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Volumn 8, Issue 3, 2013, Pages

Structural Characterization of the Self-Association of the Death Domain of p75NTR

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DIMER; NEUROTROPHIN; NEUROTROPHIN RECEPTOR P75; OLIGOMER; DISULFIDE; HYBRID PROTEIN; NERVE GROWTH FACTOR RECEPTOR; TNFRSF16 PROTEIN, RAT;

EID: 84874617834     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0057839     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0037762690 scopus 로고    scopus 로고
    • Neurotrophins and their receptors: a convergence point for many signalling pathways
    • Chao MV, (2003) Neurotrophins and their receptors: a convergence point for many signalling pathways. Nature Reviews Neuroscience 4: 299-309.
    • (2003) Nature Reviews Neuroscience , vol.4 , pp. 299-309
    • Chao, M.V.1
  • 3
    • 0030851905 scopus 로고    scopus 로고
    • NMR structure of the death domain of the p75 neurotrophin receptor
    • Liepinsh E, Ilag LL, Otting G, Ibanez CF, (1997) NMR structure of the death domain of the p75 neurotrophin receptor. EMBO J 16: 4999-5005.
    • (1997) EMBO J , vol.16 , pp. 4999-5005
    • Liepinsh, E.1    Ilag, L.L.2    Otting, G.3    Ibanez, C.F.4
  • 6
    • 0036591405 scopus 로고    scopus 로고
    • The many faces of p75NTR
    • Hempstead BL, (2002) The many faces of p75NTR. Curr Opin Neurobiol 12: 260-267.
    • (2002) Curr Opin Neurobiol , vol.12 , pp. 260-267
    • Hempstead, B.L.1
  • 7
    • 0036344505 scopus 로고    scopus 로고
    • Neurotrophin signaling through the p75 neurotrophin receptor
    • Roux PP, Barker PA, (2002) Neurotrophin signaling through the p75 neurotrophin receptor. Prog Neurobiol 67: 203-233.
    • (2002) Prog Neurobiol , vol.67 , pp. 203-233
    • Roux, P.P.1    Barker, P.A.2
  • 9
    • 36348954513 scopus 로고    scopus 로고
    • Modulation of semaphorin3A activity by p75 neurotrophin receptor influences peripheral axon patterning
    • Ben-Zvi A, Ben-Gigi L, Klein H, Behar O, (2007) Modulation of semaphorin3A activity by p75 neurotrophin receptor influences peripheral axon patterning. The Journal of Neuroscience 27: 13000.
    • (2007) The Journal of Neuroscience , vol.27 , pp. 13000
    • Ben-Zvi, A.1    Ben-Gigi, L.2    Klein, H.3    Behar, O.4
  • 10
    • 50849086093 scopus 로고    scopus 로고
    • p75NTR mediates ephrin-A reverse signaling required for axon repulsion and mapping
    • Lim YS, McLaughlin T, Sung TC, Santiago A, Lee KF, et al. (2008) p75NTR mediates ephrin-A reverse signaling required for axon repulsion and mapping. Neuron 59: 746-758.
    • (2008) Neuron , vol.59 , pp. 746-758
    • Lim, Y.S.1    McLaughlin, T.2    Sung, T.C.3    Santiago, A.4    Lee, K.F.5
  • 11
    • 0032736538 scopus 로고    scopus 로고
    • Signaling of neuronal cell death by the p75NTR neurotrophin receptor
    • Coulson EJ, Reid K, Bartlett PF, (1999) Signaling of neuronal cell death by the p75NTR neurotrophin receptor. Mol Neurobiol 20: 29-44.
    • (1999) Mol Neurobiol , vol.20 , pp. 29-44
    • Coulson, E.J.1    Reid, K.2    Bartlett, P.F.3
  • 12
    • 34347209978 scopus 로고    scopus 로고
    • A cell-biological model of p75NTR signaling
    • Blochl A, Blochl R, (2007) A cell-biological model of p75NTR signaling. J Neurochem 102: 289-305.
