메뉴 건너뛰기




Volumn 5, Issue 1, 2010, Pages

NO signaling and S-nitrosylation regulate PTEN inhibition in neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN PEROXIDE; NITRIC OXIDE; PHOSPHATIDATE PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEASOME; PROTEIN KINASE B; S NITROSOCYSTEINE; UBIQUITIN PROTEIN LIGASE NEDD4;

EID: 78149253527     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-5-49     Document Type: Article
Times cited : (127)

References (51)
  • 2
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • 10.1074/jbc.273.22.13375. 9593664
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. T Maehama JE Dixon, J Biol Chem 1998 273 13375 13378 10.1074/jbc.273.22.13375 9593664
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 4
    • 0035824396 scopus 로고    scopus 로고
    • Negative regulation of neuronal stem/progenitor cell proliferation by the PTEN tumor suppressor gene in vivo
    • 10.1126/science.1065518. 11691952
    • Negative regulation of neuronal stem/progenitor cell proliferation by the PTEN tumor suppressor gene in vivo. M Groszer R Erickson DD Scripture-Adams R Lesche A Trumpp JA Zack HI Kornblum X Liu H Wu, Science 2001 294 2186 2189 10.1126/science.1065518 11691952
    • (2001) Science , vol.294 , pp. 2186-2189
    • Groszer, M.1    Erickson, R.2    Scripture-Adams, D.D.3    Lesche, R.4    Trumpp, A.5    Zack, J.A.6    Kornblum, H.I.7    Liu, X.8    Wu, H.9
  • 6
    • 35748935116 scopus 로고    scopus 로고
    • Phosphatase PTEN in neuronal injury and brain disorders
    • DOI 10.1016/j.tins.2007.08.006, PII S0166223607002470
    • Phosphatase PTEN in neuronal injury and brain disorders. N Chang YH El-Hayek E Gomez Q Wan, Trends in Neurosci 2007 30 581 586 10.1016/j.tins.2007. 08.006 (Pubitemid 350051425)
    • (2007) Trends in Neurosciences , vol.30 , Issue.11 , pp. 581-586
    • Chang, N.1    El-Hayek, Y.H.2    Gomez, E.3    Wan, Q.4
  • 8
    • 75949103435 scopus 로고    scopus 로고
    • E3 ligase Nedd4 promotes axon branching by downregulating PTEN
    • 10.1016/j.neuron.2010.01.017. 20159448
    • E3 ligase Nedd4 promotes axon branching by downregulating PTEN. J Drinjakovic H Jung DS Campbell L Strochlic A Dwivedy CE Holt, Neuron 2010 65 341 357 10.1016/j.neuron.2010.01.017 20159448
    • (2010) Neuron , vol.65 , pp. 341-357
    • Drinjakovic, J.1    Jung, H.2    Campbell, D.S.3    Strochlic, L.4    Dwivedy, A.5    Holt, C.E.6
  • 9
    • 77953562076 scopus 로고    scopus 로고
    • Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination
    • 10.1126/science.1187735. 20448149
    • Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination. L Cotter M Ozçelik C Jacob JA Pereira V Locher R Baumann JB Relvas U Suter N Tricaud, Science 2010 328 1415 1418 10.1126/science.1187735 20448149
    • (2010) Science , vol.328 , pp. 1415-1418
    • Cotter, L.1    Ozçelik, M.2    Jacob, C.3    Pereira, J.A.4    Locher, V.5    Baumann, R.6    Relvas, J.B.7    Suter, U.8    Tricaud, N.9
  • 10
    • 33644817011 scopus 로고    scopus 로고
    • Disruption of PTEN coupling with 5-HT2C receptors suppresses behavioral responses induced by drugs of abuse
    • 10.1038/nm1349. 16474401
    • Disruption of PTEN coupling with 5-HT2C receptors suppresses behavioral responses induced by drugs of abuse. SP Ji Y Zhang J Van Cleemput W Jiang M Liao L Li Q Wan JR Backstrom X Zhang, Nat Med 2006 12 324 329 10.1038/nm1349 16474401
    • (2006) Nat Med , vol.12 , pp. 324-329
    • Ji, S.P.1    Zhang, Y.2    Van Cleemput, J.3    Jiang, W.4    Liao, M.5    Li, L.6    Wan, Q.7    Backstrom, J.R.8    Zhang, X.9
  • 11
    • 16244391770 scopus 로고    scopus 로고
    • Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer's disease pathology
    • 10.1111/j.1471-4159.2004.02949.x. 15773910
    • Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer's disease pathology. RJ Griffin A Moloney M Kelliher JA Johnston R Ravid P Dockery R O'Connor C O'Neill, J Neurochem 2005 93 105 117 10.1111/j.1471-4159.2004. 02949.x 15773910
    • (2005) J Neurochem , vol.93 , pp. 105-117
    • Griffin, R.J.1    Moloney, A.2    Kelliher, M.3    Johnston, J.A.4    Ravid, R.5    Dockery, P.6    O'Connor, R.7    O'Neill, C.8
  • 13
    • 33845619414 scopus 로고    scopus 로고
    • Tumor-suppressor PTEN affects tau phosphorylation, aggregation, and binding to microtubules
    • 10.1096/fj.06-5721fje. 16645045
    • Tumor-suppressor PTEN affects tau phosphorylation, aggregation, and binding to microtubules. X Zhang F Li A Bulloj YW Zhang G Tong Z Zhang FF Liao H Xu, FASEB J 2006 20 1272 1274 10.1096/fj.06-5721fje 16645045
    • (2006) FASEB J , vol.20 , pp. 1272-1274
    • Zhang, X.1    Li, F.2    Bulloj, A.3    Zhang, Y.W.4    Tong, G.5    Zhang, Z.6    Liao, F.F.7    Xu, H.8
  • 14
    • 51849155581 scopus 로고    scopus 로고
    • Post-translational regulation of PTEN
    • 10.1038/onc.2008.242. 18794880
    • Post-translational regulation of PTEN. X Wang X Jiang, Oncogene 2008 27 5454 5463 10.1038/onc.2008.242 18794880
    • (2008) Oncogene , vol.27 , pp. 5454-5463
    • Wang, X.1    Jiang, X.2
  • 15
    • 77951240772 scopus 로고    scopus 로고
    • Functional interaction of phosphatase and tensin homologue (PTEN) with the E3 ligase NEDD4-1 during neuronal response to zinc
    • 10.1074/jbc.M109.091637. 20100827
    • Functional interaction of phosphatase and tensin homologue (PTEN) with the E3 ligase NEDD4-1 during neuronal response to zinc. YD Kwak B Wang W Pan H Xu X Jiang FF Liao, J Biol Chem 2010 285 9847 9857 10.1074/jbc.M109.091637 20100827
    • (2010) J Biol Chem , vol.285 , pp. 9847-9857
    • Kwak, Y.D.1    Wang, B.2    Pan, W.3    Xu, H.4    Jiang, X.5    Liao, F.F.6
  • 16
    • 0033946740 scopus 로고    scopus 로고
    • Phosphorylation of the PTEN tail regulates protein stability and function
    • 10.1128/MCB.20.14.5010-5018.2000. 10866658
    • Phosphorylation of the PTEN tail regulates protein stability and function. F Vazquez S Ramaswamy N Nakamura WR Sellers, Mol Cell Biol 2000 20 5010 5018 10.1128/MCB.20.14.5010-5018.2000 10866658
    • (2000) Mol Cell Biol , vol.20 , pp. 5010-5018
    • Vazquez, F.1    Ramaswamy, S.2    Nakamura, N.3    Sellers, W.R.4
  • 17
    • 34547490078 scopus 로고    scopus 로고
    • PTEN is destabilized by phosphorylation on Thr 366
    • 10.1042/BJ20061837. 17444818
    • PTEN is destabilized by phosphorylation on Thr 366. H Maccario NM Perera L Davidson CP Downes NR Leslie, Biochem J 2007 405 439 444 10.1042/BJ20061837 17444818
    • (2007) Biochem J , vol.405 , pp. 439-444
    • MacCario, H.1    Perera, N.M.2    Davidson, L.3    Downes, C.P.4    Leslie, N.R.5
  • 19
    • 0142137134 scopus 로고    scopus 로고
    • Redox regulation of PI 3-kinase signalling via inactivation of PTEN
    • 10.1093/emboj/cdg513. 14532122
    • Redox regulation of PI 3-kinase signalling via inactivation of PTEN. NR Leslie D Bennett YE Lindsay H Stewart A Gray CP Downes, EMBO J 2003 22 5501 5510 10.1093/emboj/cdg513 14532122
    • (2003) EMBO J , vol.22 , pp. 5501-5510
    • Leslie, N.R.1    Bennett, D.2    Lindsay, Y.E.3    Stewart, H.4    Gray, A.5    Downes, C.P.6
  • 20
    • 23944468310 scopus 로고    scopus 로고
    • Redox regulation of PTEN by S-nitrosothiols
    • 15967877
    • Redox regulation of PTEN by S-nitrosothiols. CX Yu S Li AR Whorton, Mol Pharmacol 2005 68 847 854 15967877
    • (2005) Mol Pharmacol , vol.68 , pp. 847-854
    • Yu, C.X.1    Li, S.2    Whorton, A.R.3
  • 21
    • 34548159221 scopus 로고    scopus 로고
    • Akt activation by arachidonic acid metabolism occurs via oxidation and inactivation of PTEN tumor suppressor
    • 10.1038/sj.onc.1210391. 17369849
