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Volumn 108, Issue 43, 2011, Pages

Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling

Author keywords

Acetylation; Neuropathy; Sirtuin

Indexed keywords

ATYPICAL PROTEIN KINASE C; MYELIN; PROTEIN KINASE C; PROTEINASE ACTIVATED RECEPTOR 3; SIRTUIN 2; UNCLASSIFIED DRUG;

EID: 80055085172     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1104969108     Document Type: Article
Times cited : (134)

References (61)
  • 1
    • 78149433845 scopus 로고    scopus 로고
    • Myelination and support of axonal integrity by glia
    • Nave KA (2010) Myelination and support of axonal integrity by glia. Nature 468:244-252.
    • (2010) Nature , vol.468 , pp. 244-252
    • Nave, K.A.1
  • 3
    • 77955073094 scopus 로고    scopus 로고
    • Control of Schwann cell myelination
    • Jessen KR, Mirsky R (2010) Control of Schwann cell myelination. F1000 Biol Rep 2:19.
    • (2010) F1000 Biol Rep , vol.2 , pp. 19
    • Jessen, K.R.1    Mirsky, R.2
  • 4
    • 24944438343 scopus 로고    scopus 로고
    • Nab proteins are essential for peripheral nervous system myelination
    • Le N, et al. (2005) Nab proteins are essential for peripheral nervous system myelination. Nat Neurosci 8:932-940.
    • (2005) Nat Neurosci , vol.8 , pp. 932-940
    • Le, N.1
  • 5
    • 0024437196 scopus 로고
    • Impaired nerve regeneration in streptozotocin-diabetic rats. Effects of treatment with an aldose reductase inhibitor
    • Ekström AR, Tomlinson DR (1989) Impaired nerve regeneration in streptozotocin-diabetic rats. Effects of treatment with an aldose reductase inhibitor. J Neurol Sci 93:231-237.
    • (1989) J Neurol Sci , vol.93 , pp. 231-237
    • Ekström, A.R.1    Tomlinson, D.R.2
  • 6
    • 22144470885 scopus 로고    scopus 로고
    • Impaired peripheral nerve regeneration in diabetes mellitus
    • DOI 10.1111/j.1085-9489.2005.0010205.x
    • Kennedy JM, Zochodne DW (2005) Impaired peripheral nerve regeneration in diabetes mellitus. J Peripher Nerv Syst 10:144-157. (Pubitemid 40984889)
    • (2005) Journal of the Peripheral Nervous System , vol.10 , Issue.2 , pp. 144-157
    • Kennedy, J.M.1    Zochodne, D.W.2
  • 7
    • 0016607090 scopus 로고
    • Peripheral nerve regeneration in experimental diabetes
    • Sharma AK, Thomas PK (1975) Peripheral nerve regeneration in experimental diabetes. J Neurol Sci 24:417-424.
    • (1975) J Neurol Sci , vol.24 , pp. 417-424
    • Sharma, A.K.1    Thomas, P.K.2
  • 8
    • 0032601004 scopus 로고    scopus 로고
    • Nerve regeneration in diabetic neuropathy
    • Apfel SC (1999) Nerve regeneration in diabetic neuropathy. Diabetes Obes Metab 1:3-11.
    • (1999) Diabetes Obes Metab , vol.1 , pp. 3-11
    • Apfel, S.C.1
  • 9
    • 62149126997 scopus 로고    scopus 로고
    • Intermittent fasting alleviates the neuropathic phenotype in a mouse model of Charcot-Marie-Tooth disease
    • Madorsky I, et al. (2009) Intermittent fasting alleviates the neuropathic phenotype in a mouse model of Charcot-Marie-Tooth disease. Neurobiol Dis 34:146-154.
    • (2009) Neurobiol Dis , vol.34 , pp. 146-154
    • Madorsky, I.1
  • 10
    • 63549138319 scopus 로고    scopus 로고
    • Molecular architecture of myelinated peripheral nerves is supported by calorie restriction with aging
    • Rangaraju S, et al. (2009) Molecular architecture of myelinated peripheral nerves is supported by calorie restriction with aging. Aging Cell 8:178-191.
