메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages

An Intracellular Threonine of Amyloid-β Precursor Protein Mediates Synaptic Plasticity Deficits and Memory Loss

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; THREONINE;

EID: 84874339639     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0057120     Document Type: Article
Times cited : (22)

References (43)
  • 1
    • 77957927865 scopus 로고    scopus 로고
    • The genetics of Alzheimer disease: back to the future
    • Bertram L, Lill CM, Tanzi RE, (2010) The genetics of Alzheimer disease: back to the future. Neuron 68: 270-281.
    • (2010) Neuron , vol.68 , pp. 270-281
    • Bertram, L.1    Lill, C.M.2    Tanzi, R.E.3
  • 2
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal R, Frangione B, Rostagno A, Mead S, Revesz T, et al. (1999) A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 399: 776-781.
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Revesz, T.5
  • 3
    • 13844255273 scopus 로고    scopus 로고
    • Molecular biology and genetics of Alzheimer's disease
    • St George-Hyslop PH, Petit A, (2005) Molecular biology and genetics of Alzheimer's disease. C R Biol 328: 119-130.
    • (2005) C R Biol , vol.328 , pp. 119-130
    • St George-Hyslop, P.H.1    Petit, A.2
  • 4
    • 23844491144 scopus 로고    scopus 로고
    • The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production
    • Matsuda S, Giliberto L, Matsuda Y, Davies P, McGowan E, et al. (2005) The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production. J Biol Chem 280: 28912-28916.
    • (2005) J Biol Chem , vol.280 , pp. 28912-28916
    • Matsuda, S.1    Giliberto, L.2    Matsuda, Y.3    Davies, P.4    McGowan, E.5
  • 5
    • 24744440136 scopus 로고    scopus 로고
    • BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid beta (Abeta) production
    • Fotinopoulou A, Tsachaki M, Vlavaki M, Poulopoulos A, Rostagno A, et al. (2005) BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid beta (Abeta) production. J Biol Chem 280: 30768-30772.
    • (2005) J Biol Chem , vol.280 , pp. 30768-30772
    • Fotinopoulou, A.1    Tsachaki, M.2    Vlavaki, M.3    Poulopoulos, A.4    Rostagno, A.5
  • 6
    • 79959586503 scopus 로고    scopus 로고
    • Maturation of BRI2 generates a specific inhibitor that reduces APP processing at the plasma membrane and in endocytic vesicles
    • Matsuda S, Matsuda Y, Snapp EL, D'Adamio L, (2011) Maturation of BRI2 generates a specific inhibitor that reduces APP processing at the plasma membrane and in endocytic vesicles. Neurobiol Aging 32: 1400-1408.
    • (2011) Neurobiol Aging , vol.32 , pp. 1400-1408
    • Matsuda, S.1    Matsuda, Y.2    Snapp, E.L.3    D'Adamio, L.4
  • 7
    • 52049089901 scopus 로고    scopus 로고
    • BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate
    • Matsuda S, Giliberto L, Matsuda Y, McGowan EM, D'Adamio L, (2008) BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate. J Neurosci 28: 8668-8676.
    • (2008) J Neurosci , vol.28 , pp. 8668-8676
    • Matsuda, S.1    Giliberto, L.2    Matsuda, Y.3    McGowan, E.M.4    D'Adamio, L.5
  • 8
    • 0034712749 scopus 로고    scopus 로고
    • A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred
    • Vidal R, Revesz T, Rostagno A, Kim E, Holton JL, et al. (2000) A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred. Proc Natl Acad Sci U S A 97: 4920-4925.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4920-4925
    • Vidal, R.1    Revesz, T.2    Rostagno, A.3    Kim, E.4    Holton, J.L.5
  • 9
    • 84856956771 scopus 로고    scopus 로고
    • Probing sporadic and familial Alzheimer's disease using induced pluripotent stem cells
    • Israel MA, Yuan SH, Bardy C, Reyna SM, Mu Y, et al. (2012) Probing sporadic and familial Alzheimer's disease using induced pluripotent stem cells. Nature 482: 216-220.
