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Volumn 168-169, Issue , 2012, Pages 48-59

Modulation of the neurotensin solution structure in the presence of ganglioside GM1 bicelle

Author keywords

Bicelle; Docking; GM1; Neurotensin; NMR; NTS3

Indexed keywords

GANGLIOSIDE GM1; NEUROTENSIN; PEPTIDE; SORTILIN;

EID: 84864041624     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2012.06.003     Document Type: Article
Times cited : (14)

References (49)
  • 3
    • 0031435902 scopus 로고    scopus 로고
    • Nenrotensin-like immunoreactivity in the brain of the chicken, Gallus domesticus
    • DOI 10.1017/S0021878297002719
    • V. Esposito, P. Girolamo, and G. Gargiulo Neurotensin-like immunoreactivity in the brain of the chicken, Gallus domesticus Journal of Anatomy 191 1997 537 546 (Pubitemid 28022415)
    • (1997) Journal of Anatomy , vol.191 , Issue.4 , pp. 537-546
    • Esposito, V.1    De Girolamo, P.2    Gargiulo, G.3
  • 4
    • 0030890835 scopus 로고    scopus 로고
    • Negative modulation of nitric oxide production by neurotensin as a putative mechanism of the diuretic action of SR 48692 in rats
    • DOI 10.1038/sj.bjp.0701016
    • T. Croci, M. Landi, D. Gully, J.P. Maffrand, G.L. Fur, and L. Manara Negative modulation of nitric oxide production by neurotensin as a putative mechanism of the diuretic action of SR 48692 in rats British Journal of Pharmacology 120 1997 1312 1318 (Pubitemid 27149682)
    • (1997) British Journal of Pharmacology , vol.120 , Issue.7 , pp. 1312-1318
    • Croci, T.1    Landi, M.2    Gully, D.3    Maffrand, J.-P.4    Le Fur, G.5    Manara, L.6
  • 5
    • 0037042195 scopus 로고    scopus 로고
    • Probing the environment of neurotensin whilst bound to the neurotensin receptor by solid state NMR
    • DOI 10.1016/S0014-5793(02)02656-X, PII S001457930202656X
    • P.T.F. Williamson, S. Bains, C. Chung, R. Cooke, and A. Watts Probing the environment of neurotensin whilst bound to the neurotensin receptor by solid state NMR FEBS Letters 518 2002 111 115 (Pubitemid 34454974)
    • (2002) FEBS Letters , vol.518 , Issue.1-3 , pp. 111-115
    • Williamson, P.T.F.1    Bains, S.2    Chung, C.3    Cooke, R.4    Watts, A.5
  • 6
    • 77957200346 scopus 로고    scopus 로고
    • Targeting neurotensin as a potential novel approach for the treatment of autism
    • A. Ghanizadeh Targeting neurotensin as a potential novel approach for the treatment of autism Journal of Neuroinflammation 58 2010 1 2
    • (2010) Journal of Neuroinflammation , vol.58 , pp. 1-2
    • Ghanizadeh, A.1
  • 7
    • 33748756339 scopus 로고    scopus 로고
    • Involvement of neurotensin in cancer growth: Evidence, mechanisms and development of diagnostic tools
    • DOI 10.1016/j.peptides.2006.04.030, PII S0196978106002956
    • R.E. Carraway, and A.M. Plona Involvement of neurotensin in cancer growth: evidence, mechanisms and development of diagnostic tools Peptides 27 2006 2445 2460 (Pubitemid 44402788)
    • (2006) Peptides , vol.27 , Issue.10 , pp. 2445-2460
    • Carraway, R.E.1    Plona, A.M.2
  • 8
    • 33748893018 scopus 로고    scopus 로고
    • Interactions between neurotensin receptors and G proteins
    • DOI 10.1016/j.peptides.2006.04.027, PII S0196978106002981
    • D. Pelaprat Interactions between neurotensin receptors and G proteins Peptides 27 2006 2476 2487 (Pubitemid 44425365)
    • (2006) Peptides , vol.27 , Issue.10 , pp. 2476-2487
    • Pelaprat, D.1
