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Volumn 12, Issue 1, 2015, Pages 29-41

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

Author keywords

Calpains; cAMP PKA CREB cascade; ERK1 2 MAP kinase pathway; HAT; HDAC; NO cascade

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; BUNGAROTOXIN RECEPTOR; CALPAIN; CYCLIC AMP; CYCLIC AMP BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; METABOTROPIC RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 7; N METHYL DEXTRO ASPARTIC ACID; NEUROTROPHIN RECEPTOR P75; NITRIC OXIDE; PROTEIN SERINE THREONINE KINASE; STRESS ACTIVATED PROTEIN KINASE; UBIQUITINATED PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN;

EID: 84926612728     PISSN: 19337213     EISSN: 18787479     Source Type: Journal    
DOI: 10.1007/s13311-014-0327-5     Document Type: Review
Times cited : (124)

References (199)
  • 1
    • 0028898888 scopus 로고
    • Mechanisms of synaptic dysfunction in Alzheimer's disease
    • COI: 1:STN:280:DyaK2Mzit1Omtw%3D%3D, PID: 7599445
    • Masliah E. Mechanisms of synaptic dysfunction in Alzheimer's disease. Histol Histopathol 1995;10:509-519.
    • (1995) Histol Histopathol , vol.10 , pp. 509-519
    • Masliah, E.1
  • 2
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • COI: 1:CAS:528:DC%2BD38XotFSnur0%3D, PID: 12399581
    • Selkoe DJ. Alzheimer's disease is a synaptic failure. Science 2002;298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 3
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid beta-peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling
    • Vitolo OV, Sant'Angelo A, Costanzo V et al. Amyloid beta-peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling. Proc Natl Acad Sci U S A 2002;99:13217-13221.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13217-13221
    • Vitolo, O.V.1    Sant'Angelo, A.2    Costanzo, V.3
  • 4
    • 84860806555 scopus 로고    scopus 로고
    • The molecular biology of memory: cAMP, PKA, CRE, CREB-1, CREB-2, and CPEB
    • COI: 1:CAS:528:DC%2BC3sXhsFyisLw%3D, PID: 22583753
    • Kandel ER. The molecular biology of memory: cAMP, PKA, CRE, CREB-1, CREB-2, and CPEB. Mol Brain 2012;5:14.
    • (2012) Mol Brain , vol.5 , pp. 14
    • Kandel, E.R.1
  • 6
    • 0037040402 scopus 로고    scopus 로고
    • Expression of constitutively active CREB protein facilitates the late phase of long-term potentiation by enhancing synaptic capture
    • COI: 1:CAS:528:DC%2BD38XisFOhtLs%3D, PID: 11893339
    • Barco A, Alarcon JM, Kandel ER. Expression of constitutively active CREB protein facilitates the late phase of long-term potentiation by enhancing synaptic capture. Cell 2002;108:689-703.
    • (2002) Cell , vol.108 , pp. 689-703
    • Barco, A.1    Alarcon, J.M.2    Kandel, E.R.3
  • 7
    • 77952889956 scopus 로고    scopus 로고
    • CREB's control of intrinsic and synaptic plasticity: implications for CREB-dependent memory models
    • COI: 1:CAS:528:DC%2BC3cXmtFCisr8%3D, PID: 20223527
    • Benito E, Barco A. CREB's control of intrinsic and synaptic plasticity: implications for CREB-dependent memory models. Trends Neurosci 2010;33:230-240.
    • (2010) Trends Neurosci , vol.33 , pp. 230-240
    • Benito, E.1    Barco, A.2
  • 8
    • 4644261125 scopus 로고    scopus 로고
    • Regulation of histone acetylation during memory formation in the hippocampus
    • Levenson JM, O' Riordan KJ, Brown KD, Trinh MA, Molfese DL, Sweatt JD. Regulation of histone acetylation during memory formation in the hippocampus. J Biol Chem 2004;279:40545-40559.
    • (2004) J Biol Chem , vol.279 , pp. 40545-40559
  • 9
    • 2942705826 scopus 로고    scopus 로고
    • Chromatin acetylation, memory, and LTP are impaired in CBP+/- mice: a model for the cognitive deficit in Rubinstein–Taybi syndrome and its amelioration
    • Alarcón JM, Malleret G, Touzani K, et al. Chromatin acetylation, memory, and LTP are impaired in CBP+/- mice: a model for the cognitive deficit in Rubinstein–Taybi syndrome and its amelioration. Neuron 2004;42:947-959.
    • (2004) Neuron , vol.42 , pp. 947-959
    • Alarcón, J.M.1    Malleret, G.2    Touzani, K.3
  • 10
    • 84984929135 scopus 로고    scopus 로고
    • The role of histone acetylation in memory formation and cognitive impairments
    • COI: 1:CAS:528:DC%2BC38Xhs1ynurrE, PID: 22669172
    • Peixoto L, Abel T. The role of histone acetylation in memory formation and cognitive impairments. Neuropsychopharmacology 2013;38:62-76.
    • (2013) Neuropsychopharmacology , vol.38 , pp. 62-76
    • Peixoto, L.1    Abel, T.2
  • 11
    • 2942731425 scopus 로고    scopus 로고
    • CBP histone acetyltransferase activity is a critical component of memory consolidation
    • COI: 1:CAS:528:DC%2BD2cXlsleisr4%3D, PID: 15207240
    • Korzus E, Rosenfeld MG, Mayford M. CBP histone acetyltransferase activity is a critical component of memory consolidation. Neuron 2004;42:961-972.
    • (2004) Neuron , vol.42 , pp. 961-972
    • Korzus, E.1    Rosenfeld, M.G.2    Mayford, M.3
  • 12
    • 77952168294 scopus 로고    scopus 로고
    • Altered histone acetylation is associated with age-dependent memory impairment in mice
    • Peleg S, Sananbenesi F, Zovoilis A, et al. Altered histone acetylation is associated with age-dependent memory impairment in mice. Science 2010;328:753-756.
    • (2010) Science , vol.328 , pp. 753-756
  • 13
    • 0035744704 scopus 로고    scopus 로고
    • The molecular biology of memory storage: a dialog between genes and synapses
    • COI: 1:CAS:528:DC%2BD38Xms1yqtrk%3D, PID: 12168768
    • Kandel ER. The molecular biology of memory storage: a dialog between genes and synapses. Biosci Rep 2001;21:565-611.
    • (2001) Biosci Rep , vol.21 , pp. 565-611
    • Kandel, E.R.1
  • 14
    • 0014688623 scopus 로고
    • A cyclic AMP–stimulated protein kinase in adipose tissue
    • COI: 1:CAS:528:DyaF1MXkslOmsLg%3D, PID: 4308081
    • Corbin JD, Krebs EG. A cyclic AMP–stimulated protein kinase in adipose tissue. Biochem Biophys Res Commun 1969;36: 328-336.
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 328-336
    • Corbin, J.D.1    Krebs, E.G.2
  • 15
    • 84914153002 scopus 로고
    • Cyclophilin D deficiency rescues Abeta-impaired PKA/CREB signaling and alleviates synaptic degeneration
    • Du H, Guo L, Wu X, et al. Cyclophilin D deficiency rescues Abeta-impaired PKA/CREB signaling and alleviates synaptic degeneration. Biochim Biophys Acta 2014;1842:2517-2527.
    • (1842) Biochim Biophys Acta , vol.2014 , pp. 2517-2527
    • Du, H.1    Guo, L.2    Wu, X.3
  • 16
    • 84864987239 scopus 로고    scopus 로고
    • Alzheimer's beta-secretase (BACE1) regulates the cAMP/PKA/CREB pathway independently of beta-amyloid
    • Chen Y, Huang X, Zhang YW et al. Alzheimer's beta-secretase (BACE1) regulates the cAMP/PKA/CREB pathway independently of beta-amyloid. J Neurosci 2012;32:11390-11395.
    • (2012) J Neurosci , vol.32 , pp. 11390-11395
    • Chen, Y.1    Huang, X.2    Zhang, Y.W.3
  • 17
    • 80053221873 scopus 로고    scopus 로고
    • Caffeine induces beneficial changes in PKA signaling and JNK and ERK activities in the striatum and cortex of Alzheimer's transgenic mice
    • Zeitlin R, Patel S, Burgess S, Arendash GW, Echeverria V. Caffeine induces beneficial changes in PKA signaling and JNK and ERK activities in the striatum and cortex of Alzheimer's transgenic mice. Brain Res 2011;1417:127-136.
    • (2011) Brain Res , vol.1417 , pp. 127-136
    • Zeitlin, R.1    Patel, S.2    Burgess, S.3    Arendash, G.W.4    Echeverria, V.5
  • 18
    • 84875717632 scopus 로고    scopus 로고
    • Environmental novelty activates beta2-adrenergic signaling to prevent the impairment of hippocampal LTP by Abeta oligomers
    • Li S, Jin M, Zhang D et al. Environmental novelty activates beta2-adrenergic signaling to prevent the impairment of hippocampal LTP by Abeta oligomers. Neuron 2013;77:929-941.
    • (2013) Neuron , vol.77 , pp. 929-941
    • Li, S.1    Jin, M.2    Zhang, D.3
  • 19
    • 58149385218 scopus 로고    scopus 로고
    • Picomolar amyloid-beta positively modulates synaptic plasticity and memory in hippocampus
    • Puzzo D, Privitera L, Leznik E et al. Picomolar amyloid-beta positively modulates synaptic plasticity and memory in hippocampus. J Neurosci 2008;28:14537-14545.
    • (2008) J Neurosci , vol.28 , pp. 14537-14545
    • Puzzo, D.1    Privitera, L.2    Leznik, E.3
  • 20
    • 79955474315 scopus 로고    scopus 로고
    • Endogenous amyloid-beta is necessary for hippocampal synaptic plasticity and memory
    • Puzzo D, Privitera L, Fa M et al. Endogenous amyloid-beta is necessary for hippocampal synaptic plasticity and memory. Ann Neurol 2011;69:819-830.
    • (2011) Ann Neurol , vol.69 , pp. 819-830
    • Puzzo, D.1    Privitera, L.2    Fa, M.3
  • 21
    • 84899935373 scopus 로고    scopus 로고
    • A novel mechanism for cyclic adenosine monophosphate-mediated memory formation: Role of amyloid beta
    • Ricciarelli R, Puzzo D, Bruno O et al. A novel mechanism for cyclic adenosine monophosphate-mediated memory formation: Role of amyloid beta. Ann Neurol 2014;75:602-607.
    • (2014) Ann Neurol , vol.75 , pp. 602-607
    • Ricciarelli, R.1    Puzzo, D.2    Bruno, O.3
  • 22
    • 84897425079 scopus 로고    scopus 로고
    • Clinical and molecular genetics of the phosphodiesterases (PDEs)
    • Azevedo MF, Faucz FR, Bimpaki E et al. Clinical and molecular genetics of the phosphodiesterases (PDEs). Endocr Rev 2014;35:195-233.
    • (2014) Endocr Rev , vol.35 , pp. 195-233
    • Azevedo, M.F.1    Faucz, F.R.2    Bimpaki, E.3
  • 23
    • 0037458648 scopus 로고    scopus 로고
    • Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling
    • Conti M, Richter W, Mehats C et al. Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling. J Biol Chem 2003;278:5493-5496.
    • (2003) J Biol Chem , vol.278 , pp. 5493-5496
    • Conti, M.1    Richter, W.2    Mehats, C.3
  • 24
    • 0037443097 scopus 로고    scopus 로고
    • PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization
    • COI: 1:CAS:528:DC%2BD3sXhtVKktbc%3D, PID: 12444918
    • Houslay MD, Adams DR. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem J 2003;370:1-18.
