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Volumn 63, Issue 3, 2011, Pages 206-213

Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations

Author keywords

evolution; hemeproteins; neuroglobin; protein function; protein structure; structural biology

Indexed keywords

NEUROGLOBIN;

EID: 79953252674     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.444     Document Type: Conference Paper
Times cited : (12)

References (45)
  • 1
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • Burmester, T., Weich, B., Reinhardt, S., and, Hankeln, T., (2000) A vertebrate globin expressed in the brain. Nature 407, 520-523.
    • (2000) Nature , vol.407 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 3
    • 38649090098 scopus 로고    scopus 로고
    • Neuroglobin: an endogenous neuroprotectant
    • DOI 10.1016/j.coph.2007.09.003, PII S1471489207001592
    • Greenberg, D. A., Jin, K., and, Khan, A. A., (2008) Neuroglobin: an endogenous neuroprotectant. Curr. Opin. Pharm. 8, 20-24. (Pubitemid 351168689)
    • (2008) Current Opinion in Pharmacology , vol.8 , Issue.1 , pp. 20-24
    • Greenberg, D.A.1    Jin, K.2    Khan, A.A.3
  • 5
    • 0141704224 scopus 로고    scopus 로고
    • Oxidized human neuroglobin acts as a heterotrimeric Gα protein guanine nucleotide dissociation inhibitor
    • DOI 10.1074/jbc.M305519200
    • Wakasugi, K., Nakano, T., and, Morishima, I., (2003) Oxidized human neuroglobin acts as a heterotrimeric Gα protein guanine nucleotide dissociation inhibitor. J. Biol. Chem. 278, 36505-36512. (Pubitemid 37139980)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36505-36512
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 6
    • 37649003389 scopus 로고    scopus 로고
    • Neuroglobin attenuates β amyloid neurotoxicity in vitro and transgenic Alzheimer phenotype in vivo
    • Khan, A.A., Mao, X. O., Banwait, S., Jin, K., and, Greenberg, D. A., (2007) Neuroglobin attenuates β amyloid neurotoxicity in vitro and transgenic Alzheimer phenotype in vivo. Proc. Natl. Acad. Sci. USA 104, 19114-19119.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19114-19119
    • Khan, A.A.1    Mao, X.O.2    Banwait, S.3    Jin, K.4    Greenberg, D.A.5
  • 9
    • 0041833723 scopus 로고    scopus 로고
    • Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity
    • DOI 10.1016/S0969-2126(03)00166-7
    • Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., and, Bolognesi, M., (2003) Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure 11, 1087-1095. (Pubitemid 37103070)
    • (2003) Structure , vol.11 , Issue.9 , pp. 1087-1095
    • Pesce, A.1    Dewilde, S.2    Nardini, M.3    Moens, L.4    Ascenzi, P.5    Hankeln, T.6    Burmester, T.7    Bolognesi, M.8
  • 12
  • 14
    • 59649130012 scopus 로고    scopus 로고
    • Cold-adapted Antarctic fish: The discovery of neuroglobin in the dominant suborder Notothenioidei
    • Cheng, C.-H. C., di Prisco, G., and, Verde, C., (2009a) Cold-adapted Antarctic fish: the discovery of neuroglobin in the dominant suborder Notothenioidei. Gene 433, 100-101.
    • (2009) Gene , vol.433 , pp. 100-101
    • Cheng, C.-H.C.1    Di Prisco, G.2    Verde, C.3
  • 15
    • 63449084083 scopus 로고    scopus 로고
    • The "icefish paradox". Which is the task of neuroglobin in Antarctic haemoglobin-less icefish?
    • Cheng, C.-H. C., di Prisco, G., and, Verde, C., (2009b) The "icefish paradox". Which is the task of neuroglobin in Antarctic haemoglobin-less icefish? IUBMB Life 61, 184-188.
    • (2009) IUBMB Life , vol.61 , pp. 184-188
    • Cheng, C.-H.C.1    Di Prisco, G.2    Verde, C.3
  • 16
    • 17144430126 scopus 로고    scopus 로고
    • The cellular and subcellular localization of neuroglobin and cytoglobin - A clue to their function?
    • DOI 10.1080/15216540500037794
    • Hankeln, T., Wystub, S., Laufs, T., Schmidt, M., Gerlach, F., Saaler-Reinhardt, S., Reuss, S., and, Burmester, T., (2004) The cellular and subcellular localization of neuroglobin and cytoglobinâa clue to their function? IUBMB Life 56, 671-679. (Pubitemid 40515812)
    • (2004) IUBMB Life , vol.56 , Issue.11-12 , pp. 671-679
    • Hankeln, T.1    Wystub, S.2    Laufs, T.3    Schmidt, M.4    Gerlach, F.5    Saaler-Reinhardt, S.6    Reuss, S.7    Burmester, T.8