    • (2009) Aging Cell , vol.8 , pp. 178-191
    • Rangaraju, S.1
  • 12
    • 34547413569 scopus 로고    scopus 로고
    • Sirtuin functions in health and disease
    • DOI 10.1210/me.2007-0079
    • Yamamoto H, Schoonjans K, Auwerx J (2007) Sirtuin functions in health and disease. Mol Endocrinol 21:1745-1755. (Pubitemid 47173788)
    • (2007) Molecular Endocrinology , vol.21 , Issue.8 , pp. 1745-1755
    • Yamamoto, H.1    Schoonjans, K.2    Auwerx, J.3
  • 13
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis MC, Sinclair DA (2010) Mammalian sirtuins: Biological insights and disease relevance. Annu Rev Pathol 5:253-295.
    • (2010) Annu Rev Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 14
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11:437-444. (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 15
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin
    • DOI 10.1523/JNEUROSCI.4181-06.2007
    • Li W, et al. (2007) Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin. J Neurosci 27:2606-2616. (Pubitemid 46393594)
    • (2007) Journal of Neuroscience , vol.27 , Issue.10 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6    Guo, J.7    Ling, E.-A.8    Liang, F.9
  • 16
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • DOI 10.1128/MCB.23.9.3173-3185.2003
    • Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 23:3173-3185. (Pubitemid 36459231)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.9 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.-S.4    Tainsky, M.A.5
  • 17
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
    • DOI 10.1016/j.cmet.2007.07.003, PII S155041310700191X
    • Jing E, Gesta S, Kahn CR (2007) SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab 6:105-114. (Pubitemid 47163621)
    • (2007) Cell Metabolism , vol.6 , Issue.2 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 20
    • 77950905065 scopus 로고    scopus 로고
    • Gelsolin is required for macrophage recruitment during remyelination of the peripheral nervous system
    • Gonçalves AF, et al. (2010) Gelsolin is required for macrophage recruitment during remyelination of the peripheral nervous system. Glia 58:706-715.
    • (2010) Glia , vol.58 , pp. 706-715
    • Gonçalves, A.F.1
  • 21
    • 33645102369 scopus 로고    scopus 로고
    • Knockout of p75(NTR) impairs remyelination of injured sciatic nerve in mice
    • Song XY, Zhou FH, Zhong JH, Wu LL, Zhou XF (2006) Knockout of p75(NTR) impairs remyelination of injured sciatic nerve in mice. J Neurochem 96:833-842.
    • (2006) J Neurochem , vol.96 , pp. 833-842
    • Song, X.Y.1    Zhou, F.H.2    Zhong, J.H.3    Wu, L.L.4    Zhou, X.F.5
  • 24
    • 77949755601 scopus 로고    scopus 로고
    • Pals1 is a major regulator of the epithelial-like polarization and the extension of the myelin sheath in peripheral nerves
    • Ozçelik M, et al. (2010) Pals1 is a major regulator of the epithelial-like polarization and the extension of the myelin sheath in peripheral nerves. J Neurosci 30:4120-4131.
    • (2010) J Neurosci , vol.30 , pp. 4120-4131
    • Ozçelik, M.1
  • 25
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang W, et al. (2011) Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol Cell 43:33-44.
    • (2011) Mol Cell , vol.43 , pp. 33-44
    • Jiang, W.1
  • 26
    • 77954225200 scopus 로고    scopus 로고
    • Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity
    • Zhao Y, et al. (2010) Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity. Nat Cell Biol 12:665-675.
    • (2010) Nat Cell Biol , vol.12 , pp. 665-675
    • Zhao, Y.1
  • 27
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty G, Petersen C, Gao L, Macara IG (2000) The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol 2:531-539.