    • (2003) Biochem J , vol.370 , pp. 1-18
    • Houslay, M.D.1    Adams, D.R.2
  • 25
    • 3342953638 scopus 로고    scopus 로고
    • Implications of PDE4 structure on inhibitor selectivity across PDE families
    • COI: 1:CAS:528:DC%2BD2cXlt1Sjsbo%3D, PID: 15224132
    • Ke H. Implications of PDE4 structure on inhibitor selectivity across PDE families. Int J Impot Res 2004;16(Suppl. 1):S24-S27.
    • (2004) Int J Impot Res , vol.16 , pp. 24-27
    • Ke, H.1
  • 26
    • 2542584749 scopus 로고    scopus 로고
    • Progressive age-related development of Alzheimer-like pathology in APP/PS1 mice
    • Trinchese F, Liu S, Battaglia F et al. Progressive age-related development of Alzheimer-like pathology in APP/PS1 mice. Ann Neurol 2004;55:801-814.
    • (2004) Ann Neurol , vol.55 , pp. 801-814
    • Trinchese, F.1    Liu, S.2    Battaglia, F.3
  • 27
    • 85047694516 scopus 로고    scopus 로고
    • Persistent improvement in synaptic and cognitive functions in an Alzheimer mouse model after rolipram treatment
    • Gong B, Vitolo OV, Trinchese F et al. Persistent improvement in synaptic and cognitive functions in an Alzheimer mouse model after rolipram treatment. J Clin Invest 2004;114:1624-1634.
    • (2004) J Clin Invest , vol.114 , pp. 1624-1634
    • Gong, B.1    Vitolo, O.V.2    Trinchese, F.3
  • 28
    • 77957354074 scopus 로고    scopus 로고
    • Inhibition of phosphodiesterase-4 reverses memory deficits produced by Abeta25-35 or Abeta1-40 peptide in rats
    • Cheng YF, Wang C, Lin HB et al. Inhibition of phosphodiesterase-4 reverses memory deficits produced by Abeta25-35 or Abeta1-40 peptide in rats. Psychopharmacology (Berl) 2010;212:181-191.
    • (2010) Psychopharmacology (Berl) , vol.212 , pp. 181-191
    • Cheng, Y.F.1    Wang, C.2    Lin, H.B.3
  • 29
    • 84889565661 scopus 로고    scopus 로고
    • RNA interference-mediated knockdown of long-form phosphodiesterase-4D (PDE4D) enzyme reverses amyloid-beta42-induced memory deficits in mice
    • Zhang C, Cheng Y, Wang H et al. RNA interference-mediated knockdown of long-form phosphodiesterase-4D (PDE4D) enzyme reverses amyloid-beta42-induced memory deficits in mice. J Alzheimers Dis 2014;38:269-280.
    • (2014) J Alzheimers Dis , vol.38 , pp. 269-280
    • Zhang, C.1    Cheng, Y.2    Wang, H.3
  • 30
    • 0024319477 scopus 로고
    • Rolipram in major depressive disorder: results of a double-blind comparative study with imipramine
    • Hebenstreit GF, Fellerer K, Fichte K et al. Rolipram in major depressive disorder: results of a double-blind comparative study with imipramine. Pharmacopsychiatry 1989;22:156-160.
    • (1989) Pharmacopsychiatry , vol.22 , pp. 156-160
    • Hebenstreit, G.F.1    Fellerer, K.2    Fichte, K.3
  • 31
    • 81455151817 scopus 로고    scopus 로고
    • GEBR-7b, a novel PDE4D selective inhibitor that improves memory in rodents at non-emetic doses
    • Bruno O, Fedele E, Prickaerts J et al. GEBR-7b, a novel PDE4D selective inhibitor that improves memory in rodents at non-emetic doses. Br J Pharmacol 2011;164:2054-2063.
    • (2011) Br J Pharmacol , vol.164 , pp. 2054-2063
    • Bruno, O.1    Fedele, E.2    Prickaerts, J.3
  • 32
    • 84886247782 scopus 로고    scopus 로고
    • Improvement of spatial memory function in APPswe/PS1dE9 mice after chronic inhibition of phosphodiesterase type 4D
    • Sierksma AS, van den Hove DL, Pfau F et al. Improvement of spatial memory function in APPswe/PS1dE9 mice after chronic inhibition of phosphodiesterase type 4D. Neuropharmacology 2014;77:120-130.
    • (2014) Neuropharmacology , vol.77 , pp. 120-130
    • Sierksma, A.S.1    van den Hove, D.L.2    Pfau, F.3
  • 33
    • 9744222883 scopus 로고    scopus 로고
    • Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
    • de Vrij FM, Fischer DF, van Leeuwen FW, Hol EM. Protein quality control in Alzheimer's disease by the ubiquitin proteasome system. Prog Neurobiol 2004;74:249-270.
    • (2004) Prog Neurobiol , vol.74 , pp. 249-270
    • de Vrij, F.M.1    Fischer, D.F.2    van Leeuwen, F.W.3    Hol, E.M.4
  • 34
    • 34547535639 scopus 로고    scopus 로고
    • The functions of UCH-L1 and its relation to neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BD2sXosFOhur8%3D, PID: 17586089
    • Setsuie R, Wada K. The functions of UCH-L1 and its relation to neurodegenerative diseases. Neurochem Int 2007;51:105-111.
    • (2007) Neurochem Int , vol.51 , pp. 105-111
    • Setsuie, R.1    Wada, K.2
  • 35
    • 0032911634 scopus 로고    scopus 로고
    • Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia
    • Chain DG, Casadio A, Schacher S et al. Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia. Neuron 1999;22:147-156.
    • (1999) Neuron , vol.22 , pp. 147-156
    • Chain, D.G.1    Casadio, A.2    Schacher, S.3
  • 36
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J, Levey AI, Weintraub ST et al. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J Biol Chem 2004;279:13256-13264.
    • (2004) J Biol Chem , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3
  • 37
    • 33747199933 scopus 로고    scopus 로고
    • Ubiquitin hydrolase uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory
    • Gong B, Cao Z, Zheng P et al. Ubiquitin hydrolase uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory. Cell 2006;126:775-788.
    • (2006) Cell , vol.126 , pp. 775-788
    • Gong, B.1    Cao, Z.2    Zheng, P.3
  • 39
    • 36849001303 scopus 로고    scopus 로고
    • The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders
    • COI: 1:CAS:528:DC%2BD2sXhtlGgtb%2FK, PID: 17925890
    • Gong B, Leznik E. The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders. Drug News Perspect 2007;20:365-370.
    • (2007) Drug News Perspect , vol.20 , pp. 365-370
    • Gong, B.1    Leznik, E.2
  • 40
    • 63849154465 scopus 로고    scopus 로고
    • Membrane-associated farnesylated UCH-L1 promotes alpha-synuclein neurotoxicity and is a therapeutic target for Parkinson's disease
    • Liu Z, Meray RK, Grammatopoulos TN et al. Membrane-associated farnesylated UCH-L1 promotes alpha-synuclein neurotoxicity and is a therapeutic target for Parkinson's disease. Proc Natl Acad Sci U S A 2009;106:4635-4640.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4635-4640
    • Liu, Z.1    Meray, R.K.2    Grammatopoulos, T.N.3
  • 41
    • 78650121290 scopus 로고    scopus 로고
    • CREB: a multifaceted regulator of neuronal plasticity and protection
    • COI: 1:CAS:528:DC%2BC3MXis1Whuw%3D%3D, PID: 21044077
    • Sakamoto K, Karelina K, Obrietan K. CREB: a multifaceted regulator of neuronal plasticity and protection. J Neurochem 2011;116:1-9.
    • (2011) J Neurochem , vol.116 , pp. 1-9
    • Sakamoto, K.1    Karelina, K.2    Obrietan, K.3
  • 42
    • 84898937370 scopus 로고    scopus 로고
    • Nuclear and cytosolic JNK signalling in neurons
    • COI: 1:CAS:528:DC%2BC2cXmtlagsLY%3D, PID: 24739785
    • Coffey ET. Nuclear and cytosolic JNK signalling in neurons. Nat Rev Neurosci 2014;15:285-299.
    • (2014) Nat Rev Neurosci , vol.15 , pp. 285-299
    • Coffey, E.T.1
  • 43
    • 84873157436 scopus 로고    scopus 로고
    • Metabolic triad in brain aging: mitochondria, insulin/IGF-1 signalling and JNK signalling
    • COI: 1:CAS:528:DC%2BC3sXhs1eitL8%3D, PID: 23356266
    • Yin F, Jiang T, Cadenas E. Metabolic triad in brain aging: mitochondria, insulin/IGF-1 signalling and JNK signalling. Biochem Soc Trans 2013;41:101-105.
    • (2013) Biochem Soc Trans , vol.41 , pp. 101-105
    • Yin, F.1    Jiang, T.2    Cadenas, E.3
  • 44
    • 73449131129 scopus 로고    scopus 로고
    • Targeting p38 MAPK pathway for the treatment of Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC3cXjtleqtg%3D%3D, PID: 19951717
    • Munoz L, Ammit AJ. Targeting p38 MAPK pathway for the treatment of Alzheimer's disease. Neuropharmacology 2010;58:561-568.
    • (2010) Neuropharmacology , vol.58 , pp. 561-568
    • Munoz, L.1    Ammit, A.J.2
  • 45
    • 73549086743 scopus 로고    scopus 로고
    • The signaling pathway leading to extracellular signal-regulated kinase 5 (ERK5) activation via G-proteins and ERK5-dependent neurotrophic effects
    • COI: 1:CAS:528:DC%2BC3cXovFymtQ%3D%3D, PID: 19858097
    • Obara Y, Nakahata N. The signaling pathway leading to extracellular signal-regulated kinase 5 (ERK5) activation via G-proteins and ERK5-dependent neurotrophic effects. Mol Pharmacol 2010;77:10-16.
    • (2010) Mol Pharmacol , vol.77 , pp. 10-16
    • Obara, Y.1    Nakahata, N.2
  • 46
    • 79952112019 scopus 로고    scopus 로고
    • The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions
    • COI: 1:CAS:528:DC%2BC3cXhtlSnsL7L, PID: 20811974
    • Keshet Y, Seger R. The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions. Methods Mol Biol 2010;661:3-38.
    • (2010) Methods Mol Biol , vol.661 , pp. 3-38
    • Keshet, Y.1    Seger, R.2
  • 47
    • 2342667386 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase 1 mediates cAMP response element-binding protein phosphorylation and activation by neurotrophins
    • Arthur JS, Fong AL, Dwyer JM et al., Mitogen- and stress-activated protein kinase 1 mediates cAMP response element-binding protein phosphorylation and activation by neurotrophins. J Neurosci 2004;24:4324-4332.
    • (2004) J Neurosci , vol.24 , pp. 4324-4332
    • Arthur, J.S.1    Fong, A.L.2    Dwyer, J.M.3
  • 48
    • 84855904096 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor and Alzheimer's disease: physiopathology and beyond
    • COI: 1:CAS:528:DC%2BC3MXhsV2msr3J, PID: 21898045
    • Diniz BS, Teixeira AL. Brain-derived neurotrophic factor and Alzheimer's disease: physiopathology and beyond. Neuromolecular Med 2011;13:217-222.