    • (2007) J Neurochem , vol.102 , pp. 289-305
    • Blochl, A.1    Blochl, R.2
  • 13
    • 0035528832 scopus 로고    scopus 로고
    • The neurotrophin receptor p75NTR is a tumor suppressor in human prostate cancer
    • Krygier S, Djakiew D, (2001) The neurotrophin receptor p75NTR is a tumor suppressor in human prostate cancer. Anticancer Res 21: 3749-3755.
    • (2001) Anticancer Res , vol.21 , pp. 3749-3755
    • Krygier, S.1    Djakiew, D.2
  • 14
    • 6444229684 scopus 로고    scopus 로고
    • Gene therapy of prostate xenograft tumors with a p75NTR lipoplex
    • Allen J, Khwaja F, Djakiew D, (2004) Gene therapy of prostate xenograft tumors with a p75NTR lipoplex. Anticancer Res 24: 2997-3003.
    • (2004) Anticancer Res , vol.24 , pp. 2997-3003
    • Allen, J.1    Khwaja, F.2    Djakiew, D.3
  • 15
    • 26444604474 scopus 로고    scopus 로고
    • The neurotrophin receptor p75NTR mediates early anti-inflammatory effects of estrogen in the forebrain of young adult rats
    • Nordell VL, Lewis DK, Bake S, Sohrabji F, (2005) The neurotrophin receptor p75NTR mediates early anti-inflammatory effects of estrogen in the forebrain of young adult rats. BMC Neurosci 6: 58.
    • (2005) BMC Neurosci , vol.6 , pp. 58
    • Nordell, V.L.1    Lewis, D.K.2    Bake, S.3    Sohrabji, F.4
  • 16
    • 34249815194 scopus 로고    scopus 로고
    • Roles of glial p75NTR in axonal regeneration
    • Zhou XF, Li HY, (2007) Roles of glial p75NTR in axonal regeneration. J Neurosci Res 85: 1601-1605.
    • (2007) J Neurosci Res , vol.85 , pp. 1601-1605
    • Zhou, X.F.1    Li, H.Y.2
  • 17
    • 77449115618 scopus 로고    scopus 로고
    • p75NTR as a therapeutic target for neuropsychiatric diseases
    • Fujii T, Kunugi H, (2009) p75NTR as a therapeutic target for neuropsychiatric diseases. Curr Mol Pharmacol 2: 70-76.
    • (2009) Curr Mol Pharmacol , vol.2 , pp. 70-76
    • Fujii, T.1    Kunugi, H.2
  • 18
    • 80054678078 scopus 로고    scopus 로고
    • Roles of p75NTR in the pathogenesis of Alzheimer's disease: A novel therapeutic target
    • Zeng F, Lu JJ, Zhou XF, Wang YJ, (2011) Roles of p75NTR in the pathogenesis of Alzheimer's disease: A novel therapeutic target. Biochem Pharmacol.
    • (2011) Biochem Pharmacol
    • Zeng, F.1    Lu, J.J.2    Zhou, X.F.3    Wang, Y.J.4
  • 19
    • 49649094883 scopus 로고    scopus 로고
    • Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex
    • Gong Y, Cao P, Yu HJ, Jiang T, (2008) Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex. Nature 454: 789-793.
    • (2008) Nature , vol.454 , pp. 789-793
    • Gong, Y.1    Cao, P.2    Yu, H.J.3    Jiang, T.4
  • 20
    • 77950346220 scopus 로고    scopus 로고
    • Molecular and structural insight into proNGF engagement of p75NTR and sortilin
    • Feng D, Kim T, Ozkan E, Light M, Torkin R, et al. (2010) Molecular and structural insight into proNGF engagement of p75NTR and sortilin. J Mol Biol 396: 967-984.