  • 9
    • 0032942578 scopus 로고    scopus 로고
    • Neurotensin receptor-mediated inhibition of pancreatic cancer cell growth by the neurotensin antagonist SR 48692
    • M.C. Herzig, W.G. Chapman, A. Sheridan, J.B. Rake, and J.M. Woynarowski Neurotensin receptor-mediated inhibition of pancreatic cancer cell growth by the neurotensin antagonist SR 48692 Anticancer Research 19 1999 213 219 (Pubitemid 29168240)
    • (1999) Anticancer Research , vol.19 , Issue.1 A , pp. 213-219
    • Herzig, M.C.S.1    Chapman, W.G.2    Sheridan, A.3    Rake, J.B.4    Woynarowski, J.M.5
  • 10
    • 34248580608 scopus 로고    scopus 로고
    • NMR solution structure of neurotensin in membrane-mimetic environments: Molecular basis for neurotensin receptor recognition
    • DOI 10.1021/bi602567p
    • J. Coutant, P.A. Curmi, F. Toma, and J.P. Monti NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition Biochemistry 46 2007 5656 5663 (Pubitemid 46764115)
    • (2007) Biochemistry , vol.46 , Issue.19 , pp. 5656-5663
    • Coutant, J.1    Curmi, P.A.2    Toma, F.3    Monti, J.-P.4
  • 11
    • 0025857299 scopus 로고
    • Conformations of neurotensin in solution and in membrane environments studied by 2-D NMR spectroscopy
    • G.Y. Xu, and C.M. Deber Conformations of neurotensin in solution and in membrane environments studied by 2-D NMR spectroscopy International Journal of Peptide and Protein Research 37 1991 528 535
    • (1991) International Journal of Peptide and Protein Research , vol.37 , pp. 528-535
    • Xu, G.Y.1    Deber, C.M.2
  • 12
    • 0027467490 scopus 로고
    • Ganglioside metabolism. Enzymology, topology, and regulation
    • G. van Echten, and K. Sandhoff Ganglioside metabolism. Enzymology, topology, and regulation Journal of Biological Chemistry 268 1993 5341 5344 (Pubitemid 23090844)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.8 , pp. 5341-5344
    • Van Echten, G.1    Sandhoff, K.2
  • 13
    • 52449130577 scopus 로고    scopus 로고
    • Imaging mass spectrometry technology and application on ganglioside study; Visualization of age-dependent accumulation of C20-ganglioside molecular species in the mouse hippocampus
    • Y. Sugiura, S. Shimma, Y. Konishi, M.K. Yamada, and M. Setou Imaging mass spectrometry technology and application on ganglioside study; visualization of age-dependent accumulation of C20-ganglioside molecular species in the mouse hippocampus PLoS One 3 2008 1 9
    • (2008) PLoS One , vol.3 , pp. 1-9
    • Sugiura, Y.1    Shimma, S.2    Konishi, Y.3    Yamada, M.K.4    Setou, M.5
  • 14
    • 84865054172 scopus 로고    scopus 로고
    • Structure and dynamics of glycosphingolipids in lipid bilayers: Insights from molecular dynamics simulations
    • R.Y. Patel, and P.V. Balaji Structure and dynamics of glycosphingolipids in lipid bilayers: insights from molecular dynamics simulations International Journal of Carbohydrate Chemistry 2011 2011 1 9
    • (2011) International Journal of Carbohydrate Chemistry , vol.2011 , pp. 1-9
    • Patel, R.Y.1    Balaji, P.V.2
  • 15
    • 0031932859 scopus 로고    scopus 로고
    • Interaction of gangliosides with proteins depending on oligosaccharide chain and protein surface modification
    • M. Hirai, H. Iwase, S. Arai, T. Takizawa, and K. Hayashi Interaction of gangliosides with proteins depending on oligosaccharide chain and protein surface modification Biophysical Journal 74 1998 1380 1387 (Pubitemid 28108546)