    • (2012) Nature , vol.482 , pp. 216-220
    • Israel, M.A.1    Yuan, S.H.2    Bardy, C.3    Reyna, S.M.4    Mu, Y.5
  • 10
    • 84858123000 scopus 로고    scopus 로고
    • beta- but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
    • Tamayev R, Matsuda S, Arancio O, D'Adamio L, (2012) beta- but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia. EMBO Mol Med 4: 171-179.
    • (2012) EMBO Mol Med , vol.4 , pp. 171-179
    • Tamayev, R.1    Matsuda, S.2    Arancio, O.3    D'Adamio, L.4
  • 12
    • 70849110420 scopus 로고    scopus 로고
    • Generation and Initial Characterization of FDD Knock In Mice
    • Giliberto L, Matsuda S, Vidal R, D'Adamio L, (2009) Generation and Initial Characterization of FDD Knock In Mice. PLoS One 4: e7900.
    • (2009) PLoS One , vol.4
    • Giliberto, L.1    Matsuda, S.2    Vidal, R.3    D'Adamio, L.4
  • 13
    • 78049506839 scopus 로고    scopus 로고
    • Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits
    • Tamayev R, Matsuda S, Fa M, Arancio O, D'Adamio L, (2010) Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits. Proc Natl Acad Sci U S A 107: 20822-20827.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20822-20827
    • Tamayev, R.1    Matsuda, S.2    Fa, M.3    Arancio, O.4    D'Adamio, L.5
  • 14
    • 79958785727 scopus 로고    scopus 로고
    • APP heterozygosity averts memory deficit in knockin mice expressing the Danish dementia BRI2 mutant
    • Tamayev R, Matsuda S, Giliberto L, Arancio O, D'Adamio L, (2011) APP heterozygosity averts memory deficit in knockin mice expressing the Danish dementia BRI2 mutant. EMBO J 30: 2501-2509.
    • (2011) EMBO J , vol.30 , pp. 2501-2509
    • Tamayev, R.1    Matsuda, S.2    Giliberto, L.3    Arancio, O.4    D'Adamio, L.5
  • 15
    • 81855199751 scopus 로고    scopus 로고
    • Increased AbetaPP processing in familial Danish dementia patients
    • Matsuda S, Tamayev R, D'Adamio L, (2011) Increased AbetaPP processing in familial Danish dementia patients. J Alzheimers Dis 27: 385-391.
    • (2011) J Alzheimers Dis , vol.27 , pp. 385-391
    • Matsuda, S.1    Tamayev, R.2    D'Adamio, L.3
  • 16
    • 84885836460 scopus 로고    scopus 로고
    • beta - but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
    • Tamayev R, Matsuda S, D'Adamio L, (2012) beta- but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia. Mol Neurodegener 7Suppl 1: L9.
    • (2012) Mol Neurodegener , vol.7
    • Tamayev, R.1    Matsuda, S.2    D'Adamio, L.3
  • 17
    • 84862161020 scopus 로고    scopus 로고
    • Inhibition of gamma-secretase worsens memory deficits in a genetically congruous mouse model of Danish dementia
    • Tamayev R, D'Adamio L, (2012) Inhibition of gamma-secretase worsens memory deficits in a genetically congruous mouse model of Danish dementia. Mol Neurodegener 7: 19.
    • (2012) Mol Neurodegener , vol.7 , pp. 19
    • Tamayev, R.1    D'Adamio, L.2
  • 18
    • 84872324395 scopus 로고    scopus 로고
    • Caspase-9 mediates synaptic plasticity and memory deficits of Danish dementia knock-in mice: caspase-9 inhibition provides therapeutic protection
    • Tamayev R, Akpan N, Arancio O, Troy CM, L DA, (2012) Caspase-9 mediates synaptic plasticity and memory deficits of Danish dementia knock-in mice: caspase-9 inhibition provides therapeutic protection. Mol Neurodegener 7: 60.