    • (2000) Nat Cell Biol , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 28
    • 0035479930 scopus 로고    scopus 로고
    • Intercellular junctions and cellular polarity: The PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity
    • Ohno S (2001) Intercellular junctions and cellular polarity: The PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity. Curr Opin Cell Biol 13:641-648.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 641-648
    • Ohno, S.1
  • 29
    • 1542374119 scopus 로고    scopus 로고
    • Parsing the polarity code
    • Macara IG (2004) Parsing the polarity code. Nat Rev Mol Cell Biol 5:220-231.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 220-231
    • Macara, I.G.1
  • 30
    • 0642376906 scopus 로고    scopus 로고
    • Protein kinase Czeta (PKCzeta): Activation mechanisms and cellular functions
    • DOI 10.1093/jb/mvg017
    • Hirai T, Chida K (2003) Protein kinase Czeta (PKCzeta): Activation mechanisms and cellular functions. J Biochem 133:1-7. (Pubitemid 36240972)
    • (2003) Journal of Biochemistry , vol.133 , Issue.1 , pp. 1-7
    • Hirai, T.1    Chida, K.2
  • 31
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
    • Lin D, et al. (2000) A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity. Nat Cell Biol 2:540-547.
    • (2000) Nat Cell Biol , vol.2 , pp. 540-547
    • Lin, D.1
  • 32
    • 0037222950 scopus 로고    scopus 로고
    • Cell polarity: Par6, aPKC and cytoskeletal crosstalk
    • DOI 10.1016/S0955-0674(02)00005-4
    • Etienne-Manneville S, Hall A (2003) Cell polarity: Par6, aPKC and cytoskeletal crosstalk. Curr Opin Cell Biol 15:67-72. (Pubitemid 36044717)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.1 , pp. 67-72
    • Etienne-Manneville, S.1    Hall, A.2
  • 33
    • 67449114979 scopus 로고    scopus 로고
    • Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells
    • Horikoshi Y, et al. (2009) Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells. J Cell Sci 122:1595-1606.
    • (2009) J Cell Sci , vol.122 , pp. 1595-1606
    • Horikoshi, Y.1
  • 35
    • 0025639901 scopus 로고
    • Studies of the initiation of myelination by Schwann cells
    • Wood P, et al. (1990) Studies of the initiation of myelination by Schwann cells. Ann N Y Acad Sci 605:1-14.
    • (1990) Ann N Y Acad Sci , vol.605 , pp. 1-14
    • Wood, P.1
  • 36
    • 0026036698 scopus 로고
    • Schwann cell precursors and their development
    • Jessen KR, Mirsky R (1991) Schwann cell precursors and their development. Glia 4:185-194.
    • (1991) Glia , vol.4 , pp. 185-194
    • Jessen, K.R.1    Mirsky, R.2
  • 37
    • 34548389859 scopus 로고    scopus 로고
    • Protein kinase Czeta and glycogen synthase kinase-3beta control neuronal polarity in developing rodent enteric neurons, whereas SMAD specific E3 ubiquitin protein ligase 1 promotes neurite growth but does not influence polarity
    • DOI 10.1523/JNEUROSCI.0870-07.2007
    • Vohra BP, Fu M, Heuckeroth RO (2007) Protein kinase Czeta and glycogen synthase kinase-3beta control neuronal polarity in developing rodent enteric neurons, whereas SMAD specific E3 ubiquitin protein ligase 1 promotes neurite growth but does not influence polarity. J Neurosci 27:9458-9468. (Pubitemid 47358201)
    • (2007) Journal of Neuroscience , vol.27 , Issue.35 , pp. 9458-9468
    • Vohra, B.P.S.1    Fu, M.2    Heuckeroth, R.O.3
  • 38
    • 25144470229 scopus 로고    scopus 로고
    • The origin and development of glial cells in peripheral nerves
    • DOI 10.1038/nrn1746, PII NRN1746
    • Jessen KR, Mirsky R (2005) The origin and development of glial cells in peripheral nerves. Nat Rev Neurosci 6:671-682. (Pubitemid 43160316)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.9 , pp. 671-682
    • Jessen, K.R.1    Mirsky, R.2
  • 39
    • 77149172855 scopus 로고    scopus 로고
    • SIRT2-mediated protein deacetylation: An emerging key regulator in brain physiology and pathology
    • Harting K, Knöll B (2010) SIRT2-mediated protein deacetylation: An emerging key regulator in brain physiology and pathology. Eur J Cell Biol 89:262-269.