    • (1998) Biophysical Journal , vol.74 , Issue.3 , pp. 1380-1387
    • Hirai, M.1    Iwase, H.2    Arai, S.3    Takizawa, T.4    Hayashi, K.5
  • 17
    • 0020464304 scopus 로고
    • 1 ganglioside
    • DOI 10.1007/BF01954946
    • M. Rochus, G. Kayser, M. Deleers, and J.M. Ruysschaert Specific interaction between soybean agglutinin and lipid bilayers containing the GM 1 ganglioside Experientia 38 1982 1351 1352 (Pubitemid 13170741)
    • (1982) Experientia , vol.38 , Issue.11 , pp. 1351-1352
    • Rochus, M.1    Kayser, G.2    Deleers, M.3    Ruysschaert, J.M.4
  • 18
    • 0023905930 scopus 로고
    • Complex ganglioside expression and tetanus toxin binding by PC12 pheochromocytoma cells
    • K.M. Walton, K. Sandberg, T.B. Rogers, and R.L. Schnaar Complex ganglioside expression and tetanus toxin binding by PC12 pheochromocytoma cells Journal of Biological Chemistry 263 1988 2055 2063 (Pubitemid 18052169)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.4 , pp. 2055-2063
    • Walton, K.M.1    Sandberg, K.2    Rogers, T.B.3    Schnaar, R.L.4
  • 19
    • 0042691217 scopus 로고    scopus 로고
    • Gangliosides are receptors for murine polyoma virus and SV40
    • DOI 10.1093/emboj/cdg439
    • B. Tsai, J.M. Gilbert, T. Stehle, W. Lencer, T.L. Benjamin, and T.A. Rapoport Gangliosides are receptors for murine polyoma virus and SV40 EMBO Journal 22 2003 4346 4355 (Pubitemid 37087189)
    • (2003) EMBO Journal , vol.22 , Issue.17 , pp. 4346-4355
    • Tsai, B.1    Gilbert, J.M.2    Stehle, T.3    Lencer, W.4    Benjamin, T.L.5    Rapoport, T.A.6
  • 20
    • 2542469878 scopus 로고    scopus 로고
    • Glycolipid-mediated cell-cell recognition in inflammation and nerve regeneration
    • DOI 10.1016/j.abb.2004.02.019, PII S0003986104000943
    • R.L. Schnaar Glycolipid-mediated cell-cell recognition in inflammation and nerve regeneration Archives of Biochemistry and Biophysics 426 2004 163 172 (Pubitemid 38680614)
    • (2004) Archives of Biochemistry and Biophysics , vol.426 , Issue.2 , pp. 163-172
    • Schnaar, R.L.1
  • 21
    • 0033597907 scopus 로고    scopus 로고
    • Glycosphingolipid-enriched signaling domain in mouse neuroblastoma Neuro2a cells. Mechanism of ganglioside-dependent neuritogenesis
    • A. Prinetti, K. Iwabuchi, and S. Hakomori Glycosphingolipid-enriched signaling domain in mouse neuroblastoma Neuro2a cells. Mechanism of ganglioside-dependent neuritogenesis Journal of Biological Chemistry 274 1999 20916 20924
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 20916-20924
    • Prinetti, A.1    Iwabuchi, K.2    Hakomori, S.3
  • 22
    • 48549100652 scopus 로고    scopus 로고
    • Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease - A review
    • T. Ariga, M.P. McDonald, and R.K. Yu Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease - a review Journal of Lipid Research 49 2008 1157 1175
    • (2008) Journal of Lipid Research , vol.49 , pp. 1157-1175
    • Ariga, T.1    McDonald, M.P.2    Yu, R.K.3
  • 25
    • 0034616635 scopus 로고    scopus 로고
    • Influence of cellular ganglioside depletion on tumor formation
    • W. Deng, R. Li, and S. Ladisch Influence of cellular ganglioside depletion on tumor formation Journal of the National Cancer Institute 92 2000 912 917 (Pubitemid 30429191)
    • (2000) Journal of the National Cancer Institute , vol.92 , Issue.11 , pp. 912-917
    • Deng, W.1    Li, R.2    Ladisch, S.3
  • 26
  • 27