    • (2010) J Mol Biol , vol.396 , pp. 967-984
    • Feng, D.1    Kim, T.2    Ozkan, E.3    Light, M.4    Torkin, R.5
  • 21
    • 0034213950 scopus 로고    scopus 로고
    • Dimerization-dependent block of the proapoptotic effect of p75NTR
    • Wang JJ, Rabizadeh S, Tasinato A, Sperandio S, Ye X, et al. (2000) Dimerization-dependent block of the proapoptotic effect of p75NTR. J Neurosci Res 60: 587-593.
    • (2000) J Neurosci Res , vol.60 , pp. 587-593
    • Wang, J.J.1    Rabizadeh, S.2    Tasinato, A.3    Sperandio, S.4    Ye, X.5
  • 22
    • 64149116399 scopus 로고    scopus 로고
    • Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers
    • Vilar M, Charalampopoulos I, Kenchappa RS, Simi A, Karaca E, et al. (2009) Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers. Neuron 62: 72-83.
    • (2009) Neuron , vol.62 , pp. 72-83
    • Vilar, M.1    Charalampopoulos, I.2    Kenchappa, R.S.3    Simi, A.4    Karaca, E.5
  • 23
    • 40049083421 scopus 로고    scopus 로고
    • 5, 5′-Dithio-bis (2-nitrobenzoic acid) modification of cysteine improves the crystal quality of human chloride intracellular channel protein 2
    • Mi W, Li L, Su XD, (2008) 5, 5′-Dithio-bis (2-nitrobenzoic acid) modification of cysteine improves the crystal quality of human chloride intracellular channel protein 2. Biochemical and Biophysical Research Communications 368: 919-922.
    • (2008) Biochemical and Biophysical Research Communications , vol.368 , pp. 919-922
    • Mi, W.1    Li, L.2    Su, X.D.3
  • 24
    • 0037408391 scopus 로고    scopus 로고
    • The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI
    • Yamashita T, Tohyama M, (2003) The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI. Nat Neurosci 6: 461-467.
    • (2003) Nat Neurosci , vol.6 , pp. 461-467
    • Yamashita, T.1    Tohyama, M.2
  • 25
    • 34247842740 scopus 로고    scopus 로고
    • The death domain superfamily in intracellular signaling of apoptosis and inflammation
    • Park HH, Lo YC, Lin SC, Wang L, Yang JK, et al. (2007) The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annual Review of Immunology 25: 561.
    • (2007) Annual Review of Immunology , vol.25 , pp. 561
    • Park, H.H.1    Lo, Y.C.2    Lin, S.C.3    Wang, L.4    Yang, J.K.5
  • 26
    • 0033601077 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex between the death domains of Pelle and Tube
    • Xiao T, Towb P, Wasserman SA, Sprang SR, (1999) Three-dimensional structure of a complex between the death domains of Pelle and Tube. Cell 99: 545-555.
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 27
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park HH, Logette E, Raunser S, Cuenin S, Walz T, et al. (2007) Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 128: 533-546.
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3    Cuenin, S.4    Walz, T.5
  • 28
    • 60549106191 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure unravels signalling by receptor clustering
    • Scott FL, Stec B, Cristina Pop M, (2008) The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 457: 1019-1022.
    • (2008) Nature , vol.457 , pp. 1019-1022
    • Scott, F.L.1    Stec, B.2    Cristina Pop, M.3
  • 29
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin SC, Lo YC, Wu H, (2010) Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 465: 885-890.
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 30
    • 78549236456 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
    • Wang L, Yang JK, Kabaleeswaran V, Rice AJ, Cruz AC, et al. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature Structural & Molecular Biology 17: 1324-1329.
    • (2010) Nature Structural & Molecular Biology , vol.17 , pp. 1324-1329
    • Wang, L.1    Yang, J.K.2    Kabaleeswaran, V.3    Rice, A.J.4    Cruz, A.C.5
  • 31
    • 0035896406 scopus 로고    scopus 로고
    • A docking model of key components of the DISC complex: death domain superfamily interactions redefined
    • Weber CH, Vincenz C, (2001) A docking model of key components of the DISC complex: death domain superfamily interactions redefined. FEBS letters 492: 171-176.