    • (2011) Neuromolecular Med , vol.13 , pp. 217-222
    • Diniz, B.S.1    Teixeira, A.L.2
  • 50
    • 33747891466 scopus 로고    scopus 로고
    • Stage-dependent BDNF serum concentrations in Alzheimer's disease
    • Laske C, Stransky E, Leyhe T, et al. Stage-dependent BDNF serum concentrations in Alzheimer's disease. J Neural Transm 2006;113:1217-1224.
    • (2006) J Neural Transm , vol.113 , pp. 1217-1224
    • Laske, C.1    Stransky, E.2
  • 51
    • 75649087374 scopus 로고    scopus 로고
    • Decreased serum brain-derived neurotrophic factor levels in elderly korean with dementia
    • Lee JG, Shin BS, You YS, et al. Decreased serum brain-derived neurotrophic factor levels in elderly korean with dementia. Psychiatry Investig 2009;6:299-305.
    • (2009) Psychiatry Investig , vol.6 , pp. 299-305
    • Lee, J.G.1    Shin, B.S.2    You, Y.S.3
  • 52
    • 42949119345 scopus 로고    scopus 로고
    • CSF multianalyte profile distinguishes Alzheimer and Parkinson diseases
    • Zhang J, Sokal I, Peskind ER, et al. CSF multianalyte profile distinguishes Alzheimer and Parkinson diseases. Am J Clin Pathol 2008;129:526-529.
    • (2008) Am J Clin Pathol , vol.129 , pp. 526-529
    • Zhang, J.1    Sokal, I.2    Peskind, E.R.3
  • 53
    • 65549104991 scopus 로고    scopus 로고
    • Cerebrospinal fluid concentration of brain-derived neurotrophic factor and cognitive function in non-demented subjects
    • Li G, Peskind ER, Millard SP et al. Cerebrospinal fluid concentration of brain-derived neurotrophic factor and cognitive function in non-demented subjects. PLoS One 2009;4:e5424.
    • (2009) PLoS One , vol.e5424 , pp. 4
    • Li, G.1    Peskind, E.R.2    Millard, S.P.3
  • 54
    • 3342908640 scopus 로고    scopus 로고
    • Beta-amyloid peptide at sublethal concentrations downregulates brain-derived neurotrophic factor functions in cultured cortical neurons
    • Tong L, Balazs R, Thornton PL, Cotman CW. Beta-amyloid peptide at sublethal concentrations downregulates brain-derived neurotrophic factor functions in cultured cortical neurons. J Neurosci 2004;24:6799-6809.
    • (2004) J Neurosci , vol.24 , pp. 6799-6809
    • Tong, L.1    Balazs, R.2    Thornton, P.L.3    Cotman, C.W.4
  • 55
    • 0034797352 scopus 로고    scopus 로고
    • Differential activation of neuronal ERK, JNK/SAPK and p38 in Alzheimer disease: the 'two hit' hypothesis
    • Zhu X, Castellani RJ, Takeda A et al. Differential activation of neuronal ERK, JNK/SAPK and p38 in Alzheimer disease: the 'two hit' hypothesis. Mech Ageing Dev 2001;123:39-46.
    • (2001) Mech Ageing Dev , vol.123 , pp. 39-46
    • Zhu, X.1    Castellani, R.J.2    Takeda, A.3
  • 56
    • 0033516947 scopus 로고    scopus 로고
    • Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation
    • Perry G, Roder H, Nunomura A et al. Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation. Neuroreport 1999;10:2411-2415.
    • (1999) Neuroreport , vol.10 , pp. 2411-2415
    • Perry, G.1    Roder, H.2    Nunomura, A.3
  • 57
    • 0035094403 scopus 로고    scopus 로고
    • Phosphorylated map kinase (ERK1, ERK2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration
    • Ferrer I, Blanco R, Carmona M et al. Phosphorylated map kinase (ERK1, ERK2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration. Brain Pathol 2001;11:144-158.
    • (2001) Brain Pathol , vol.11 , pp. 144-158
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3
  • 58
    • 0035875962 scopus 로고    scopus 로고
    • Beta-amyloid activates the mitogen-activated protein kinase cascade via hippocampal alpha7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer's disease
    • Dineley KT, Westerman M, Bui D, Bell K, Ashe KH, Sweatt JD. Beta-amyloid activates the mitogen-activated protein kinase cascade via hippocampal alpha7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer's disease. J Neurosci 2001;21:4125-4133.
    • (2001) J Neurosci , vol.21 , pp. 4125-4133
    • Dineley, K.T.1    Westerman, M.2    Bui, D.3    Bell, K.4    Ashe, K.H.5    Sweatt, J.D.6
  • 59
    • 0035166616 scopus 로고    scopus 로고
    • The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory
    • COI: 1:CAS:528:DC%2BD3MXhtVGls7w%3D, PID: 11145972
    • Sweatt JD. The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory. J Neurochem 2001;76:1-10.
    • (2001) J Neurochem , vol.76 , pp. 1-10
    • Sweatt, J.D.1
  • 60
    • 58549105755 scopus 로고    scopus 로고
    • MAP'ing CNS development and cognition: an ERKsome process
    • COI: 1:CAS:528:DC%2BD1MXitVamurg%3D, PID: 19186160
    • Samuels IS, Saitta SC, Landreth GE. MAP'ing CNS development and cognition: an ERKsome process. Neuron 2009;61:160-167.
    • (2009) Neuron , vol.61 , pp. 160-167
    • Samuels, I.S.1    Saitta, S.C.2    Landreth, G.E.3
  • 61
    • 33846245536 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinases by glutamate receptors
    • COI: 1:CAS:528:DC%2BD2sXptlyqsA%3D%3D, PID: 17018022
    • Wang JQ, Fibuch EE, Mao L. Regulation of mitogen-activated protein kinases by glutamate receptors. J Neurochem 2007;100:1-11.
    • (2007) J Neurochem , vol.100 , pp. 1-11
    • Wang, J.Q.1    Fibuch, E.E.2    Mao, L.3
  • 62
    • 33646516019 scopus 로고    scopus 로고
    • Mechanisms of ERK1/2 regulation by seven-transmembrane-domain receptors
    • COI: 1:CAS:528:DC%2BD28XmtFequrs%3D
    • Werry TD, Christopoulos A Sexton PA. Mechanisms of ERK1/2 regulation by seven-transmembrane-domain receptors. Curr Pharm Design 2006;12:1683-1702.
    • (2006) Curr Pharm Design , vol.12 , pp. 1683-1702
    • Werry, T.D.1    Christopoulos, A.2    Sexton, P.A.3
  • 63
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP et al. Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 2007;282:11590-11601.
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3
  • 64
    • 0030817292 scopus 로고    scopus 로고
    • Effects of beta-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor
    • Cowburn RF, Wiehager B, Trief E, Li-Li M, Sundstrom E. Effects of beta-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor. Neurochem Res 1997;22:1437-1442.
    • (1997) Neurochem Res , vol.22 , pp. 1437-1442
    • Cowburn, R.F.1    Wiehager, B.2    Trief, E.3    Li-Li, M.4    Sundstrom, E.5
  • 65
    • 84884200967 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer abeta oligomer bound to cellular prion protein
    • Um JW, Kaufman AC, Kostylev M et al. Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer abeta oligomer bound to cellular prion protein. Neuron 2013;79:887-902.
    • (2013) Neuron , vol.79 , pp. 887-902
    • Um, J.W.1    Kaufman, A.C.2    Kostylev, M.3
  • 66
  • 67
    • 84903202395 scopus 로고    scopus 로고
    • inhibition in microglia prevents ischemia-dependent synaptic dysfunction in an amyloid-enriched environment
    • Origlia N, Criscuolo C, Arancio O, Yan SS, Domenici L. RAGE inhibition in microglia prevents ischemia-dependent synaptic dysfunction in an amyloid-enriched environment. J Neurosci 2014;34:8749-8760.
    • (2014) J Neurosci , vol.34 , pp. 8749-8760
    • Origlia, N.1    Criscuolo, C.2    Arancio, O.3    Yan, S.S.4    Domenici, L.R.A.G.E.5
  • 68
    • 69249209789 scopus 로고    scopus 로고
    • Pharmacology of the intracellular pathways activated by amyloid beta protein
    • COI: 1:CAS:528:DC%2BD1MXnslejsr8%3D, PID: 19519498
    • Balleza-Tapia H, Pena F. Pharmacology of the intracellular pathways activated by amyloid beta protein. Mini Rev Med Chem 2009;9:724-740.
    • (2009) Mini Rev Med Chem , vol.9 , pp. 724-740
    • Balleza-Tapia, H.1    Pena, F.2
  • 69
    • 78649993978 scopus 로고    scopus 로고
    • Phosphorylation of APP-CTF-AICD domains and interaction with adaptor proteins: signal transduction and/or transcriptional role–relevance for Alzheimer pathology
    • Schettini G, Govoni S, Racchi M, Rodriguez G. Phosphorylation of APP-CTF-AICD domains and interaction with adaptor proteins: signal transduction and/or transcriptional role–relevance for Alzheimer pathology. J Neurochem 2010;115:1299-1308.
    • (2010) J Neurochem , vol.115 , pp. 1299-1308
    • Schettini, G.1    Govoni, S.2    Racchi, M.3    Rodriguez, G.4
  • 70
    • 84877633053 scopus 로고    scopus 로고
    • Small molecule p75NTR ligand prevents cognitive deficits and neurite degeneration in an Alzheimer's mouse model
    • Knowles JK, Simmons DA, Nguyen TV et al. Small molecule p75NTR ligand prevents cognitive deficits and neurite degeneration in an Alzheimer's mouse model. Neurobiol Aging 2013;34:2052-2063.
    • (2013) Neurobiol Aging , vol.34 , pp. 2052-2063
    • Knowles, J.K.1    Simmons, D.A.2    Nguyen, T.V.3
  • 71
    • 0028277844 scopus 로고
    • Membrane depolarization and calcium influx stimulate MEK and MAP kinase via activation of Ras
    • Rosen LB, Simmons DA, Nguyen TV et al. Membrane depolarization and calcium influx stimulate MEK and MAP kinase via activation of Ras. Neuron 1994;12:1207-1221.
    • (1994) Neuron , vol.12 , pp. 1207-1221
    • Rosen, L.B.1    Simmons, D.A.2    Nguyen, T.V.3
  • 72
    • 33845718056 scopus 로고    scopus 로고
    • Ca2+ -stimulated adenylyl cyclases regulate ERK-dependent activation of MSK1 during fear conditioning
    • Sindreu CB, Scheiner ZS, Storm DR. Ca2+ -stimulated adenylyl cyclases regulate ERK-dependent activation of MSK1 during fear conditioning. Neuron 2007;53:79-89.
    • (2007) Neuron , vol.53 , pp. 79-89
    • Sindreu, C.B.1    Scheiner, Z.S.2    Storm, D.R.3
  • 74
    • 59449090590 scopus 로고    scopus 로고
    • The CREB/CRE transcriptional pathway: protection against oxidative stress-mediated neuronal cell death
    • Lee B, Cao R, Choi YS et al. The CREB/CRE transcriptional pathway: protection against oxidative stress-mediated neuronal cell death. J Neurochem 2009;108:1251-1265.
    • (2009) J Neurochem , vol.108 , pp. 1251-1265
    • Lee, B.1    Cao, R.2    Choi, Y.S.3
  • 75
    • 0026549985 scopus 로고
    • Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state
    • Drewes G, Lichtenberg-Kraag B, Doring F et al. Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state. EMBO J 1992;11:2131-2138.
