzheimer’s disease", Lancet, 388, pp.505~517 (2016)
  81. Selkoe DJ, "The amyloid hypothesis of Alzheimer’s disease at 25 years", EMBO Mol Med, 8, pp.595~608 (2016)
  82. Iqbal K, "Tau in Alzheimer disease and related tauopathies", Curr Alzheimer Res, 7, pp.656~664 (2010)
  83. Layfield R, "Neurofibrillary tangles of Alzheimer’s disease brains contain 14-3-3 proteins", Neurosci Lett, 209, pp.57~60 (1996)
  84. Fountoulakis M, "Increased levels of 14-3-3γ and ε proteins in brain of patients with Alzheimer’s disease and Down syndrome", J Neural Transm Suppl, 57, pp.323~335 (1999)
  85. Gu O, "Downregulation of 14-3-3 proteins in Alzheimer’s Disease", Mol Neurobiol, 57, pp.32~40 (2020)
  86. "Creutzfeldt–Jakob Disease Fact Sheet" (2003)[URL]
  87. Spero M, "Creutzfeldt-Jakob disease : case report and review of the literature", Acta Clin Croat, 49, pp.181~187 (2010)
  88. Hsich G, "The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies", N Engl J Med, 335, pp.24~30 (1996)
  89. Zerr I, "Detection of 14-3-3 protein in the cerebrospinal fluid supports the diagnosis of Creutzfeldt–Jakob disease", Ann Neurol, 43, pp.32~40 (1998)
  90. Lemstra AW, "14-3-3 testing in diagnosing Creutzfeldt–Jakob disease : a prospective study in 112 patients", Neurology, 55, pp.514~516 (2000)
  91. Burkhard PR, "CSF detection of the 14-3-3 protein in unselected patients with dementia", Neurology, 56, pp.1528~1533 (2001)
  92. Wiltfang J, "Isoform pattern of 14-3-3 proteins in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease", J Neurochem, 73, pp.2485~2490 (1999)
  93. Shiga Y, "14-3-3 protein levels and isoform patterns in the cerebrospinal fluid of Creutzfeldt-Jakob disease patients in the progressive and terminal stages", J Clin Neurosci, 13, pp.661~665 (2006)
  94. Matsui Y, "High sensitivity of an ELISA kit for detection of the gammaisoform of 14-3-3 proteins : usefulness in laboratory diagnosis of human prion disease", BMC Neurol, 11, pp.120~ (2011)
  95. Leitão MJ, "Sporadic Creutzfeldt-Jakob disease diagnostic accuracy is improved by a new CSF ELISA 14-3-3γ assay", Neuroscience, 322, pp.398~407 (2016)
  96. Kilani RT, "Detection of high levels of 2 specific isoforms of 14-3-3proteins in synovial fluid from patients with joint inflammation", J Rheumatol, 34, pp.1650~1657 (2007)
  97. Sardari K, "Increased levels of the 14-3-3η and γ proteins in the synovial fluid of dogs with unilateral cranial cruciate ligament rupture", Can J Vet Res, 75, pp.271~277 (2011)
  98. Lee D, "Role of glial 14-3-3 gamma protein in autoimmune demyelination", J Neuroinflammation, 6, pp.187~ (2015)
  99. Dendrou CA, "Immunopathology of multiple sclerosis", Nat Rev Immunol, 15, pp.545~558 (2015)
  100. Nakahara J, "Current concepts in multiple sclerosis : autoimmunity versus oligodendrogliopathy", Clin Rev Allergy Immunol, 42, pp.26~34 (2012)
  101. Constantinescu CS, "Experimental autoimmune encephalomyelitis(EAE)as a model for multiple sclerosis(MS)", Br J Pharmacol, 164, pp.1079~1106 (2011)
  102. Pirim I, "Ischemic rat brains contain immunoreactivity of 14-3-3 proteins", Int J Neurosci, 95, pp.101~106 (1998)
  103. Kawamoto Y, "Upregulated expression of 14-3-3 proteins in astrocytes from human cerebrovascular ischemic lesions", Stroke, 37, pp.830~835 (2006)
  104. Fujii K, "Detection of 14-3-3 protein in the cerebrospinal fluid in mitochondrial encephalopathy with lactic acidosis and stroke-like episodes", J Neurol Sci, 239, pp.115~118 (2005)
  105. Lai XJ, "Selective 14-3-3γ induction quenches p-β-catenin Ser37", Bax-enhanced cell death in cerebral cortical neurons during ischemia, 2014, pp.5, e1184~
  106. Jang SW, "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons", J Biol Chem, 284, pp.24512~24525 (2009)
  107. Zhou XY, "14-3-3 Isoforms differentially regulate NFκB signaling in the brain after ischemia-reperfusion", Neurochem Res, 42, pp.2354~2362 (2017)
  108. Otsuka S, "Preconditioning exercise reduces brain damage and neuronal apoptosis through enhanced endogenous 14-3-3γ after focal brain ischemia in rats", Brain Struct Funct, 224, pp.739~740 (2019)