    • (2001) FEBS Letters , vol.492 , pp. 171-176
    • Weber, C.H.1    Vincenz, C.2
  • 32
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Bailey S, (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 34
    • 0033231183 scopus 로고    scopus 로고
    • The zinc finger protein NRIF interacts with the neurotrophin receptor p75(NTR) and participates in programmed cell death
    • Casademunt E, Carter BD, Benzel I, Frade JM, Dechant G, et al. (1999) The zinc finger protein NRIF interacts with the neurotrophin receptor p75(NTR) and participates in programmed cell death. EMBO J 18: 6050-6061.
    • (1999) EMBO J , vol.18 , pp. 6050-6061
    • Casademunt, E.1    Carter, B.D.2    Benzel, I.3    Frade, J.M.4    Dechant, G.5
  • 35
    • 17144418443 scopus 로고    scopus 로고
    • Neurotrophin receptor interacting factor (NRIF) is an essential mediator of apoptotic signaling by the p75 neurotrophin receptor
    • Linggi MS, Burke TL, Williams BB, Harrington A, Kraemer R, et al. (2005) Neurotrophin receptor interacting factor (NRIF) is an essential mediator of apoptotic signaling by the p75 neurotrophin receptor. J Biol Chem 280: 13801-13808.
    • (2005) J Biol Chem , vol.280 , pp. 13801-13808
    • Linggi, M.S.1    Burke, T.L.2    Williams, B.B.3    Harrington, A.4    Kraemer, R.5
  • 36
    • 77957794023 scopus 로고    scopus 로고
    • Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus
    • Esposito D, Sankar A, Morgner N, Robinson CV, Rittinger K, et al. (2010) Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus. Structure 18: 1378-1390.
    • (2010) Structure , vol.18 , pp. 1378-1390
    • Esposito, D.1    Sankar, A.2    Morgner, N.3    Robinson, C.V.4    Rittinger, K.5
  • 37
    • 0035882380 scopus 로고    scopus 로고
    • A prosurvival function for the p75 receptor death domain mediated via the caspase recruitment domain receptor-interacting protein 2
    • Khursigara G, Bertin J, Yano H, Moffett H, DiStefano PS, et al. (2001) A prosurvival function for the p75 receptor death domain mediated via the caspase recruitment domain receptor-interacting protein 2. J Neurosci 21: 5854-5863.
    • (2001) J Neurosci , vol.21 , pp. 5854-5863
    • Khursigara, G.1    Bertin, J.2    Yano, H.3    Moffett, H.4    DiStefano, P.S.5
  • 38
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J, (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125: 1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 39
    • 26944498689 scopus 로고    scopus 로고
    • The intracellular domain of p75NTR as a determinant of cellular reducing potential and response to oxidant stress
    • Tyurina YY, Nylander KD, Mirnics ZK, Portugal C, Yan C, et al. (2005) The intracellular domain of p75NTR as a determinant of cellular reducing potential and response to oxidant stress. Aging Cell 4: 187-196.
    • (2005) Aging Cell , vol.4 , pp. 187-196
    • Tyurina, Y.Y.1    Nylander, K.D.2    Mirnics, Z.K.3    Portugal, C.4    Yan, C.5
  • 40
    • 67449132349 scopus 로고    scopus 로고
    • p75NTR-dependent modulation of cellular handling of reactive oxygen species
    • Mi Z, Rogers DA, Mirnics ZK, Schor NF, (2009) p75NTR-dependent modulation of cellular handling of reactive oxygen species. J Neurochem 110: 295-306.
    • (2009) J Neurochem , vol.110 , pp. 295-306
    • Mi, Z.1    Rogers, D.A.2    Mirnics, Z.K.3    Schor, N.F.4
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 276: 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A, Teplyakov A, (1997) MOLREP: an automated program for molecular replacement. Journal of Applied Crystallography 30: 1022-1025.
    • (1997) Journal of Applied Crystallography , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2


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