    • (2010) Eur J Cell Biol , vol.89 , pp. 262-269
    • Harting, K.1    Knöll, B.2
  • 40
    • 56249139409 scopus 로고    scopus 로고
    • Polarity proteins in glial cell functions
    • Etienne-Manneville S (2008) Polarity proteins in glial cell functions. Curr Opin Neurobiol 18:488-494.
    • (2008) Curr Opin Neurobiol , vol.18 , pp. 488-494
    • Etienne-Manneville, S.1
  • 41
    • 77953562076 scopus 로고    scopus 로고
    • Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination
    • Cotter L, et al. (2010) Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328:1415-1418.
    • (2010) Science , vol.328 , pp. 1415-1418
    • Cotter, L.1
  • 42
    • 79751524086 scopus 로고    scopus 로고
    • Both Schwann cell and axonal defects cause motor peripheral neuropathy in Ebf2-/- mice
    • Giacomini C, et al. (2011) Both Schwann cell and axonal defects cause motor peripheral neuropathy in Ebf2-/- mice. Neurobiol Dis 42:73-84.
    • (2011) Neurobiol Dis , vol.42 , pp. 73-84
    • Giacomini, C.1
  • 44
    • 78650398190 scopus 로고    scopus 로고
    • Atypical protein kinase C regulates primary dendrite specification of cerebellar Purkinje cells by localizing Golgi apparatus
    • Tanabe K, et al. (2010) Atypical protein kinase C regulates primary dendrite specification of cerebellar Purkinje cells by localizing Golgi apparatus. J Neurosci 30:16983-16992.
    • (2010) J Neurosci , vol.30 , pp. 16983-16992
    • Tanabe, K.1
  • 45
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: Lessons in polarity
    • Suzuki A, Ohno S (2006) The PAR-aPKC system: Lessons in polarity. J Cell Sci 119:979-987.
    • (2006) J Cell Sci , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 46
    • 0037434790 scopus 로고    scopus 로고
    • Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity
    • DOI 10.1038/nature01423
    • Etienne-Manneville S, Hall A (2003) Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity. Nature 421:753-756. (Pubitemid 36227627)
    • (2003) Nature , vol.421 , Issue.6924 , pp. 753-756
    • Etienne-Manneville, S.1    Hall, A.2
  • 49
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependent SIR2 family deacetylases: Implications for metabolic diseases
    • Imai S, Guarente L (2010) Ten years of NAD-dependent SIR2 family deacetylases: Implications for metabolic diseases. Trends Pharmacol Sci 31:212-220.
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 50
    • 34547681377 scopus 로고    scopus 로고
    • Diabetes mellitus and the peripheral nervous system: Manifestations and mechanisms
    • Zochodne DW (2007) Diabetes mellitus and the peripheral nervous system: Manifestations and mechanisms. Muscle Nerve 36:144-166.