    • (2012) Mol Neurodegener , vol.7 , pp. 60
    • Tamayev, R.1    Akpan, N.2    Arancio, O.3    Troy, C.M.L.D.A.4
  • 19
    • 0142211267 scopus 로고    scopus 로고
    • Amyloid beta protein precursor is phosphorylated by JNK-1 independent of, yet facilitated by, JNK-interacting protein (JIP)-1
    • Scheinfeld MH, Ghersi E, Davies P, D'Adamio L, (2003) Amyloid beta protein precursor is phosphorylated by JNK-1 independent of, yet facilitated by, JNK-interacting protein (JIP)-1. J Biol Chem 278: 42058-42063.
    • (2003) J Biol Chem , vol.278 , pp. 42058-42063
    • Scheinfeld, M.H.1    Ghersi, E.2    Davies, P.3    D'Adamio, L.4
  • 20
    • 0035955712 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid
    • Ando K, Iijima KI, Elliott JI, Kirino Y, Suzuki T, (2001) Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid. J Biol Chem 276: 40353-40361.
    • (2001) J Biol Chem , vol.276 , pp. 40353-40361
    • Ando, K.1    Iijima, K.I.2    Elliott, J.I.3    Kirino, Y.4    Suzuki, T.5
  • 21
    • 69049118186 scopus 로고    scopus 로고
    • The interactome of the Amyloid betaeta Precursor Protein family members is shaped by phosphorylation of their intracellular domains
    • Tamayev R, Zhou D, D'Adamio L, (2009) The interactome of the Amyloid betaeta Precursor Protein family members is shaped by phosphorylation of their intracellular domains. Mol Neurodegener 4: 28.
    • (2009) Mol Neurodegener , vol.4 , pp. 28
    • Tamayev, R.1    Zhou, D.2    D'Adamio, L.3
  • 22
    • 33947140574 scopus 로고    scopus 로고
    • Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism?
    • Balastik M, Lim J, Pastorino L, Lu KP, (2007) Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism? Biochim Biophys Acta 1772: 422-429.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 422-429
    • Balastik, M.1    Lim, J.2    Pastorino, L.3    Lu, K.P.4
  • 23
    • 34249880509 scopus 로고    scopus 로고
    • Amyloid precursor protein cytoplasmic domain with phospho-Thr668 accumulates in Alzheimer's disease and its transgenic models: a role to mediate interaction of Abeta and tau
    • Shin RW, Ogino K, Shimabuku A, Taki T, Nakashima H, et al. (2007) Amyloid precursor protein cytoplasmic domain with phospho-Thr668 accumulates in Alzheimer's disease and its transgenic models: a role to mediate interaction of Abeta and tau. Acta Neuropathol 113: 627-636.
    • (2007) Acta Neuropathol , vol.113 , pp. 627-636
    • Shin, R.W.1    Ogino, K.2    Shimabuku, A.3    Taki, T.4    Nakashima, H.5
  • 24
    • 79952952445 scopus 로고    scopus 로고
    • The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function
    • Barbagallo AP, Wang Z, Zheng H, D'Adamio L, (2011) The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function. PLoS One 6: e18006.
    • (2011) PLoS One , vol.6
    • Barbagallo, A.P.1    Wang, Z.2    Zheng, H.3    D'Adamio, L.4
  • 25
    • 0032737316 scopus 로고    scopus 로고
    • Exposing rats to a predator impairs spatial working memory in the radial arm water maze
    • Diamond DM, Park CR, Heman KL, Rose GM, (1999) Exposing rats to a predator impairs spatial working memory in the radial arm water maze. Hippocampus 9: 542-552.
    • (1999) Hippocampus , vol.9 , pp. 542-552
    • Diamond, D.M.1    Park, C.R.2    Heman, K.L.3    Rose, G.M.4
  • 26
    • 84861719008 scopus 로고    scopus 로고
    • Membrane-microdomain localization of amyloid beta-precursor protein (APP) C-terminal fragments is regulated by phosphorylation of the cytoplasmic Thr668 residue
    • Matsushima T, Saito Y, Elliott JI, Iijima-Ando K, Nishimura M, et al. (2012) Membrane-microdomain localization of amyloid beta-precursor protein (APP) C-terminal fragments is regulated by phosphorylation of the cytoplasmic Thr668 residue. J Biol Chem 287: 19715-19724.