    • Akt activation by arachidonic acid metabolism occurs via oxidation and inactivation of PTEN tumor suppressor. TM Covey K Edes FA Fitzpatrick, Oncogene 2007 26 5784 5792 10.1038/sj.onc.1210391 17369849
    • (2007) Oncogene , vol.26 , pp. 5784-5792
    • Covey, T.M.1    Edes, K.2    Fitzpatrick, F.A.3
  • 22
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • 10.1074/jbc.M111899200. 11916965
    • Reversible inactivation of the tumor suppressor PTEN by H2O2. SR Lee KS Yang J Kwon C Lee W Jeong SG Rhee, J Biol Chem 2002 277 20336 20342 10.1074/jbc.M111899200 11916965
    • (2002) J Biol Chem , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 23
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • 10.1073/pnas.0407396101. 15534200
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. J Kwon SR Lee KS Yang Y Ahn YJ Kim ER Stadtman SG Rhee, Proc Natl Acad Sci USA 2004 101 16419 16424 10.1073/pnas.0407396101 15534200
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16419-16424
    • Kwon, J.1    Lee, S.R.2    Yang, K.S.3    Ahn, Y.4    Kim, Y.J.5    Stadtman, E.R.6    Rhee, S.G.7
  • 24
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • 10.1016/j.molmed.2009.06.007. 19726230
    • Protein S-nitrosylation in health and disease: a current perspective. MW Foster DT Hess JS Stamler, Trends Mol Med 2009 15 391 404 10.1016/j.molmed.2009. 06.007 19726230
    • (2009) Trends Mol Med , vol.15 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 25
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • 10.1038/ncb851. 12244325
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. J Haendeler J Hoffmann V Tischler BC Berk AM Zeiher S Dimmeler, Nat Cell Biol 2002 4 743 749 10.1038/ncb851 12244325
    • (2002) Nat Cell Biol , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 26
    • 77951834544 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits mTOR signaling by activation of AMPKalpha leading to apoptosis of neuronal cells
    • 10.1038/labinvest.2010.36. 20142804
    • Hydrogen peroxide inhibits mTOR signaling by activation of AMPKalpha leading to apoptosis of neuronal cells. L Chen B Xu L Liu Y Luo J Yin H Zhou W Chen T Shen X Han S Huang, Lab Invest 2010 90 762 773 10.1038/labinvest.2010.36 20142804
    • (2010) Lab Invest , vol.90 , pp. 762-773
    • Chen, L.1    Xu, B.2    Liu, L.3    Luo, Y.4    Yin, J.5    Zhou, H.6    Chen, W.7    Shen, T.8    Han, X.9    Huang, S.10
  • 27
    • 33644687454 scopus 로고    scopus 로고
    • PTEN activity is modulated during ischemia and reperfusion: Involvement in the induction and decay of preconditioning
    • 10.1161/01.RES.0000195656.52760.30. 16284183
    • PTEN activity is modulated during ischemia and reperfusion: involvement in the induction and decay of preconditioning. Z Cai GL Semenza, Circ Res 2005 97 1351 1359 10.1161/01.RES.0000195656.52760.30 16284183
    • (2005) Circ Res , vol.97 , pp. 1351-1359
    • Cai, Z.1    Semenza, G.L.2
  • 28
    • 33745763116 scopus 로고    scopus 로고
    • Cerebral preconditioning and ischaemic tolerance
    • 10.1038/nrn1927. 16715053
    • Cerebral preconditioning and ischaemic tolerance. JM Gidday, Nat Rev Neurosci 2006 7 437 448 10.1038/nrn1927 16715053
    • (2006) Nat Rev Neurosci , vol.7 , pp. 437-448
    • Gidday, J.M.1
  • 29
    • 65549106019 scopus 로고    scopus 로고
    • Ischemic postconditioning as a novel avenue to protect against brain injury after stroke
    • 10.1038/jcbfm.2009.13. 19240739
    • Ischemic postconditioning as a novel avenue to protect against brain injury after stroke. H Zhao, J Cereb Blood Flow Metab 2009 29 873 885 10.1038/jcbfm.2009.13 19240739
    • (2009) J Cereb Blood Flow Metab , vol.29 , pp. 873-885
    • Zhao, H.1
  • 32
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • 10.1016/S0092-8674(00)81663-3. 10555148
    • Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. JO Lee H Yang MM Georgescu A Di Cristofano T Maehama Y Shi JE Dixon P Pandolfi NP Pavletich, Cell 1999 99 323 334 10.1016/S0092-8674(00)81663-3 10555148
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 33
    • 60849132775 scopus 로고    scopus 로고
    • Phosphorylation keeps PTEN phosphatase closed for business
    • 10.1073/pnas.0812473106. 19174524
    • Phosphorylation keeps PTEN phosphatase closed for business. AH Ross A Gericke, Proc Natl Acad Sci USA 2009 106 1297 1398 10.1073/pnas.0812473106 19174524
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1297-1398
    • Ross, A.H.1    Gericke, A.2
  • 35
    • 0347624596 scopus 로고    scopus 로고
    • S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway
    • 10.1128/MCB.24.1.330-337.2004. 14673166
    • S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway. S Kim SS Wing P Ponka, Mol Cell Biol 2004 24 330 337 10.1128/MCB.24.1.330-337.2004 14673166
    • (2004) Mol Cell Biol , vol.24 , pp. 330-337
    • Kim, S.1    Wing, S.S.2    Ponka, P.3
  • 36
    • 38149062111 scopus 로고    scopus 로고
    • Nitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins
    • 10.1074/jbc.M708821200. 17993647
    • Nitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins. CM Lee BY Kim L Li ET Morgan, J Biol Chem 2008 283 889 898 10.1074/jbc.M708821200 17993647
    • (2008) J Biol Chem , vol.283 , pp. 889-898
    • Lee, C.M.1    Kim, B.Y.2    Li, L.3    Morgan, E.T.4
  • 37
    • 47049087270 scopus 로고    scopus 로고
    • Role of S-nitrosylation in apoptosis resistance and carcinogenesis
    • 10.1016/j.niox.2008.04.019. 18474261
    • Role of S-nitrosylation in apoptosis resistance and carcinogenesis. AK Iyer N Azad L Wang Y Rojanasakul, Nitric Oxide 2008 19 146 151 10.1016/j.niox.2008.04.019 18474261
    • (2008) Nitric Oxide , vol.19 , pp. 146-151
    • Iyer, A.K.1    Azad, N.2    Wang, L.3    Rojanasakul, Y.4
  • 38
    • 70350514910 scopus 로고    scopus 로고
    • Nitric oxide regulates lung carcinoma cell anoikis through inhibition of Ubiquitin-proteasomal degradation of caveolin-1
    • 10.1074/jbc.M109.050864. 19706615
    • Nitric oxide regulates lung carcinoma cell anoikis through inhibition of Ubiquitin-proteasomal degradation of caveolin-1. P Chanvorachote U Nimmannit Y Lu S Talbott BH Jiang Y Rojanasakul, J Biol Chem 2009 284 28476 28484 10.1074/jbc.M109.050864 19706615
    • (2009) J Biol Chem , vol.284 , pp. 28476-28484
    • Chanvorachote, P.1    Nimmannit, U.2    Lu, Y.3    Talbott, S.4    Jiang, B.H.5    Rojanasakul, Y.6
  • 39
    • 33747425620 scopus 로고    scopus 로고
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease
    • 16914869
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease. A Takashima, J Alzheimers Dis 2006 9 3 Suppl 309 317 16914869
    • (2006) J Alzheimers Dis , vol.9 , Issue.3 SUPPL. , pp. 309-317
    • Takashima, A.1
  • 40
    • 72449142133 scopus 로고    scopus 로고
    • CK2 is a novel negative regulator of NADPH oxidase and a neuroprotectant in mice after cerebral ischemia
    • 10.1523/JNEUROSCI.4161-09.2009. 19940173
    • CK2 is a novel negative regulator of NADPH oxidase and a neuroprotectant in mice after cerebral ischemia. GS Kim JE Jung K Niizuma PH Chan, J Neurosci 2009 29 14779 14789 10.1523/JNEUROSCI.4161-09.2009 19940173
    • (2009) J Neurosci , vol.29 , pp. 14779-14789
    • Kim, G.S.1    Jung, J.E.2    Niizuma, K.3    Chan, P.H.4
  • 41
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • 10.1111/j.1460-9568.2005.04391.x. 16262633
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. F Liu I Grundke-Iqbal K Iqbal CX Gong, Eur J Neurosci 2005 22 1942 1950 10.1111/j.1460-9568.2005.04391.x 16262633
    • (2005) Eur J Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 44
    • 34047195222 scopus 로고    scopus 로고
    • PTEN, the Achilles' heel of myocardial ischaemia/reperfusion injury?