  109. Dong Y, "Ischemia activates JNK", c-Jun, J Neurochem, pp.2009, 109[DOI]
  110. Chen XQ, "The association of 14-3-3gamma and actin plays a role in cell division and apoptosis in astrocytes", Biochem Biophys Res Commun, 296, pp.657~663 (2002)
  111. Chen XQ, "14-3-3gamma is upregulated by in vitro ischemia and binds to protein kinase Raf in primary cultures of astrocytes", Glia, 42, pp.315~324 (2003)
  112. Umahara T, "Intranuclear localization and isoform-dependent translocation of 14-3-3 proteins in human brain with infarction", J Neurol Sci, 260, pp.159~166 (2007)
  113. Chen XQ, "Association of 14-3-3gamma and phosphorylated bad attenuates injury in ischemic astrocytes", J Cereb Blood Flow Metab, 25, pp.338~347 (2005)
  114. Dong Y, "Ischemia activates JNK", c-Jun, J Neurochem, pp.2009, 109[DOI]
  115. Pang Y, "Ischemia preconditioning protects astrocytes from ischemic injury through 14-3-3γ", J Neurosci Res, 93, pp.1507~1518 (2015)
  116. Hermeking H, "14-3-3 proteins in cell cycle regulation", Semin Cancer Biol, 16, pp.183~192 (2006)
  117. Morrison DK, "The 14-3-3 proteins : integrators of diverse signaling cues that impact cell fate and cancer development", Trends Cell Biol, 19, pp.16~23 (2009)
  118. Gardino AK, "14-3-3 proteins as signaling integration points for cell cycle control and apoptosis", Semin Cell Dev Biol, 22, pp.688~695 (2011)
  119. Jin Y, "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation", EMBO J, 25, pp.1207~1218 (2006)
  120. Lee JH, "14-3-3gamma inhibition of MDMX-mediated p21 turnover independent of p53", J Biol Chem, 286, pp.5136~5142 (2011)
  121. Cao WD, "Immunocytochemical detection of 14-3-3 in primary nervous system tumors", J Neurooncol, 77, pp.125~130 (2006)
  122. Cao L, "Identification of 14-3-3 protein isoforms in human astrocytoma by immunohistochemistry", Neurosci Lett, 432, pp.94~99 (2008)
  123. Yang X, "Isoform-specific expression of 14-3-3 proteins in human astrocytoma", J Neurol Sci, 276, pp.54~59 (2009)
  124. Liang S, "Quantitative protein expression profiling of 14-3-3 isoforms in human renal carcinoma shows 14-3-3 epsilon is involved in limitedly increasing renal cell proliferation", Electrophoresis, 30, pp.4152~4162 (2009)
  125. Com E, "Quantitative proteomic Isotope-Coded Protein Label(ICPL)analysis reveals alteration of several functional processes in the glioblastoma", J Proteomics, 75, pp.3898~3913 (2012)
  126. Cao W, "Targeting 14-3-3protein, difopein induces apoptosis of human glioma cells and suppresses tumor growth in mice", Apoptosis, 15, pp.230~241 (2010)
  127. Liu J, "Transmembrane protein with unknown function 16A overexpression promotes glioma formation through the nuclear factor-kappaB signaling pathway", Mol Med Rep, 9, pp.1068~1074 (2014)
  128. Yao ZQ, "A novel small-molecule activator of Sirtuin-1 induces autophagic cell death", mitophagy as a potential therapeutic strategy in glioblastoma, 2018, pp.9, 767~
  129. Steinacker P, "Unchanged Survival Rates of 14-3-3 Knockout Mice after Inoculation with Pathological Prion Protein", Mol Cell Biol, 25, pp.1339~1346 (2005)
  130. 김도언, "14-3-3γ Haploinsufficient Mice Display Hyperactive and Stress-sensitive Behaviors", Experimental Neurobiology, 28(1), pp.43~53 (2019), 한국뇌신경과학회
  131. Cheah PS, "Neurodevelopmental and neuropsychiatric behavior defects arise from 14-3-3zeta deficiency", Mol Psychiatry, 17, pp.451~466 (2012)
  132. Xu X, "14-3-3zeta deficient mice in the BALB", c background display behavioral and anatomical defects associated with neurodevelopmental disorders, 2015, pp.5, 12434~
  133. Jaehne EJ, "In-vivo administration of clozapine affects behaviour but does not reverse dendritic spine deficits in the 14-3-3 KO mouse model of schizophrenia-like disorders", Pharmacol Biochem Behav, 138, pp.1~8 (2015)
  134. Ikeda M, "Identification of YWHAE, a gene encoding 14-3-3epsilon, as a possible susceptibility gene for schizophrenia", Hum Mol Genet, 17, pp.3212~3222 (2008)
  135. Wachi T, "Complete ablation of the 14-3-3epsilon protein results in multiple defects in neuropsychiatric behaviors", Behav Brain Res, 319, pp.31~36 (2017)

관련 논문AI추천

이 간행물의 다른 논문 (7건)