    • (1992) EMBO J , vol.11 , pp. 2131-2138
    • Drewes, G.1    Lichtenberg-Kraag, B.2    Doring, F.3
  • 76
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta
    • Reynolds CH, Betts JC, Blackstock WP, Nebreda AR, Anderton BH. Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. J Neurochem 2000;74:1587-1595.
    • (2000) J Neurochem , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3    Nebreda, A.R.4    Anderton, B.H.5
  • 77
    • 0027453202 scopus 로고
    • Functional studies of Alzheimer's disease tau protein
    • COI: 1:CAS:528:DyaK3sXktVKgsb0%3D, PID: 8426226
    • Lu Q, Wood JG. Functional studies of Alzheimer's disease tau protein. J Neurosci 1993;13:508-515.
    • (1993) J Neurosci , vol.13 , pp. 508-515
    • Lu, Q.1    Wood, J.G.2
  • 78
    • 0032972004 scopus 로고    scopus 로고
    • Hyperactivation of mitogen-activated protein kinase increases phospho-tau immunoreactivity within human neuroblastoma: additive and synergistic influence of alteration of additional kinase activities
    • COI: 1:CAS:528:DyaK1MXhs12hsbo%3D, PID: 10081608
    • Ekinci FJ, Shea TB. Hyperactivation of mitogen-activated protein kinase increases phospho-tau immunoreactivity within human neuroblastoma: additive and synergistic influence of alteration of additional kinase activities. Cell Mol Neurobiol 1999;19:249-260.
    • (1999) Cell Mol Neurobiol , vol.19 , pp. 249-260
    • Ekinci, F.J.1    Shea, T.B.2
  • 79
    • 0035253794 scopus 로고    scopus 로고
    • Hyperphosphorylation of tau is mediated by ERK activation during anticancer drug-induced apoptosis in neuroblastoma cells
    • Guise S, Braguer D, Carles G, Delacourte A, Briand C. Hyperphosphorylation of tau is mediated by ERK activation during anticancer drug-induced apoptosis in neuroblastoma cells. J Neurosci Res 2001;63:257-267.
    • (2001) J Neurosci Res , vol.63 , pp. 257-267
    • Guise, S.1    Braguer, D.2    Carles, G.3    Delacourte, A.4    Briand, C.5
  • 80
    • 85062139768 scopus 로고
    • Tau phosphorylation in brain slices: pharmacological evidence for convergent effects of protein phosphatases on tau and mitogen-activated protein kinase
    • Garver TD, Oyler GA, Harris KA et al. Tau phosphorylation in brain slices: pharmacological evidence for convergent effects of protein phosphatases on tau and mitogen-activated protein kinase. Mol Pharmacol 1995;47:745-756.
    • (1995) Mol Pharmacol , vol.47 , pp. 745-756
    • Garver, T.D.1    Oyler, G.A.2    Harris, K.A.3
  • 81
    • 0035934224 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase cascade and phosphorylation of cytoskeletal proteins after neurone-specific activation of p21ras. II. Cytoskeletal proteins and dendritic morphology
    • Holzer M, Rodel L, Seeger G et al. Activation of mitogen-activated protein kinase cascade and phosphorylation of cytoskeletal proteins after neurone-specific activation of p21ras. II. Cytoskeletal proteins and dendritic morphology. Neuroscience 2001;105:1041-1054.
    • (2001) Neuroscience , vol.105 , pp. 1041-1054
    • Holzer, M.1    Rodel, L.2    Seeger, G.3
  • 82
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • COI: 1:CAS:528:DC%2BC3sXnvVGkur0%3D, PID: 23684085
    • Spillantini MG, Goedert M. Tau pathology and neurodegeneration. Lancet Neurol 2013;12:609-622.
    • (2013) Lancet Neurol , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 83
    • 0033957692 scopus 로고    scopus 로고
    • PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid in mature hippocampal neurons
    • COI: 1:CAS:528:DC%2BD3cXlt1yi, PID: 10617113
    • Rapoport M, Ferreira A. PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid in mature hippocampal neurons. J Neurochem 2000;74:125-133.
    • (2000) J Neurochem , vol.74 , pp. 125-133
    • Rapoport, M.1    Ferreira, A.2
  • 84
    • 0028179001 scopus 로고
    • Secreted beta-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation
    • Greenberg SM, Koo EH, Selkoe DJ, Qiu WQ, Kosik KS. Secreted beta-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation. Proc Natl Acad Sci U S A 1994;91:7104-7108.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7104-7108
    • Greenberg, S.M.1    Koo, E.H.2    Selkoe, D.J.3    Qiu, W.Q.4    Kosik, K.S.5
  • 85
    • 0031952526 scopus 로고    scopus 로고
    • Regulation of secretion of Alzheimer amyloid precursor protein by the mitogen-activated protein kinase cascade
    • Desdouits-Magnen J, Desdouits F, Takeda S et al. Regulation of secretion of Alzheimer amyloid precursor protein by the mitogen-activated protein kinase cascade. J Neurochem 1998;70:524-530.
    • (1998) J Neurochem , vol.70 , pp. 524-530
    • Desdouits-Magnen, J.1    Desdouits, F.2    Takeda, S.3
  • 86
    • 0031453010 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway
    • Mills J, Laurent Charest D, Lam F et al. Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway. J Neurosci 1997;17:9415-9422.
    • (1997) J Neurosci , vol.17 , pp. 9415-9422
    • Mills, J.1    Laurent Charest, D.2    Lam, F.3
  • 87
    • 30744453036 scopus 로고    scopus 로고
    • ERK1/2 is an endogenous negative regulator of the gamma-secretase activity
    • Kim SK, Park HJ, Hong HS, Baik EJ, Jung MW, Mook-Jung I. ERK1/2 is an endogenous negative regulator of the gamma-secretase activity. FASEB J 2006;20:157-159.
    • (2006) FASEB J , vol.20 , pp. 157-159
    • Kim, S.K.1    Park, H.J.2    Hong, H.S.3    Baik, E.J.4    Jung, M.W.5    Mook-Jung, I.6
  • 88
    • 45249108210 scopus 로고    scopus 로고
    • Sodium selenite inhibits gamma-secretase activity through activation of ERK
    • Tung YT, Hsu WM, Wang BJ et al. Sodium selenite inhibits gamma-secretase activity through activation of ERK. Neurosci Lett 2008;440:38-43.
    • (2008) Neurosci Lett , vol.440 , pp. 38-43
    • Tung, Y.T.1    Hsu, W.M.2    Wang, B.J.3
  • 89
    • 84863253131 scopus 로고    scopus 로고
    • Activation of NMDA receptors upregulates a disintegrin and metalloproteinase 10 via a Wnt/MAPK signaling pathway
    • Wan X-Z, Li B, Li Y-C et al. Activation of NMDA receptors upregulates a disintegrin and metalloproteinase 10 via a Wnt/MAPK signaling pathway. J Neurosci 2012;32:3910-3916.
    • (2012) J Neurosci , vol.32 , pp. 3910-3916
    • Wan, X.-Z.1    Li, B.2    Li, Y.-C.3
  • 90
    • 33645799439 scopus 로고    scopus 로고
    • The neuropeptide PACAP promotes the alpha-secretase pathway for processing the Alzheimer amyloid precursor protein
    • Kojro E, Postina R, Buro C, Meiringer C, Gehrig-Burger K, Fahrenholz F. The neuropeptide PACAP promotes the alpha-secretase pathway for processing the Alzheimer amyloid precursor protein. FASEB J 2006;20:512-514.
    • (2006) FASEB J , vol.20 , pp. 512-514
    • Kojro, E.1    Postina, R.2    Buro, C.3    Meiringer, C.4    Gehrig-Burger, K.5    Fahrenholz, F.6
  • 91
    • 0035971080 scopus 로고    scopus 로고
    • Activated cAMP-response element-binding protein regulates neuronal expression of presenilin-1
    • Mitsuda N, Ohkubo N, Tamatani M et al. Activated cAMP-response element-binding protein regulates neuronal expression of presenilin-1. J Biol Chem 2001;276:9688-9698.
    • (2001) J Biol Chem , vol.276 , pp. 9688-9698
    • Mitsuda, N.1    Ohkubo, N.2    Tamatani, M.3
  • 92
    • 84886813109 scopus 로고    scopus 로고
    • The role of nitric oxide in pre-synaptic plasticity and homeostasis
    • PID: 24198758
    • Hardingham N, Dachtler J, Fox K. The role of nitric oxide in pre-synaptic plasticity and homeostasis. Front Cell Neurosci 2013;7:190.
    • (2013) Front Cell Neurosci , vol.7 , pp. 190
    • Hardingham, N.1    Dachtler, J.2    Fox, K.3
  • 93
    • 33751535253 scopus 로고    scopus 로고
    • Involvement of the nitric oxide pathway in synaptic dysfunction following amyloid elevation in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BD28XhtlentbzJ, PID: 17180876
    • Puzzo D, Palmeri A, Arancio O. Involvement of the nitric oxide pathway in synaptic dysfunction following amyloid elevation in Alzheimer's disease. Rev Neurosci 2006;17:497-523.
    • (2006) Rev Neurosci , vol.17 , pp. 497-523
    • Puzzo, D.1    Palmeri, A.2    Arancio, O.3
  • 94
    • 0033493229 scopus 로고    scopus 로고
    • Nitric oxide signaling contributes to late-phase LTP and CREB phosphorylation in the hippocampus
    • COI: 1:CAS:528:DyaK1MXnslyrt70%3D, PID: 10575022
    • Lu YF, Kandel ER, Hawkins RD. Nitric oxide signaling contributes to late-phase LTP and CREB phosphorylation in the hippocampus. J Neurosci 1999;19:10250-10261.
    • (1999) J Neurosci , vol.19 , pp. 10250-10261
    • Lu, Y.F.1    Kandel, E.R.2    Hawkins, R.D.3
  • 95
    • 84866480918 scopus 로고    scopus 로고
    • Cyclic GMP/protein kinase G type-Ialpha (PKG-Ialpha) signaling pathway promotes CREB phosphorylation and maintains higher c-IAP1, livin, survivin, and Mcl-1 expression and the inhibition of PKG-Ialpha kinase activity synergizes with cisplatin in non-small cell lung cancer cells
    • COI: 1:CAS:528:DC%2BC38XhtlKjtbzK, PID: 22740515
    • Wong JC, Bathina M, Fiscus RR. Cyclic GMP/protein kinase G type-Ialpha (PKG-Ialpha) signaling pathway promotes CREB phosphorylation and maintains higher c-IAP1, livin, survivin, and Mcl-1 expression and the inhibition of PKG-Ialpha kinase activity synergizes with cisplatin in non-small cell lung cancer cells. J Cell Biochem 2012;113:3587-3598.
    • (2012) J Cell Biochem , vol.113 , pp. 3587-3598
    • Wong, J.C.1    Bathina, M.2    Fiscus, R.R.3
  • 96
    • 30744455255 scopus 로고    scopus 로고
    • A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons
    • Riccio A, Alvania RS, Lonze BE, et al. A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons. Mol Cell 2006;21:283-294.
    • (2006) Mol Cell , vol.21 , pp. 283-294
    • Riccio, A.1    Alvania, R.S.2    Lonze, B.E.3
  • 97
    • 0029926167 scopus 로고    scopus 로고
    • Hippocampal cGMP and cAMP are differentially involved in memory processing of inhibitory avoidance learning
    • Bernabeu R, Schmitz P, Faillace MP, Izquierdo I, Medina JH. Hippocampal cGMP and cAMP are differentially involved in memory processing of inhibitory avoidance learning. Neuroreport 1996;7:585-588.