    • 44649169827 scopus 로고    scopus 로고
    • Evidence for effect of GM1 on opioid peptide conformation: NMR study on leucine enkephalin in ganglioside-containing isotropic phospholipid bicelles
    • A. Gayen, and C. Mukhopadhyay Evidence for effect of GM1 on opioid peptide conformation: NMR study on leucine enkephalin in ganglioside-containing isotropic phospholipid bicelles Langmuir 24 2008 5422 5432
    • (2008) Langmuir , vol.24 , pp. 5422-5432
    • Gayen, A.1    Mukhopadhyay, C.2
  • 28
    • 78649777782 scopus 로고
    • NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles
    • A. Gayen, S.K. Goswami, and C. Mukhopadhyay NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles Biochimica et Biophysica Acta 2011 1808 127 139
    • (1808) Biochimica et Biophysica Acta , vol.2011 , pp. 127-139
    • Gayen, A.1    Goswami, S.K.2    Mukhopadhyay, C.3
  • 31
    • 69949137268 scopus 로고    scopus 로고
    • The DOSY Toolbox: A new tool for processing PFG NMR diffusion data
    • M. Nilsson The DOSY Toolbox: A new tool for processing PFG NMR diffusion data Journal of Magnetic Resonance 200 2009 296 302
    • (2009) Journal of Magnetic Resonance , vol.200 , pp. 296-302
    • Nilsson, M.1
  • 32
    • 4744352080 scopus 로고    scopus 로고
    • Amantadine partition and localization in phospholipid membrane: A solution NMR study
    • DOI 10.1016/j.bbrc.2004.09.039, PII S0006291X04020844
    • J.F. Wang, J.R. Schnell, and J.J. Chou Amantadine partition and localization in phospholipid membrane: a solution NMR study Biochemical and Biophysical Research Communications 324 2004 212 217 (Pubitemid 39311480)
    • (2004) Biochemical and Biophysical Research Communications , vol.324 , Issue.1 , pp. 212-217
    • Wang, J.1    Schnell, J.R.2    Chou, J.J.3
  • 33
    • 1542285304 scopus 로고    scopus 로고
    • 1H NMR Investigation of the Conformation of Methionine-Enkephalin in Fast-Tumbling Bicelles
    • 1H NMR Investigation of the Conformation of Methionine-Enkephalin in Fast-Tumbling Bicelles Biophysical Journal 86 2004 1587 1600 (Pubitemid 38295592)
    • (2004) Biophysical Journal , vol.86 , Issue.3 , pp. 1587-1600
    • Marcotte, I.1    Separovic, F.2    Auger, M.3    Gagne, S.M.4
  • 34
    • 0035852133 scopus 로고    scopus 로고
    • Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy
    • DOI 10.1021/ja011967l
    • S. Gaemers, and A. Bax Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy Journal of the American Chemical Society 123 2001 12343 12352 (Pubitemid 33136071)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.49 , pp. 12343-12352
    • Gaemers, S.1    Bax, A.2
  • 37
    • 0035742163 scopus 로고    scopus 로고
    • The VMD-XPLOR visualization package for NMR structure refinement
    • D. Schwieters, and G.M. Clore The VMD-XPLOR visualization package for NMR structure refinement Journal of Magnetic Resonance 149 2001 239 244
    • (2001) Journal of Magnetic Resonance , vol.149 , pp. 239-244
    • Schwieters, D.1    Clore, G.M.2
  • 39
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: Intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • DOI 10.1038/sj.cdd.4401934, PII 4401934
    • M.G. Hinds, C. Smits, R. Fredericks-Short, J.M. Risk, M. Bailey, D.C.S. Huang, and C.L. Day Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets Cell Death and Differentiation 14 2007 128 136 (Pubitemid 44911900)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.1 , pp. 128-136