  • 17
    • 0037449744 scopus 로고    scopus 로고
    • How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina
    • DOI 10.1074/jbc.M209909200
    • Schmidt, M., Giessl, A., Laufs, T., Hankeln, T., Wolfrum, U., and, Burmester, T., (2003) How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina. J. Biol. Chem. 278, 1932-1935. (Pubitemid 36801434)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 1932-1935
    • Schmidt, M.1    Giessl, A.2    Laufs, T.3    Hankeln, T.4    Wolfrum, U.5    Burmester, T.6
  • 20
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and, Heringa, J., (2000) T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 21
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A., and, Blundell, T. L., (1993) Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815. (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 23
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • Cheatham, T. E., III, Cieplak, P., and, Kollman, P. A., (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat. J. Biomol. Struct. Dyn. 16, 845-862. (Pubitemid 29157655)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.16 , Issue.4 , pp. 845-862
    • Cheatham III, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 26
    • 69849099148 scopus 로고    scopus 로고
    • High pressure reveals structural determinants for globin hexacoordination: Neuroglobin and myoglobin cases
    • Capece, L., Marà, M. A., Bidon-Chanal, A., Nadra, A., Luque, F.J., and, Estrin, D. A., (2009) High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases. Proteins 75, 885-894.
    • (2009) Proteins , vol.75 , pp. 885-894
    • Capece, L.1    Martaì, M.A.2    Bidon-Chanal, A.3    Nadra, A.4    Luque, F.J.5    Estrin, D.A.6
  • 27
    • 77949317319 scopus 로고    scopus 로고
    • Unraveling the molecular basis for ligand binding in truncated hemoglobins: The trHbO Bacillus subtilis case
    • Boechi, L., Mañez, P. A., Luque, F. J., Marà, M. A., and, Estrin, D. A., (2010) Unraveling the molecular basis for ligand binding in truncated hemoglobins: the trHbO Bacillus subtilis case. Proteins 78, 962-970.
    • (2010) Proteins , vol.78 , pp. 962-970
    • Boechi, L.1    Mañez, P.A.2    Luque, F.J.3    Martaì, M.A.4    Estrin, D.A.5
  • 28
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, T. E., III, DeBolt, S., Ferguson, D., Seibel, G., and, Kollman, P., (1995) AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun. 91, 1-41.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham Iii, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 30
    • 34447299690 scopus 로고    scopus 로고
    • Molecular dynamics simulation of deoxy and carboxy murine neuroglobin in water
    • DOI 10.1529/biophysj.106.099648
    • Anselmi, M., Brunori, M., Vallone, B., and, Di Nola, A., (2007) Molecular dynamics simulation of deoxy and carboxy murine neuroglobin in water. Biophys. J. 93, 434-441. (Pubitemid 47057810)
    • (2007) Biophysical Journal , vol.93 , Issue.2 , pp. 434-441
    • Anselmi, M.1    Brunori, M.2    Vallone, B.3    Di Nola, A.4
  • 31
    • 77955199850 scopus 로고    scopus 로고
    • Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin
    • Astudillo, L., Bernad, S., Derrien, V., Sebban, P., and, Miksovska, J., (2010) Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin. Bioph. J. 99, L16-L18.
    • (2010) Bioph. J. , vol.99
    • Astudillo, L.1    Bernad, S.2    Derrien, V.3    Sebban, P.4    Miksovska, J.5
  • 32
    • 0035929255 scopus 로고    scopus 로고
    • Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis
    • DOI 10.1006/bbrc.2001.5614
    • Awenius, C., Hankeln, T., and, Burmester, T., (2001) Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis. Biochem. Biophys. Res. Commun. 287, 418-21. (Pubitemid 32917614)
    • (2001) Biochemical and Biophysical Research Communications , vol.287 , Issue.2 , pp. 418-421
    • Awenius, C.1    Hankeln, T.2    Burmester, T.3
  • 34
    • 12944327813 scopus 로고    scopus 로고
    • The nature of the diversity of Antarctic fishes
    • DOI 10.1007/s00300-004-0667-4
    • Eastman, J. T., (2005) The nature of the diversity of Antarctic fishes. Polar Biol. 28, 93-107. (Pubitemid 40171914)