    • (1996) Neuroreport , vol.7 , pp. 585-588
    • Bernabeu, R.1    Schmitz, P.2    Faillace, M.P.3    Izquierdo, I.4    Medina, J.H.5
  • 98
    • 32044472303 scopus 로고    scopus 로고
    • Critical role of nitric oxide-cGMP cascade in the formation of cAMP-dependent long-term memory
    • Matsumoto Y, Unoki S, Aonuma H, Mizunami M. Critical role of nitric oxide-cGMP cascade in the formation of cAMP-dependent long-term memory. Learn Mem 2006;13:35-44.
    • (2006) Learn Mem , vol.13 , pp. 35-44
    • Matsumoto, Y.1    Unoki, S.2    Aonuma, H.3    Mizunami, M.4
  • 99
    • 33847305401 scopus 로고    scopus 로고
    • Time-dependent involvement of cAMP and cGMP in consolidation of object memory: studies using selective phosphodiesterase type 2, 4 and 5 inhibitors
    • Rutten K, Prickaerts J, Hendrix M, van der Staay FJ, Sik A, Blokland A. Time-dependent involvement of cAMP and cGMP in consolidation of object memory: studies using selective phosphodiesterase type 2, 4 and 5 inhibitors. Eur J Pharmacol 2007;558:107-112.
    • (2007) Eur J Pharmacol , vol.558 , pp. 107-112
    • Rutten, K.1    Prickaerts, J.2    Hendrix, M.3    van der Staay, F.J.4    Sik, A.5    Blokland, A.6
  • 100
    • 84930899312 scopus 로고    scopus 로고
    • Improved long-term memory via enhancing cGMP-PKG signaling requires cAMP-PKA signaling
    • Bollen E, Puzzo D, Rutten K, et al. Improved long-term memory via enhancing cGMP-PKG signaling requires cAMP-PKA signaling. Neuropsychopharmacology 2014;39:2497-2505.
    • (2014) Neuropsychopharmacology , vol.39 , pp. 2497-2505
    • Bollen, E.1    Puzzo, D.2    Rutten, K.3
  • 101
    • 0033119839 scopus 로고    scopus 로고
    • Regulation of CBP-mediated transcription by neuronal calcium signaling
    • COI: 1:CAS:528:DyaK1MXivVOhu7c%3D, PID: 10230799
    • Hu SC, Chrivia J, Ghosh A. Regulation of CBP-mediated transcription by neuronal calcium signaling. Neuron 1999;22:799-808.
    • (1999) Neuron , vol.22 , pp. 799-808
    • Hu, S.C.1    Chrivia, J.2    Ghosh, A.3
  • 102
    • 0030972807 scopus 로고    scopus 로고
    • Transcriptional regulation by cyclic AMP
    • COI: 1:CAS:528:DyaK2sXktFOksbk%3D, PID: 9242925
    • Montminy M. Transcriptional regulation by cyclic AMP. Annu Rev Biochem 1997;66:807-822.
    • (1997) Annu Rev Biochem , vol.66 , pp. 807-822
    • Montminy, M.1
  • 103
    • 0032034262 scopus 로고    scopus 로고
    • Ca2+ influx regulates BDNF transcription by a CREB family transcription factor-dependent mechanism
    • Tao X, Finkbeiner S, Arnold DB, Shaywitz AJ, Greenberg ME. Ca2+ influx regulates BDNF transcription by a CREB family transcription factor-dependent mechanism. Neuron 1998;20:709-726.
    • (1998) Neuron , vol.20 , pp. 709-726
    • Tao, X.1    Finkbeiner, S.2    Arnold, D.B.3    Shaywitz, A.J.4    Greenberg, M.E.5
  • 104
    • 0031036208 scopus 로고    scopus 로고
    • Morphological plasticity of dendritic spines in central neurons is mediated by activation of cAMP response element binding protein
    • COI: 1:CAS:528:DyaK2sXhtl2nsLs%3D, PID: 9037079
    • Murphy DD, Segal M. Morphological plasticity of dendritic spines in central neurons is mediated by activation of cAMP response element binding protein. Proc Natl Acad Sci U S A 1997;94:1482-1487.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1482-1487
    • Murphy, D.D.1    Segal, M.2
  • 105
    • 0032934183 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's beta-amyloid induced vasoactivity and proinflammatory response in microglia by a cGMP-dependent mechanism
    • Paris D, Town T, Parker TA, et al. Inhibition of Alzheimer's beta-amyloid induced vasoactivity and proinflammatory response in microglia by a cGMP-dependent mechanism. Exp Neurol 1999;157:211-221.
    • (1999) Exp Neurol , vol.157 , pp. 211-221
    • Paris, D.1    Town, T.2    Parker, T.A.3
  • 106
    • 0032447180 scopus 로고    scopus 로고
    • Vascular nitric oxide may lessen Alzheimer's risk
    • COI: 1:CAS:528:DyaK1MXhtleit74%3D, PID: 10052865
    • McCarty MF. Vascular nitric oxide may lessen Alzheimer's risk. Med Hypotheses 1998;51:465-476.
    • (1998) Med Hypotheses , vol.51 , pp. 465-476
    • McCarty, M.F.1
  • 107
    • 0037404666 scopus 로고    scopus 로고
    • Abeta42 generation is toxic to endothelial cells and inhibits eNOS function through an Akt/GSK-3beta signaling-dependent mechanism
    • Suhara T, Magrane J, Rosen K, et al. Abeta42 generation is toxic to endothelial cells and inhibits eNOS function through an Akt/GSK-3beta signaling-dependent mechanism. Neurobiol Aging 2003;24:437-451.
    • (2003) Neurobiol Aging , vol.24 , pp. 437-451
    • Suhara, T.1    Magrane, J.2    Rosen, K.3
  • 108
    • 0036884511 scopus 로고    scopus 로고
    • Beta-amyloid inhibits NOS activity by subtracting NADPH availability
    • Venturini G, Colasanti M, Persichini T, et al. Beta-amyloid inhibits NOS activity by subtracting NADPH availability. FASEB J 2002;16:1970-1972.
    • (2002) FASEB J , vol.16 , pp. 1970-1972
    • Venturini, G.1    Colasanti, M.2    Persichini, T.3
  • 109
    • 0036077251 scopus 로고    scopus 로고
    • Beta-amyloid peptides decrease soluble guanylyl cyclase expression in astroglial cells
    • Baltrons MA, Pedraza CE, Heneka MT, Garcia A. Beta-amyloid peptides decrease soluble guanylyl cyclase expression in astroglial cells. Neurobiol Dis 2002;10:139-149.
    • (2002) Neurobiol Dis , vol.10 , pp. 139-149
    • Baltrons, M.A.1    Pedraza, C.E.2    Heneka, M.T.3    Garcia, A.4
  • 110
    • 22544485048 scopus 로고    scopus 로고
    • Amyloid-beta peptide inhibits activation of the nitric oxide/cGMP/cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity
    • Puzzo D, Vitolo O, Trinchese F, Jacob JP, Palmeri A, Arancio O. Amyloid-beta peptide inhibits activation of the nitric oxide/cGMP/cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity. J Neurosci 2005;25:6887-6897.
    • (2005) J Neurosci , vol.25 , pp. 6887-6897
    • Puzzo, D.1    Vitolo, O.2    Trinchese, F.3    Jacob, J.P.4    Palmeri, A.5    Arancio, O.6
  • 111
    • 78650992961 scopus 로고    scopus 로고
    • Amyloid-beta inhibits No-cGMP signaling in a CD36- and CD47-dependent manner
    • Miller TW, Isenberg JS, Shih HB, Wang Y, Robert DD. Amyloid-beta inhibits No-cGMP signaling in a CD36- and CD47-dependent manner. PLoS One 2010;5:e15686.
    • (2010) PLoS One , vol.e15686 , pp. 5
    • Miller, T.W.1    Isenberg, J.S.2    Shih, H.B.3    Wang, Y.4    Robert, D.D.5
  • 112
    • 67649342620 scopus 로고    scopus 로고
    • Phosphodiesterase 5 inhibition improves synaptic function, memory, and amyloid-beta load in an Alzheimer's disease mouse model
    • Puzzo D, Staniszewski A, Deng SX, et al. Phosphodiesterase 5 inhibition improves synaptic function, memory, and amyloid-beta load in an Alzheimer's disease mouse model. J Neurosci 2009;29:8075-8086.
    • (2009) J Neurosci , vol.29 , pp. 8075-8086
    • Puzzo, D.1    Staniszewski, A.2    Deng, S.X.3
  • 113
    • 84875080648 scopus 로고    scopus 로고
    • Inhibition of phosphodiesterase-5 rescues age-related impairment of synaptic plasticity and memory
    • Palmeri A, Privitera L, Giunta S, Loreto C, Puzzo D. Inhibition of phosphodiesterase-5 rescues age-related impairment of synaptic plasticity and memory. Behav Brain Res 2013;240:11-20.
    • (2013) Behav Brain Res , vol.240 , pp. 11-20
    • Palmeri, A.1    Privitera, L.2    Giunta, S.3    Loreto, C.4    Puzzo, D.5
  • 114
    • 0034706062 scopus 로고    scopus 로고
    • Guanosine 3',5'-cyclic monophosphate mediated inhibition of cell death induced by nerve growth factor withdrawal and beta-amyloid: protective effects of propentofylline
    • COI: 1:CAS:528:DC%2BD3cXmtF2hs7c%3D, PID: 10974437
    • Wirtz-Brugger F, Giovanni A. Guanosine 3',5'-cyclic monophosphate mediated inhibition of cell death induced by nerve growth factor withdrawal and beta-amyloid: protective effects of propentofylline. Neuroscience 2000;99:737-750.
    • (2000) Neuroscience , vol.99 , pp. 737-750
    • Wirtz-Brugger, F.1    Giovanni, A.2
  • 115
    • 0028883271 scopus 로고
    • Reduced nitric oxide responsive soluble guanylyl cyclase activity in the superior temporal cortex of patients with Alzheimer's disease
    • Bonkale WL, Winblad B, Ravid R, Cowburn RF. Reduced nitric oxide responsive soluble guanylyl cyclase activity in the superior temporal cortex of patients with Alzheimer's disease. Neurosci Lett 1995;187:5-8.
    • (1995) Neurosci Lett , vol.187 , pp. 5-8
    • Bonkale, W.L.1    Winblad, B.2    Ravid, R.3    Cowburn, R.F.4
  • 116
    • 0036723924 scopus 로고    scopus 로고
    • Nitric oxide regulates cGMP-dependent cAMP-responsive element binding protein phosphorylation and Bcl-2 expression in cerebellar neurons: implication for a survival role of nitric oxide
    • Ciani E, Guidi S, Bartesaghi R, Contestabile A. Nitric oxide regulates cGMP-dependent cAMP-responsive element binding protein phosphorylation and Bcl-2 expression in cerebellar neurons: implication for a survival role of nitric oxide. J Neurochem 2002;82:1282-1289.
    • (2002) J Neurochem , vol.82 , pp. 1282-1289
    • Ciani, E.1    Guidi, S.2    Bartesaghi, R.3    Contestabile, A.4
  • 117
    • 0034649494 scopus 로고    scopus 로고
    • NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation
    • Gudi T, Casteel DE, Vinson C, Boss GR, Pilz RB. NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation. Oncogene 2000;19:6324-6333.