    • (2012) J Biol Chem , vol.287 , pp. 19715-19724
    • Matsushima, T.1    Saito, Y.2    Elliott, J.I.3    Iijima-Ando, K.4    Nishimura, M.5
  • 27
    • 33645300736 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production
    • Pastorino L, Sun A, Lu PJ, Zhou XZ, Balastik M, et al. (2006) The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440: 528-534.
    • (2006) Nature , vol.440 , pp. 528-534
    • Pastorino, L.1    Sun, A.2    Lu, P.J.3    Zhou, X.Z.4    Balastik, M.5
  • 28
    • 33749073965 scopus 로고    scopus 로고
    • Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP
    • Sano Y, Nakaya T, Pedrini S, Takeda S, Iijima-Ando K, et al. (2006) Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP. PLoS ONE 1: e51.
    • (2006) PLoS ONE , vol.1
    • Sano, Y.1    Nakaya, T.2    Pedrini, S.3    Takeda, S.4    Iijima-Ando, K.5
  • 29
    • 78649496201 scopus 로고    scopus 로고
    • Tyr682 in the Intracellular Domain of APP Regulates Amyloidogenic APP Processing In Vivo
    • Barbagallo AP, Weldon R, Tamayev R, Zhou D, Giliberto L, et al. (2010) Tyr682 in the Intracellular Domain of APP Regulates Amyloidogenic APP Processing In Vivo. PLoS One 5: e15503.
    • (2010) PLoS One , vol.5
    • Barbagallo, A.P.1    Weldon, R.2    Tamayev, R.3    Zhou, D.4    Giliberto, L.5
  • 30
  • 31
    • 0037452773 scopus 로고    scopus 로고
    • JNK-interacting protein-1 promotes transcription of A beta protein precursor but not A beta precursor-like proteins, mechanistically different than Fe65
    • Scheinfeld MH, Matsuda S, D'Adamio L, (2003) JNK-interacting protein-1 promotes transcription of A beta protein precursor but not A beta precursor-like proteins, mechanistically different than Fe65. Proc Natl Acad Sci U S A 100: 1729-1734.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 1729-1734
    • Scheinfeld, M.H.1    Matsuda, S.2    D'Adamio, L.3
  • 32
    • 0036462590 scopus 로고    scopus 로고
    • Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP)
    • Scheinfeld MH, Roncarati R, Vito P, Lopez PA, Abdallah M, et al. (2002) Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP). J Biol Chem 277: 3767-3775.
    • (2002) J Biol Chem , vol.277 , pp. 3767-3775
    • Scheinfeld, M.H.1    Roncarati, R.2    Vito, P.3    Lopez, P.A.4    Abdallah, M.5
  • 33
    • 0037076398 scopus 로고    scopus 로고
    • The gamma-secretase-generated intracellular domain of beta-amyloid precursor protein binds Numb and inhibits Notch signaling
    • Roncarati R, Sestan N, Scheinfeld MH, Berechid BE, Lopez PA, et al. (2002) The gamma-secretase-generated intracellular domain of beta-amyloid precursor protein binds Numb and inhibits Notch signaling. Proc Natl Acad Sci U S A 99: 7102-7107.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7102-7107
    • Roncarati, R.1    Sestan, N.2    Scheinfeld, M.H.3    Berechid, B.E.4    Lopez, P.A.5
  • 34
    • 0141532147 scopus 로고    scopus 로고
    • Amyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1
    • Matsuda S, Matsuda Y, D'Adamio L, (2003) Amyloid beta protein precursor (AbetaPP), but not AbetaPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1. J Biol Chem 278: 38601-38606.