    • (2005) Polar Biology , vol.28 , Issue.2 , pp. 93-107
    • Eastman, J.T.1
  • 36
    • 0037036931 scopus 로고    scopus 로고
    • Tracking the evolutionary loss of hemoglobin expression by the white-blooded Antarctic icefishes
    • DOI 10.1016/S0378-1119(02)00691-1, PII S0378111902006911
    • di Prisco, G., Cocca, E., Parker, S. K., and, Detrich, H. W., III., (2002) Tracking the evolutionary loss of hemoglobin expression by the white-blooded Antarctic icefishes. Gene 295, 185-191. (Pubitemid 35279250)
    • (2002) Gene , vol.295 , Issue.2 , pp. 185-191
    • Di Prisco, G.1    Cocca, E.2    Parker, S.K.3    Detrich III, H.W.4
  • 37
    • 33749574079 scopus 로고    scopus 로고
    • A genomic fossil reveals key steps in hemoglobin loss by the Antarctic icefishes
    • DOI 10.1093/molbev/msl071
    • Near, T. J., Parker, S. W., and, Detrich, H. W., III., (2006) A Genomic fossil reveals key steps in hemoglobin loss by the Antarctic icefishes. Mol. Biol. Evol. 23, 2008-2016. (Pubitemid 44536810)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.11 , pp. 2008-2016
    • Near, T.J.1    Parker, S.K.2    Detrich III, H.W.3
  • 38
    • 33745651826 scopus 로고    scopus 로고
    • When bad things happen to good fish: The loss of hemoglobin and myoglobin expression in Antarctic icefishes
    • DOI 10.1242/jeb.02091
    • Sidell, B. D., and, O'Brien K. M., (2006) When bad thing happen to good fish: the loss of hemoglobin and myoglobin expression in Antarctic icefishes. J. Exp. Biol. 209, 1791-1802. (Pubitemid 43965856)
    • (2006) Journal of Experimental Biology , vol.209 , Issue.10 , pp. 1791-1802
    • Sidell, B.D.1    O'Brien, K.M.2
  • 39
    • 0036339668 scopus 로고    scopus 로고
    • Peripheral oxygen transport in skeletal muscle of Antarctic and sub-Antarctic notothenioid fish
    • Egginton, S., Skilbeck, C., Hoofd, L., Calvo, J., and, Johnston, I. A., (2002) Peripheral oxygen transport in skeletal muscle of Antarctic and sub-Antarctic notothenioid fish. J. Exp. Biol. 205, 769-779. (Pubitemid 34861244)
    • (2002) Journal of Experimental Biology , vol.205 , Issue.6 , pp. 769-779
    • Egginton, S.1    Skilbeck, C.2    Hoofd, L.3    Calvo, J.4    Johnston, I.A.5
  • 40
    • 77953024975 scopus 로고    scopus 로고
    • Relationship among circulating hemoglobin, nitric oxide synthase activities and angiogenic poise in red- and white-blooded Antarctic notothenioid fishes
    • Beers, J. M., Borley, K. A., and, Sidell, B. D., (2010) Relationship among circulating hemoglobin, nitric oxide synthase activities and angiogenic poise in red- and white-blooded Antarctic notothenioid fishes. Comp. Biochem Physiol A Mol. Integr. Physiol. 156, 422-429.
    • (2010) Comp. Biochem Physiol A Mol. Integr. Physiol. , vol.156 , pp. 422-429
    • Beers, J.M.1    Borley, K.A.2    Sidell, B.D.3
  • 41
    • 43249104256 scopus 로고    scopus 로고
    • Zebrafish neuroglobin is a cell-membrane-penetrating globin
    • DOI 10.1021/bi800286m
    • Watanabe, S., and, Wakasugi, K., (2008) Zebrafish neuroglobin is a cell-membrane-penetrating globin. Biochemistry 47, 5266-5270. (Pubitemid 351656970)
    • (2008) Biochemistry , vol.47 , Issue.19 , pp. 5266-5270
    • Watanabe, S.1    Wakasugi, K.2
  • 42
    • 37649012488 scopus 로고    scopus 로고
    • Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy
    • Ishikawa, H., Kim, S., Kwak, K., Wakasugi, K., and, Fayer, M. D., (2007) Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy. Proc. Natl. Acad. Sci. USA 104, 19309-19314.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19309-19314
    • Ishikawa, H.1    Kim, S.2    Kwak, K.3    Wakasugi, K.4    Fayer, M.D.5
  • 45
    • 77649199218 scopus 로고    scopus 로고
    • The physiology of climate change: How potentials for acclimatization and genetic adaptation will determine winners and losers
    • Somero, G. N., (2010) The physiology of climate change: how potentials for acclimatization and genetic adaptation will determine winners and losers. J. Exp. Biol. 213, 912-920.
    • (2010) J. Exp. Biol. , vol.213 , pp. 912-920
    • Somero, G.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.