    • (2000) Oncogene , vol.19 , pp. 6324-6333
    • Gudi, T.1    Casteel, D.E.2    Vinson, C.3    Boss, G.R.4    Pilz, R.B.5
  • 118
    • 0035907325 scopus 로고    scopus 로고
    • Beta -amyloid-(1-42) impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival Is not compromised
    • Tong L, Thornton PL, Balazs R, Cotman CW. Beta -amyloid-(1-42) impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival Is not compromised. J Biol Chem 2001;276:17301-17306.
    • (2001) J Biol Chem , vol.276 , pp. 17301-17306
    • Tong, L.1    Thornton, P.L.2    Balazs, R.3    Cotman, C.W.4
  • 119
    • 84869152162 scopus 로고    scopus 로고
    • Age-related loss of nitric oxide synthase in skeletal muscle causes reductions in calpain S-nitrosylation that increase myofibril degradation and sarcopenia
    • Samengo G, Avik A, Fedor B, et al. Age-related loss of nitric oxide synthase in skeletal muscle causes reductions in calpain S-nitrosylation that increase myofibril degradation and sarcopenia. Aging Cell 2012;11:1036-1045.
    • (2012) Aging Cell , vol.11 , pp. 1036-1045
    • Samengo, G.1    Avik, A.2    Fedor, B.3
  • 120
    • 77955088377 scopus 로고    scopus 로고
    • Cyclic GMP and nitric oxide synthase in aging and Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC3cXmsFSqtr0%3D, PID: 20213343
    • Domek-Lopacinska KU, Strosznajder JB. Cyclic GMP and nitric oxide synthase in aging and Alzheimer's disease. Mol Neurobiol 2010;41:129-137.
    • (2010) Mol Neurobiol , vol.41 , pp. 129-137
    • Domek-Lopacinska, K.U.1    Strosznajder, J.B.2
  • 121
    • 0037129914 scopus 로고    scopus 로고
    • Neuronal and inducible nitric oxide synthase expressions and activities in the hippocampi and cortices of young adult, aged cognitively unimpaired, and impaired Long-Evans rats
    • Law A, O'Donnell J, Gauthier S, Quirion R. Neuronal and inducible nitric oxide synthase expressions and activities in the hippocampi and cortices of young adult, aged cognitively unimpaired, and impaired Long-Evans rats. Neuroscience 2002;112:267-275.
    • (2002) Neuroscience , vol.112 , pp. 267-275
    • Law, A.1    O'Donnell, J.2    Gauthier, S.3    Quirion, R.4
  • 122
    • 33846979103 scopus 로고    scopus 로고
    • Ageing reduces nitric-oxide- and prostaglandin-mediated vasodilatation in exercising humans
    • COI: 1:CAS:528:DC%2BD2sXjsVyktrY%3D, PID: 17138603
    • Schrage WG, Eisenach JH, Joyner MJ. Ageing reduces nitric-oxide- and prostaglandin-mediated vasodilatation in exercising humans. J Physiol 2007;579:227-236.
    • (2007) J Physiol , vol.579 , pp. 227-236
    • Schrage, W.G.1    Eisenach, J.H.2    Joyner, M.J.3
  • 123
    • 0036235003 scopus 로고    scopus 로고
    • Nitric-oxide releasing molecules: a new class of drugs with several major indications
    • COI: 1:CAS:528:DC%2BD38XhvFKmurk%3D, PID: 11864065
    • Burgaud JL, Riffaud JP, Del Soldato P. Nitric-oxide releasing molecules: a new class of drugs with several major indications. Curr Pharm Des 2002;8:201-213.
    • (2002) Curr Pharm Des , vol.8 , pp. 201-213
    • Burgaud, J.L.1    Riffaud, J.P.2    Del Soldato, P.3
  • 124
    • 0037088914 scopus 로고    scopus 로고
    • Microglial activation and beta -amyloid deposit reduction caused by a nitric oxide-releasing nonsteroidal anti-inflammatory drug in amyloid precursor protein plus presenilin-1 transgenic mice
    • Jantzen PT, Connor KE, DiCarlo G, et al. Microglial activation and beta -amyloid deposit reduction caused by a nitric oxide-releasing nonsteroidal anti-inflammatory drug in amyloid precursor protein plus presenilin-1 transgenic mice. J Neurosci 2002;22:2246-2254.
    • (2002) J Neurosci , vol.22 , pp. 2246-2254
    • Jantzen, P.T.1    Connor, K.E.2    DiCarlo, G.3
  • 126
    • 20844461153 scopus 로고    scopus 로고
    • Nitric oxide mimetic molecules as therapeutic agents in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BD2MXltVantrY%3D, PID: 15974915
    • Thatcher GR, Bennett BM, Reynolds JN. Nitric oxide mimetic molecules as therapeutic agents in Alzheimer's disease. Curr Alzheimer Res 2005;2:171-182.
    • (2005) Curr Alzheimer Res , vol.2 , pp. 171-182
    • Thatcher, G.R.1    Bennett, B.M.2    Reynolds, J.N.3
  • 127
    • 1942519702 scopus 로고    scopus 로고
    • Attenuation of chronic neuroinflammation by a nitric oxide-releasing derivative of the antioxidant ferulic acid
    • Wenk GL, McGann-Gramling K, Hauss-Wegrzyniak B, et al. Attenuation of chronic neuroinflammation by a nitric oxide-releasing derivative of the antioxidant ferulic acid. J Neurochem. 2004;89:484-493.
    • (2004) J Neurochem , vol.89 , pp. 484-493
    • Wenk, G.L.1    McGann-Gramling, K.2    Hauss-Wegrzyniak, B.3
  • 128
    • 84872115394 scopus 로고    scopus 로고
    • Synthesis of quinoline derivatives: discovery of a potent and selective phosphodiesterase 5 inhibitor for the treatment of Alzheimer's disease
    • Fiorito J, Saeed F, Zhang H, et al. Synthesis of quinoline derivatives: discovery of a potent and selective phosphodiesterase 5 inhibitor for the treatment of Alzheimer's disease. Eur J Med Chem 2013; 60:285-294.
    • (2013) Eur J Med Chem , vol.60 , pp. 285-294
    • Fiorito, J.1    Saeed, F.2    Zhang, H.3
  • 129
    • 84889560709 scopus 로고    scopus 로고
    • Effect of phosphodiesterase-5 inhibition on apoptosis and beta amyloid load in aged mice
    • Puzzo D, Loreto C, Giunta S, et al. Effect of phosphodiesterase-5 inhibition on apoptosis and beta amyloid load in aged mice. Neurobiol Aging 2014;35:520-531.
    • (2014) Neurobiol Aging , vol.35 , pp. 520-531
    • Puzzo, D.1    Loreto, C.2    Giunta, S.3
  • 131
    • 79960104591 scopus 로고    scopus 로고
    • Impact of genetic insights into calpain biology
    • Sorimachi H, Hata S, Ono Y. Impact of genetic insights into calpain biology. J Biochem 2011;150:23-37.
    • (2011) J Biochem , vol.150 , pp. 23-37
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 132
    • 33747870115 scopus 로고    scopus 로고
    • Calpain and synaptic function
    • Wu HY, Lynch DR. Calpain and synaptic function. Mol Neurobiol 2006;33:215-236.
    • (2006) Mol Neurobiol , vol.33 , pp. 215-236
    • Wu, H.Y.1    Lynch, D.R.2
  • 134
    • 0024340134 scopus 로고
    • The role of autolysis in activity of the Ca2+-dependent proteinases (mu-calpain and m-calpain)
    • Cong J, Goll DE, Peterson AM, Kapprell HP. The role of autolysis in activity of the Ca2+-dependent proteinases (mu-calpain and m-calpain). J Biol Chem 1989;264:10096-10103.
    • (1989) J Biol Chem , vol.264 , pp. 10096-10103
  • 135
    • 27844553889 scopus 로고    scopus 로고
    • Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain
    • Liu F, Grundke-Iqbal I, Iqbal K, Oda Y, Tomizawa K, Gong CX. Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain. J Biol Chem 2005;280:37755-37762.
    • (2005) J Biol Chem , vol.280 , pp. 37755-37762
  • 136
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration
    • Saito K, Elce JS, Hamos JE, Nixon RA. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 1993;90:2628-2632.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 137
    • 0023280254 scopus 로고
    • Protein kinase C injection into hippocampal pyramidal cells elicits features of long term potentiation
    • Hu GY, Hvalby O, Walaas SI, et al. Protein kinase C injection into hippocampal pyramidal cells elicits features of long term potentiation. Nature 1987;328:426-429.
    • (1987) Nature , vol.328 , pp. 426-429
    • Hu, G.Y.1    Hvalby, O.2    Walaas, S.I.3
  • 138
    • 0028880861 scopus 로고
    • Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism
    • Lledo, PM, Hjelmstad GO, Mukherji S, Soderling TR, Malenka RC, Nicoll RA. Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism. Proc Natl Acad Sci U S A 1995;92:11175-11179.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 11175-11179
  • 139
    • 0024461379 scopus 로고
    • Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP
    • Malinow R, Schulman H, Tsien RW. Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP. Science 1989;245:862-826.
    • (1989) Science , vol.245 , pp. 862-826
    • Malinow, R.1    Schulman, H.2    Tsien, R.W.3
  • 140
    • 0030857360 scopus 로고    scopus 로고
    • Postsynaptic inhibitors of calcium/calmodulin-dependent protein kinase type II block induction but not maintenance of pairing-induced long-term potentiation
    • Otmakhov N, Griffith LC, Lisman JE. Postsynaptic inhibitors of calcium/calmodulin-dependent protein kinase type II block induction but not maintenance of pairing-induced long-term potentiation. J Neurosci 1997;17:5357-5365.
    • (1997) J Neurosci , vol.17 , pp. 5357-5365
    • Otmakhov, N.1    Griffith, L.C.2    Lisman, J.E.3
  • 141
    • 0030756917 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIalpha undergo neurotoxin-induced proteolysis
    • Hajimohammadreza I, Raser KJ, Nath R, Nadimpalli R, Scott M, Wang KK. Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIalpha undergo neurotoxin-induced proteolysis. J Neurochem 1997;69:1006-1013.
    • (1997) J Neurochem , vol.69 , pp. 1006-1013
    • Hajimohammadreza, I.1    Raser, K.J.2    Nath, R.3    Nadimpalli, R.4    Scott, M.5    Wang, K.K.6
  • 142
    • 0029799241 scopus 로고    scopus 로고
    • Bidirectional regulation of protein kinase M zeta in the maintenance of long-term potentiation and long-term depression
    • Hrabetova S, Sacktor TC. Bidirectional regulation of protein kinase M zeta in the maintenance of long-term potentiation and long-term depression. J Neurosci 1996;16:5324-5233.
    • (1996) J Neurosci , vol.16 , pp. 5233-5324
    • Hrabetova, S.1    Sacktor, T.C.2
  • 143
    • 1042301378 scopus 로고    scopus 로고
    • Critical role of calpain-mediated cleavage of calcineurin in excitotoxic neurodegeneration
    • Wu HY, Tomizawa K, Oda Y, et al. Critical role of calpain-mediated cleavage of calcineurin in excitotoxic neurodegeneration. J Biol Chem 2004;279:4929-4940.
    • (2004) J Biol Chem , vol.279 , pp. 4929-4940
    • Wu, H.Y.1    Tomizawa, K.2    Oda, Y.3
  • 144
    • 0027441185 scopus 로고
    • Specific cleavage of transcription factors by the thiol protease, m-calpain
    • Watt F, Molloy PL. Specific cleavage of transcription factors by the thiol protease, m-calpain. Nucleic Acids Res 1993;21:5092-100.