    • 10.1038/sj.bjp.0707155. 17293884
    • PTEN, the Achilles' heel of myocardial ischaemia/reperfusion injury? MM Mocanu DM Yellon, Br J Pharmacol 2007 150 833 838 10.1038/sj.bjp.0707155 17293884
    • (2007) Br J Pharmacol , vol.150 , pp. 833-838
    • Mocanu, M.M.1    Yellon, D.M.2
  • 46
    • 66149107054 scopus 로고    scopus 로고
    • Obesity increases vascular senescence and susceptibility to ischemic injury through chronic activation of Akt and mTOR
    • 10.1126/scisignal.2000143. 19293429
    • Obesity increases vascular senescence and susceptibility to ischemic injury through chronic activation of Akt and mTOR. CY Wang HH Kim Y Hiroi N Sawada S Salomone LE Benjamin K Walsh MA Moskowitz JK Liao, Sci Signal 2009 2 62 a11 10.1126/scisignal.2000143 19293429
    • (2009) Sci Signal , vol.2 , Issue.62
    • Wang, C.Y.1    Kim, H.H.2    Hiroi, Y.3    Sawada, N.4    Salomone, S.5    Benjamin, L.E.6    Walsh, K.7    Moskowitz, M.A.8    Liao, J.K.9
  • 47
    • 37849027524 scopus 로고    scopus 로고
    • Phosphatase and tensin homolog, deleted on chromosome 10 deficiency in brain causes defects in synaptic structure, transmission and plasticity, and myelination abnormalities
    • 10.1016/j.neuroscience.2007.10.048. 18082964
    • Phosphatase and tensin homolog, deleted on chromosome 10 deficiency in brain causes defects in synaptic structure, transmission and plasticity, and myelination abnormalities. MM Fraser IT Bayazitov SS Zakharenko SJ Baker, Neuroscience 2008 151 476 488 10.1016/j.neuroscience.2007.10.048 18082964
    • (2008) Neuroscience , vol.151 , pp. 476-488
    • Fraser, M.M.1    Bayazitov, I.T.2    Zakharenko, S.S.3    Baker, S.J.4
  • 48
    • 70349124239 scopus 로고    scopus 로고
    • Statin's excitoprotection is mediated by sAPP and the subsequent attenuation of calpain-induced truncation events, likely via rho-ROCK signaling
    • 10.1523/JNEUROSCI.6150-08.2009. 19741129
    • Statin's excitoprotection is mediated by sAPP and the subsequent attenuation of calpain-induced truncation events, likely via rho-ROCK signaling. T Ma Y Zhao YD Kwak Z Yang R Thompson Z Luo H Xu FF Liao, J Neurosci 2009 29 11226 11236 10.1523/JNEUROSCI.6150-08.2009 19741129
    • (2009) J Neurosci , vol.29 , pp. 11226-11236
    • Ma, T.1    Zhao, Y.2    Kwak, Y.D.3    Yang, Z.4    Thompson, R.5    Luo, Z.6    Xu, H.7    Liao, F.F.8
  • 49
    • 0026632865 scopus 로고
    • Effect of nitric oxide production on the redox modulatory site of the NMDA receptor-channel complex
    • 10.1016/0896-6273(92)90130-6. 1376999
    • Effect of nitric oxide production on the redox modulatory site of the NMDA receptor-channel complex. SZ Lei ZH Pan SK Aggarwal HS Chen J Hartman NJ Sucher SA Lipton, Neuron 1992 8 1087 1099 10.1016/0896-6273(92)90130-6 1376999
    • (1992) Neuron , vol.8 , pp. 1087-1099
    • Lei, S.Z.1    Pan, Z.H.2    Aggarwal, S.K.3    Chen, H.S.4    Hartman, J.5    Sucher, N.J.6    Lipton, S.A.7
  • 50
    • 3843125309 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • 10.1126/stke.2001.86.pl1. 11752655
    • The biotin switch method for the detection of S-nitrosylated proteins. SR Jaffrey SH Synder, Sci STKE 2001 2001 l1 10.1126/stke.2001.86.pl1 11752655
    • (2001) Sci STKE , vol.2001
    • Jaffrey, S.R.1    Synder, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.