    • (2007) Muscle Nerve , vol.36 , pp. 144-166
    • Zochodne, D.W.1
  • 51
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327:1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1
  • 52
    • 77952413052 scopus 로고    scopus 로고
    • SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis
    • Luthi-Carter R, et al. (2010) SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis. Proc Natl Acad Sci USA 107:7927-7932.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7927-7932
    • Luthi-Carter, R.1
  • 53
    • 0034981923 scopus 로고    scopus 로고
    • EGR2 mutations in inherited neuropathies dominant-negatively inhibit myelin gene expression
    • DOI 10.1016/S0896-6273(01)00282-3
    • Nagarajan R, et al. (2001) EGR2 mutations in inherited neuropathies dominant-negatively inhibit myelin gene expression. Neuron 30:355-368. (Pubitemid 32530581)
    • (2001) Neuron , vol.30 , Issue.2 , pp. 355-368
    • Nagarajan, R.1    Svaren, J.2    Le, N.3    Araki, T.4    Watson, M.5    Milbrandt, J.6
  • 54
    • 44849096876 scopus 로고    scopus 로고
    • The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth
    • Firestein R, et al. (2008) The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS ONE 3:e2020.
    • (2008) PLoS ONE , vol.3
    • Firestein, R.1
  • 55
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • DOI 10.1126/science.1098014
    • Araki T, Sasaki Y, Milbrandt J (2004) Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305:1010-1013. (Pubitemid 39071777)
    • (2004) Science , vol.305 , Issue.5686 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 56
    • 34547490707 scopus 로고    scopus 로고
    • Deciphering adaptor specificity in GFL-dependent RET-mediated proliferation and neurite outgrowth
    • DOI 10.1111/j.1471-4159.2007.04624.x
    • Gustin JA, Yang M, Johnson EM, Jr., Milbrandt J (2007) Deciphering adaptor specificity in GFL-dependent RET-mediated proliferation and neurite outgrowth. J Neurochem 102:1184-1194. (Pubitemid 47174234)
    • (2007) Journal of Neurochemistry , vol.102 , Issue.4 , pp. 1184-1194
    • Gustin, J.A.1    Yang, M.2    Johnson Jr., E.M.3    Milbrandt, J.4
  • 57
    • 0034022271 scopus 로고    scopus 로고
    • FK506 promotes functional recovery in crushed rat sciatic nerve
    • DOI 10.1002/(SICI)1097-4598(200004)23:4<633::AID-MUS24>3.0.CO;2-Q
    • Lee M, Doolabh VB, Mackinnon SE, Jost S (2000) FK506 promotes functional recovery in crushed rat sciatic nerve. Muscle Nerve 23:633-640. (Pubitemid 30164791)
    • (2000) Muscle and Nerve , vol.23 , Issue.4 , pp. 633-640
    • Lee, M.1    Doolabh, V.B.2    Mackinnon, S.E.3    Jost, S.4
  • 58
    • 77954413871 scopus 로고    scopus 로고
    • The differential effects of pathway- Versus target-derived glial cell line-derived neurotrophic factor on peripheral nerve regeneration
    • Magill CK, et al. (2010) The differential effects of pathway- versus target-derived glial cell line-derived neurotrophic factor on peripheral nerve regeneration. J Neurosurg 113:102-109.
    • (2010) J Neurosurg , vol.113 , pp. 102-109
    • Magill, C.K.1
  • 59
    • 50549088550 scopus 로고    scopus 로고
    • Analysis of peripheral nerve expression profiles identifies a novel myelin glycoprotein, MP11
    • Ryu EJ, et al. (2008) Analysis of peripheral nerve expression profiles identifies a novel myelin glycoprotein, MP11. J Neurosci 28:7563-7573.
    • (2008) J Neurosci , vol.28 , pp. 7563-7573
    • Ryu, E.J.1
  • 60
    • 23944452336 scopus 로고    scopus 로고
    • Preparation of enzymatically active recombinant class III protein deacetylases
    • DOI 10.1016/j.ymeth.2005.03.004, PII S1046202305000721, Protein Acetylation
    • North BJ, Schwer B, Ahuja N, Marshall B, Verdin E (2005) Preparation of enzymatically active recombinant class III protein deacetylases. Methods 36:338-345. (Pubitemid 41188064)
    • (2005) Methods , vol.36 , Issue.4 , pp. 338-345
    • North, B.J.1    Schwer, B.2    Ahuja, N.3    Marshall, B.4    Verdin, E.5


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