    • (1993) Nucleic Acids Res , vol.21 , pp. 5092-5100
    • Watt, F.1    Molloy, P.L.2
  • 145
    • 84876389884 scopus 로고    scopus 로고
    • CREB regulates the expression of neuronal glucose transporter 3: a possible mechanism related to impaired brain glucose uptake in Alzheimer's disease
    • Jin N, Qian W, Yin X, et al. CREB regulates the expression of neuronal glucose transporter 3: a possible mechanism related to impaired brain glucose uptake in Alzheimer's disease. Nucleic Acids Res 2013;41:3240-3256.
    • (2013) Nucleic Acids Res , vol.41 , pp. 3240-3256
    • Jin, N.1    Qian, W.2    Yin, X.3
  • 146
    • 0032516861 scopus 로고    scopus 로고
    • cAMP response element-binding protein monomers cooperatively assemble to form dimers on DNA
    • Wu X, Spiro C, Owen WG, McMurray CT. cAMP response element-binding protein monomers cooperatively assemble to form dimers on DNA. J Biol Chem 1998;273:20820-20827.
    • (1998) J Biol Chem , vol.273 , pp. 20820-20827
    • Wu, X.1    Spiro, C.2    Owen, W.G.3    McMurray, C.T.4
  • 147
    • 79960735446 scopus 로고    scopus 로고
    • Calpain-mediated tau cleavage: a mechanism leading to neurodegeneration shared by multiple tauopathies
    • Ferreira A, Bigio EH. Calpain-mediated tau cleavage: a mechanism leading to neurodegeneration shared by multiple tauopathies. Mol Med 2011;17:676-685.
    • (2011) Mol Med , vol.17 , pp. 676-685
  • 148
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • Higuchi M, Tomioka M, Takano J, et al. Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors. J Biol Chem 2005;280:15229-15237.
    • (2005) J Biol Chem , vol.280 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3
  • 150
    • 0343050763 scopus 로고
    • Alterations in calcium content and biochemical processes in cultured skin fibroblasts from aged and Alzheimer donors
    • Peterson C, Goldman JE. Alterations in calcium content and biochemical processes in cultured skin fibroblasts from aged and Alzheimer donors. Proc Natl Acad Sci U S A 1986;83:2758-2762.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 2758-2762
    • Peterson, C.1    Goldman, J.E.2
  • 152
    • 0032577543 scopus 로고    scopus 로고
    • m-Calpain (calcium-activated neutral proteinase) in Alzheimer's disease brains
    • Tsuji T, Shimohama S, Kimura J, Shimizu K. m-Calpain (calcium-activated neutral proteinase) in Alzheimer's disease brains. Neurosci Lett 1998;248:109-112.
    • (1998) Neurosci Lett , vol.248 , pp. 109-112
    • Tsuji, T.1    Shimohama, S.2    Kimura, J.3    Shimizu, K.4
  • 153
    • 53749096967 scopus 로고    scopus 로고
    • Calpain-mediated signaling mechanisms in neuronal injury and neurodegeneration
    • COI: 1:CAS:528:DC%2BD1cXhtVSgtLrP, PID: 18686046
    • Vosler PS, Brennan CS, Chen J. Calpain-mediated signaling mechanisms in neuronal injury and neurodegeneration. Mol Neurobiol 2008;38:78-100.
    • (2008) Mol Neurobiol , vol.38 , pp. 78-100
    • Vosler, P.S.1    Brennan, C.S.2    Chen, J.3
  • 154
    • 48749089723 scopus 로고    scopus 로고
    • Inhibition of calpains improves memory and synaptic transmission in a mouse model of Alzheimer disease
    • Trinchese F, Fa M, Liu S, et al. Inhibition of calpains improves memory and synaptic transmission in a mouse model of Alzheimer disease. J Clin Invest 2008;118:2796-2807.
    • (2008) J Clin Invest , vol.118 , pp. 2796-2807
    • Trinchese, F.1    Fa, M.2    Liu, S.3
  • 155
  • 156
    • 0030238146 scopus 로고    scopus 로고
    • Spatial learning and memory in calpastatin-deficient rats
    • Toth E, Bruin JP, Heinsbroek RP, Joosten RN. Spatial learning and memory in calpastatin-deficient rats. Neurobiol Learn Mem 1996;66:230-235.
    • (1996) Neurobiol Learn Mem , vol.66 , pp. 230-235
  • 157
    • 36448978859 scopus 로고    scopus 로고
    • Down-regulation of cAMP-dependent protein kinase by over-activated calpain in Alzheimer disease brain
    • Liang Z, Liu F, Grundke-Iqbal I, Iqbal K, Gong CX. Down-regulation of cAMP-dependent protein kinase by over-activated calpain in Alzheimer disease brain. J Neurochem 2007;103:2462-2470.
    • (2007) J Neurochem , vol.103 , pp. 2462-2470
    • Liang, Z.1    Liu, F.2    Grundke-Iqbal, I.3    Iqbal, K.4    Gong, C.X.5
  • 159
    • 84863917216 scopus 로고    scopus 로고
    • Sheng M, Sabatini BL, Sudhof TC. Synapses and Alzheimer's disease. Cold Spring Harb Perspect Biol 2012;4(5): a005777
    • Sheng M, Sabatini BL, Sudhof TC. Synapses and Alzheimer's disease. Cold Spring Harb Perspect Biol 2012;4(5): a005777.
  • 160
    • 84897924151 scopus 로고    scopus 로고
    • Calpain Dysregulation in Alzheimer's Disease
    • Ferreira A. Calpain Dysregulation in Alzheimer's Disease. ISRN Biochemistry 2012;12. doi:10.5402/2012/728571
    • (2012) ISRN Biochemistry , pp. 12
    • Ferreira, A.1
  • 161
    • 77956258994 scopus 로고    scopus 로고
    • Luo ZG. Calpain activation promotes BACE1 expression, amyloid precursor protein processing, and amyloid plaque formation in a transgenic mouse model of Alzheimer disease
    • Liang B, Duan BY, Zhou XP, Gong JX, Luo ZG. Calpain activation promotes BACE1 expression, amyloid precursor protein processing, and amyloid plaque formation in a transgenic mouse model of Alzheimer disease. J Biol Chem 2010;285:27737-27744.
    • (2010) J Biol Chem , vol.285 , pp. 27737-27744
    • Liang, B.1    Duan, B.Y.2    Zhou, X.P.3    Gong, J.X.4
  • 162
    • 0030836467 scopus 로고    scopus 로고
    • Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease
    • Grynspan F, Griffin WR, Cataldo A, Katayama S, Nixon RA. Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease. Brain Res 1997;763:145-158.
    • (1997) Brain Res , vol.763 , pp. 145-158
    • Grynspan, F.1    Griffin, W.R.2    Cataldo, A.3    Katayama, S.4    Nixon, R.A.5
  • 163
    • 84898603240 scopus 로고    scopus 로고
    • Activity-dependent p25 generation regulates synaptic plasticity and Abeta-induced cognitive impairment
    • Seo J, Giusti-Rodriguez P, Zhou Y, et al. Activity-dependent p25 generation regulates synaptic plasticity and Abeta-induced cognitive impairment. Cell 2014;157:486-498.
    • (2014) Cell , vol.157 , pp. 486-498
    • Seo, J.1    Giusti-Rodriguez, P.2    Zhou, Y.3
  • 164
    • 84857754220 scopus 로고    scopus 로고
    • Mechanistic involvement of the calpain-calpastatin system in Alzheimer neuropathology
    • Higuchi M, Iwata N, Matsuba Y, et al. Mechanistic involvement of the calpain-calpastatin system in Alzheimer neuropathology. FASEB J 2012;26:1204-1217.
    • (2012) FASEB J , vol.26 , pp. 1204-1217
    • Higuchi, M.1    Iwata, N.2    Matsuba, Y.3
  • 165
    • 79955106083 scopus 로고    scopus 로고
    • Calpain inhibitors: a survey of compounds reported in the patent and scientific literature
    • COI: 1:CAS:528:DC%2BC3MXkvFantrY%3D, PID: 21434837
    • Donkor IO. Calpain inhibitors: a survey of compounds reported in the patent and scientific literature. Expert Opin Ther Pat 2011;21:601-636.
    • (2011) Expert Opin Ther Pat , vol.21 , pp. 601-636
    • Donkor, I.O.1
  • 166
    • 77949469511 scopus 로고    scopus 로고
    • Calpains: attractive targets for the development of synthetic inhibitors
    • Pietsch M, Chua KC, Abell AD. Calpains: attractive targets for the development of synthetic inhibitors. Curr Top Med Chem 2010;10:270-293.
    • (2010) Curr Top Med Chem , vol.10 , pp. 270-293
    • Pietsch, M.1    Chua, K.C.2    Abell, A.D.3
  • 169
    • 0018895711 scopus 로고
    • Inhibition of Epoxide Derivatives on Chicken Calcium-Activated Neutral Protease (Canp) Invitro and Invivo
    • Sugita H, Ishiura S, Suzuki K, Imahori K. Inhibition of Epoxide Derivatives on Chicken Calcium-Activated Neutral Protease (Canp) Invitro and Invivo. Journal of Biochemistry 1980;87:339-341.
    • (1980) Journal of Biochemistry , vol.87 , pp. 339-341
    • Sugita, H.1    Ishiura, S.2    Suzuki, K.3    Imahori, K.4
  • 171
    • 84881466563 scopus 로고    scopus 로고
    • Design, Synthesis, and Optimization of Novel Epoxide Incorporating Peptidomimetics as Selective Calpain Inhibitors
    • Schiefer IT, Tapadar S, Litosh V, et al. Design, Synthesis, and Optimization of Novel Epoxide Incorporating Peptidomimetics as Selective Calpain Inhibitors. Journal of Medicinal Chemistry 2013;56:6054-6068.
    • (2013) Journal of Medicinal Chemistry , vol.56 , pp. 6054-6068
    • Schiefer, I.T.1    Tapadar, S.2    Litosh, V.3
  • 172
    • 0029803744 scopus 로고    scopus 로고
    • Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-amyloid precursor protein by different protease activities
    • Citron M, Diehl TS, Gordon G, Biere AL, Seubert P, Selkoe DJ. Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-amyloid precursor protein by different protease activities. Proc Natl Acad Sci U S A 1996;93:13170-13175.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13170-13175
    • Citron, M.1    Diehl, T.S.2    Gordon, G.3    Biere, A.L.4    Seubert, P.5    Selkoe, D.J.6
  • 173
    • 0028987849 scopus 로고
    • Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
    • Higaki J, Quon D, Zhong Z, Cordell B. Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. Neuron 1995;14:651-659.
    • (1995) Neuron , vol.14 , pp. 651-659
    • Higaki, J.1    Quon, D.2    Zhong, Z.3    Cordell, B.4
  • 174
    • 84863607935 scopus 로고    scopus 로고
    • The novel calpain inhibitor A-705253 prevents stress-induced tau hyperphosphorylation in vitro and in vivo
    • Nikkel AL, Martino B, Markosyan S, et al. The novel calpain inhibitor A-705253 prevents stress-induced tau hyperphosphorylation in vitro and in vivo. Neuropharmacology 2012;63:606-612.