    • Hinds, M.G.1    Smits, C.2    Fredericks-Short, R.3    Risk, J.M.4    Bailey, M.5    Huang, D.C.S.6    Day, C.L.7
  • 40
    • 0037159248 scopus 로고    scopus 로고
    • 10-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41
    • DOI 10.1021/bi026261y
    • 10-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41 Biochemistry 41 2002 12687 12696 (Pubitemid 35192498)
    • (2002) Biochemistry , vol.41 , Issue.42 , pp. 12687-12696
    • Biron, Z.1    Khare, S.2    Samson, A.O.3    Hayek, Y.4    Naider, F.5    Anglister, J.6
  • 41
    • 0033601232 scopus 로고    scopus 로고
    • A mixture of a-helical and 310-helical conformations for involucrin in the human epidermal corneocyte envelope provides a scaffold for the attachment of both lipids and proteins
    • N.D. Lazo, and D.T. Downing A mixture of a-helical and 310-helical conformations for involucrin in the human epidermal corneocyte envelope provides a scaffold for the attachment of both lipids and proteins Journal of Biological Chemistry 274 1999 37340 37344
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 37340-37344
    • Lazo, N.D.1    Downing, D.T.2
  • 42
    • 33845961807 scopus 로고    scopus 로고
    • Membrane interactions of dynorphins
    • DOI 10.1021/bi061199g
    • J. Lind, A. Graslund, and L. Maler Membrane interactions of dynorphins Biochemistry 45 2006 15931 15940 (Pubitemid 46032514)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15931-15940
    • Lind, J.1    Graslund, A.2    Maler, L.3
  • 43
    • 1042275571 scopus 로고    scopus 로고
    • Diffusion and dynamics of penetratin in different membrane mimicking media
    • DOI 10.1016/j.bbamem.2003.11.014
    • A. Andersson, J. Almqvist, F. Hagn, and L. Maler Diffusion and dynamics of penetratin in different membrane mimicking media Biochimica et Biophysica Acta 1661 2004 18 25 (Pubitemid 38201568)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1661 , Issue.1 , pp. 18-25
    • Andersson, A.1    Almqvist, J.2    Hagn, F.3    Maler, L.4
  • 44
    • 0036918932 scopus 로고    scopus 로고
    • Bicelles in structure-function studies of membrane-associated proteins
    • DOI 10.1016/S0045-2068(02)00527-8
    • J.A. Whiles, R. Deems, R.R. Vold, and E.A. Dennis Bicelles in structure-function studies of membrane-associated proteins Bioorganic Chemistry 30 2002 431 442 (Pubitemid 36294219)
    • (2002) Bioorganic Chemistry , vol.30 , Issue.6 , pp. 431-442
    • Whiles, J.A.1    Deems, R.2    Vold, R.R.3    Dennis, E.A.4
  • 45
    • 75149195391 scopus 로고    scopus 로고
    • Functional delivery of a membrane protein into oocyte membranes using bicelles
    • C. Kang, C.G. Vanoye, R.C. Welch, W.D. Van Horn, and C.R. Sanders Functional delivery of a membrane protein into oocyte membranes using bicelles Biochemistry 49 2010 653 655
    • (2010) Biochemistry , vol.49 , pp. 653-655
    • Kang, C.1    Vanoye, C.G.2    Welch, R.C.3    Van Horn, W.D.4    Sanders, C.R.5
  • 48
    • 0344981520 scopus 로고    scopus 로고
    • Three-Dimensional Structure of the Mammalian Tachykinin Peptide Neurokinin A Bound to Lipid Micelles
    • I.R. Chandrashekar, and S.M. Cowsik Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles Biophysical Journal 85 2003 4002 4011 (Pubitemid 37490309)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 4002-4011
    • Chandrashekar, I.R.1    Cowsik, S.M.2


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