    • (2003) J Biol Chem , vol.278 , pp. 38601-38606
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 35
    • 31644451099 scopus 로고    scopus 로고
    • Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease
    • D'Ambrosio C, Arena S, Fulcoli G, Scheinfeld MH, Zhou D, et al. (2006) Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease. Mol Cell Proteomics 5: 97-113.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 97-113
    • D'Ambrosio, C.1    Arena, S.2    Fulcoli, G.3    Scheinfeld, M.H.4    Zhou, D.5
  • 36
    • 2942586693 scopus 로고    scopus 로고
    • Growth factor receptor-bound protein 2 interaction with the tyrosine-phosphorylated tail of amyloid beta precursor protein is mediated by its Src homology 2 domain
    • Zhou D, Noviello C, D'Ambrosio C, Scaloni A, D'Adamio L, (2004) Growth factor receptor-bound protein 2 interaction with the tyrosine-phosphorylated tail of amyloid beta precursor protein is mediated by its Src homology 2 domain. J Biol Chem 279: 25374-25380.
    • (2004) J Biol Chem , vol.279 , pp. 25374-25380
    • Zhou, D.1    Noviello, C.2    D'Ambrosio, C.3    Scaloni, A.4    D'Adamio, L.5
  • 37
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • Tarr PE, Roncarati R, Pelicci G, Pelicci PG, D'Adamio L, (2002) Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J Biol Chem 277: 16798-16804.
    • (2002) J Biol Chem , vol.277 , pp. 16798-16804
    • Tarr, P.E.1    Roncarati, R.2    Pelicci, G.3    Pelicci, P.G.4    D'Adamio, L.5
  • 38
    • 0037144497 scopus 로고    scopus 로고
    • Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain
    • Russo C, Dolcini V, Salis S, Venezia V, Zambrano N, et al. (2002) Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain. J Biol Chem 277: 35282-35288.
    • (2002) J Biol Chem , vol.277 , pp. 35282-35288
    • Russo, C.1    Dolcini, V.2    Salis, S.3    Venezia, V.4    Zambrano, N.5
  • 39
    • 69049118186 scopus 로고    scopus 로고
    • The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains
    • Tamayev R, Zhou D, D'Adamio L, (2009) The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains. Mol Neurodegener 4: 28.
    • (2009) Mol Neurodegener , vol.4 , pp. 28
    • Tamayev, R.1    Zhou, D.2    D'Adamio, L.3
  • 40
    • 60349103104 scopus 로고    scopus 로고
    • Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling
    • Zhou D, Zambrano N, Russo T, D'Adamio L, (2009) Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling. J Alzheimers Dis 16: 301-307.
    • (2009) J Alzheimers Dis , vol.16 , pp. 301-307
    • Zhou, D.1    Zambrano, N.2    Russo, T.3    D'Adamio, L.4
  • 41
    • 84869164516 scopus 로고    scopus 로고
    • Tyr682 in the Abeta-precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance
    • Matrone C, Luvisetto S, La Rosa LR, Tamayev R, Pignataro A, et al. (2012) Tyr682 in the Abeta-precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance. Aging Cell 11: 1084-1093.
    • (2012) Aging Cell , vol.11 , pp. 1084-1093
    • Matrone, C.1    Luvisetto, S.2    La Rosa, L.R.3    Tamayev, R.4    Pignataro, A.5
  • 42
    • 78649496201 scopus 로고    scopus 로고
    • Tyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing in vivo
    • Barbagallo AP, Weldon R, Tamayev R, Zhou D, Giliberto L, et al. (2010) Tyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing in vivo. PLoS One 5: e15503.
    • (2010) PLoS One , vol.5
    • Barbagallo, A.P.1    Weldon, R.2    Tamayev, R.3    Zhou, D.4    Giliberto, L.5
  • 43
    • 34347215149 scopus 로고    scopus 로고
    • Object recognition in rats and mice: a one-trial non-matching-to-sample learning task to study 'recognition memory
    • Bevins RA, Besheer J, (2006) Object recognition in rats and mice: a one-trial non-matching-to-sample learning task to study 'recognition memory'. Nat Protoc 1: 1306-1311.
    • (2006) Nat Protoc , vol.1 , pp. 1306-1311
    • Bevins, R.A.1    Besheer, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.