    • (2012) Neuropharmacology , vol.63 , pp. 606-612
    • Nikkel, A.L.1    Martino, B.2    Markosyan, S.3
  • 175
    • 48349100916 scopus 로고    scopus 로고
    • The novel calpain inhibitor A-705253 potently inhibits oligomeric beta-amyloid-induced dynamin 1 and tau cleavage in hippocampal neurons
    • Sinjoanu RC, Kleinschmidt S, Bitner RS, Brioni JD, Moeller A, Ferreira A. The novel calpain inhibitor A-705253 potently inhibits oligomeric beta-amyloid-induced dynamin 1 and tau cleavage in hippocampal neurons. Neurochemistry International 2008;53:79-88.
    • (2008) Neurochemistry International , vol.53 , pp. 79-88
    • Sinjoanu, R.C.1    Kleinschmidt, S.2    Bitner, R.S.3    Brioni, J.D.4    Moeller, A.5    Ferreira, A.6
  • 176
    • 84864140992 scopus 로고    scopus 로고
    • Calpain Inhibitor A-705253 Mitigates Alzheimer's Disease-Like Pathology and Cognitive Decline in Aged 3xTgAD Mice
    • Medeiros R, Kitazawa M, Chabrier MA, et al. Calpain Inhibitor A-705253 Mitigates Alzheimer's Disease-Like Pathology and Cognitive Decline in Aged 3xTgAD Mice. American Journal of Pathology 2012;181:616-625.
    • (2012) American Journal of Pathology , vol.181 , pp. 616-625
    • Medeiros, R.1    Kitazawa, M.2    Chabrier, M.A.3
  • 177
    • 84886291065 scopus 로고    scopus 로고
    • Acetyltransferases (HATs) as targets for neurological therapeutics
    • Schneider A, Chatterjee S, Bousiges O, et al. Acetyltransferases (HATs) as targets for neurological therapeutics. Neurotherapeutics 2013;10:568-588.
    • (2013) Neurotherapeutics , vol.10 , pp. 568-588
  • 178
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • COI: 1:CAS:528:DC%2BD28XptVCltrY%3D, PID: 16955068
    • Bolden JE, Peart MJ, Johnstone RW. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 2006;5:769-784.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 179
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • Fischer A, Sananbenesi F, Wang X, Dobbin M, Tsai LH, et al. Recovery of learning and memory is associated with chromatin remodelling. Nature 2007;447:178-182.
    • (2007) Nature , vol.447 , pp. 178-182
  • 180
    • 52049126629 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors improve learning consolidation in young and in KA-induced-neurodegeneration and SAMP-8-mutant mice
    • Fontán-Lozano A, Romero-Granados R, Troncoso J, Múnera A, Delgado-García JM, Carrión AM. Histone deacetylase inhibitors improve learning consolidation in young and in KA-induced-neurodegeneration and SAMP-8-mutant mice. Mol Cell Neurosci 2008;39:193-201.
    • (2008) Mol Cell Neurosci , vol.39 , pp. 193-201
  • 181
    • 79954628987 scopus 로고    scopus 로고
    • The role of NR4A transcription factors in memory formation
    • COI: 1:CAS:528:DC%2BC3MXkvVKgtb8%3D, PID: 21316423
    • Hawk JD, Abel T. The role of NR4A transcription factors in memory formation. Brain Res Bull 2011;85:21-29.
    • (2011) Brain Res Bull , vol.85 , pp. 21-29
    • Hawk, J.D.1    Abel, T.2
  • 182
    • 79955023405 scopus 로고    scopus 로고
    • Activation and function of immediate-early genes in the nervous system
    • COI: 1:CAS:528:DC%2BC3MXps1Wlurs%3D, PID: 21326363
    • Perez-Cadahia B, Drobic B, Davie JR. Activation and function of immediate-early genes in the nervous system. Biochem Cell Biol 2011;89:61-73.
    • (2011) Biochem Cell Biol , vol.89 , pp. 61-73
    • Perez-Cadahia, B.1    Drobic, B.2    Davie, J.R.3
  • 183
    • 0030055163 scopus 로고    scopus 로고
    • A role for immediate-early transcription factors in learning and memory
    • COI: 1:STN:280:DyaK28zhtFyrtw%3D%3D, PID: 8754252
    • Dragunow M. A role for immediate-early transcription factors in learning and memory. Behav Genet 1996;26:293-299.
    • (1996) Behav Genet , vol.26 , pp. 293-299
    • Dragunow, M.1
  • 184
    • 34250026412 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors enhance memory and synaptic plasticity via CREB:CBP-dependent transcriptional activation
    • Vecsey CG, Hawk JD, Lattal KM, et al. Histone deacetylase inhibitors enhance memory and synaptic plasticity via CREB:CBP-dependent transcriptional activation. J Neurosci 2007;27:6128-6140.
    • (2007) J Neurosci , vol.27 , pp. 6128-6140
  • 185
    • 79958001269 scopus 로고    scopus 로고
    • The role of histone acetylation in age-associated memory impairment and Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC3MXntlGmurw%3D, PID: 21540120
    • Stilling RM, Fischer A. The role of histone acetylation in age-associated memory impairment and Alzheimer's disease. Neurobiol Learn Mem 2011;96:19-26.
    • (2011) Neurobiol Learn Mem , vol.96 , pp. 19-26
    • Stilling, R.M.1    Fischer, A.2
  • 186
    • 67649310030 scopus 로고    scopus 로고
    • Dysregulation of histone acetylation in the APP/PS1 mouse model of Alzheimer's disease
    • Francis YI, Fà M, Ashraf H, et al. Dysregulation of histone acetylation in the APP/PS1 mouse model of Alzheimer's disease. J Alzheimers Dis 2009;18:131-139.
    • (2009) J Alzheimers Dis , vol.18 , pp. 131-139
  • 187
    • 67249137941 scopus 로고    scopus 로고
    • Modulation of long-term memory for object recognition via HDAC inhibition
    • Stefanko DP, Barrett RM, Ly AR, Reolon GK, Wood MA. Modulation of long-term memory for object recognition via HDAC inhibition. Proc Natl Acad Sci U S A 2009;106:9447-9452.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9447-9452
  • 188
    • 67349220155 scopus 로고    scopus 로고
    • Phenylbutyrate ameliorates cognitive deficit and reduces tau pathology in an Alzheimer's disease mouse model
    • Ricobaraza A, Cuadrado-Tejedor M, Pérez-Mediavilla A, Frechilla D, Del Río J, García-Osta A. Phenylbutyrate ameliorates cognitive deficit and reduces tau pathology in an Alzheimer's disease mouse model. Neuropsychopharmacology 2009;34:1721-1732.
    • (2009) Neuropsychopharmacology , vol.34 , pp. 1721-1732
  • 189
    • 34748917182 scopus 로고    scopus 로고
    • Transgenic mice expressing an inhibitory truncated form of p300 exhibit long-term memory deficits
    • Oliveira AM, Wood MA, McDonough CB, Abel T. Transgenic mice expressing an inhibitory truncated form of p300 exhibit long-term memory deficits. Learn Mem 2007;14:564-572.
    • (2007) Learn Mem , vol.14 , pp. 564-572
  • 190
    • 43649104766 scopus 로고    scopus 로고
    • Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice
    • Maurice T, Duclot F, Meunier J, et al. Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice. Neuropsychopharmacology 2008;33:1584-1602.
    • (2008) Neuropsychopharmacology , vol.33 , pp. 1584-1602
  • 191
    • 84865472870 scopus 로고    scopus 로고
    • p300/CBP-associated factor selectively regulates the extinction of conditioned fear
    • Wei W, Coelho CM, Li X, et al. p300/CBP-associated factor selectively regulates the extinction of conditioned fear. J Neurosci 2012;32:11930-11941.
    • (2012) J Neurosci , vol.32 , pp. 11930-11941
  • 192
    • 84879301398 scopus 로고    scopus 로고
    • A novel activator of CBP/p300 acetyltransferases promotes neurogenesis and extends memory duration in adult mice
    • Chatterjee S1, Mizar P, Cassel R, et al. A novel activator of CBP/p300 acetyltransferases promotes neurogenesis and extends memory duration in adult mice. J Neurosci 2013;33:10698-10712.
    • (2013) J Neurosci , vol.33 , pp. 10698-10712
  • 193
    • 0029652085 scopus 로고
    • beta-Amyloid-(1-40) increases long-term potentiation in rat hippocampus in vitro
    • COI: 1:CAS:528:DyaK2MXot1yqsL0%3D, PID: 8666003
    • Wu J, Anwyl R, Rowan MJ. beta-Amyloid-(1-40) increases long-term potentiation in rat hippocampus in vitro. Eur J Pharmacol 1995;284:R1-R3.
    • (1995) Eur J Pharmacol , vol.284 , pp. 1-3
    • Wu, J.1    Anwyl, R.2    Rowan, M.J.3
  • 194
    • 0028558473 scopus 로고
    • beta-Amyloid protein induces platelet aggregation and supports platelet adhesion
    • COI: 1:CAS:528:DyaK2MXivV2ru7g%3D, PID: 7811271
    • Kowalska MA, Badellino K. beta-Amyloid protein induces platelet aggregation and supports platelet adhesion. Biochem Biophys Res Commun 1994;205:1829-1835.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1829-1835
    • Kowalska, M.A.1    Badellino, K.2
  • 195
    • 0344483869 scopus 로고    scopus 로고
    • Secreted form of amyloid precursor protein enhances basal glucose and glutamate transport and protects against oxidative impairment of glucose and glutamate transport in synaptosomes by a cyclic GMP-mediated mechanism
    • COI: 1:CAS:528:DyaK1MXkslOqs74%3D, PID: 10428048
    • Mattson MP, Guo ZH, Geiger JD. Secreted form of amyloid precursor protein enhances basal glucose and glutamate transport and protects against oxidative impairment of glucose and glutamate transport in synaptosomes by a cyclic GMP-mediated mechanism. J Neurochem 1999;73:532-537.
    • (1999) J Neurochem , vol.73 , pp. 532-537
    • Mattson, M.P.1    Guo, Z.H.2    Geiger, J.D.3
  • 196
    • 84861198956 scopus 로고    scopus 로고
    • Hormetic effect of amyloid-beta peptide in synaptic plasticity and memory
    • PID: 22284988, e15–24
    • Puzzo D, Privitera L, Palmeri A. Hormetic effect of amyloid-beta peptide in synaptic plasticity and memory. Neurobiol Aging 2012;33:1484 e15–24.
    • (2012) Neurobiol Aging , vol.33 , pp. 1484
    • Puzzo, D.1    Privitera, L.2    Palmeri, A.3
  • 197
    • 84870548539 scopus 로고    scopus 로고
    • Amyloid-beta peptide: Dr. Jekyll or Mr. Hyde?
    • PID: 22735675
    • Puzzo D, Arancio O. Amyloid-beta peptide: Dr. Jekyll or Mr. Hyde? J Alzheimers Dis 2013;33:(Suppl. 1): S111-S120.
    • (2013) J Alzheimers Dis , vol.33 , pp. 111-120
    • Puzzo, D.1    Arancio, O.2
  • 198
    • 0037312865 scopus 로고    scopus 로고
    • CREB, memory enhancement and the treatment of memory disorders: promises, pitfalls and prospects
    • COI: 1:CAS:528:DC%2BD3sXhsV2ltbs%3D, PID: 12556206
    • Barco A, Pittenger C, Kandel ER. CREB, memory enhancement and the treatment of memory disorders: promises, pitfalls and prospects. Expert Opin Ther Targets 2003;7:101-114.
    • (2003) Expert Opin Ther Targets , vol.7 , pp. 101-114
    • Barco, A.1    Pittenger, C.2    Kandel, E.R.3


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