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Volumn 21, Issue 5, 2010, Pages 1117-1129

Merging structural biology with chemical biology: Structural Chemistry at Eskitis

Author keywords

Molecular mechanisms; Protein crystallography; Protein structure function; Rational drug design

Indexed keywords


EID: 77956872162     PISSN: 10400400     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11224-010-9654-2     Document Type: Review
Times cited : (10)

References (96)
  • 1
    • 0036173404 scopus 로고    scopus 로고
    • PCSB-a program collection for structural biology and biophysical chemistry
    • Hofmann A, Wlodawer A (2002) PCSB-a program collection for structural biology and biophysical chemistry. Bioinformatics 18: 209-210.
    • (2002) Bioinformatics , vol.18 , pp. 209-210
    • Hofmann, A.1    Wlodawer, A.2
  • 2
    • 58249110492 scopus 로고    scopus 로고
    • ACDP-a Java application for data processing and analysis of protein circular dichroism spectra
    • Hofmann A (2008) ACDP-a Java application for data processing and analysis of protein circular dichroism spectra. J Appl Crystallogr 42: 137-139.
    • (2008) J Appl Crystallogr , vol.42 , pp. 137-139
    • Hofmann, A.1
  • 3
    • 11144341956 scopus 로고    scopus 로고
    • Chemical space and biology
    • Dobson CM (2004) Chemical space and biology. Nature 432: 824-828.
    • (2004) Nature , vol.432 , pp. 824-828
    • Dobson, C.M.1
  • 4
    • 14144254396 scopus 로고    scopus 로고
    • Creating small-molecule-dependent switches to modulate biological functions
    • Buskirk AR, Liu DR (2005) Creating small-molecule-dependent switches to modulate biological functions. Chem Biol 12: 151-161.
    • (2005) Chem Biol , vol.12 , pp. 151-161
    • Buskirk, A.R.1    Liu, D.R.2
  • 5
    • 11144298973 scopus 로고    scopus 로고
    • Exploring biology with small organic molecules
    • Stockwell BR (2004) Exploring biology with small organic molecules. Nature 432: 846-854.
    • (2004) Nature , vol.432 , pp. 846-854
    • Stockwell, B.R.1
  • 6
    • 0030039619 scopus 로고    scopus 로고
    • The art and practice of structure-based drug design: a molecular modeling perspective
    • Bohacek RS, McMartin C, Guida WC (1996) The art and practice of structure-based drug design: a molecular modeling perspective. Med Res Rev 16: 3-50.
    • (1996) Med Res Rev , vol.16 , pp. 3-50
    • Bohacek, R.S.1    McMartin, C.2    Guida, W.C.3
  • 7
    • 0344515366 scopus 로고    scopus 로고
    • Diversity-oriented synthesis; a challenge for synthetic chemists
    • Spring DR (2003) Diversity-oriented synthesis; a challenge for synthetic chemists. Org Biomol Chem 1: 3867-3870.
    • (2003) Org Biomol Chem , vol.1 , pp. 3867-3870
    • Spring, D.R.1
  • 8
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman DJ, Cragg GM (2007) Natural products as sources of new drugs over the last 25 years. J Nat Prod 70: 461-477.
    • (2007) J Nat Prod , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 9
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C, Lombardo F, Dominy B, Feeney P (1997) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 23: 3-25.
    • (1997) Adv Drug Deliv Rev , vol.23 , pp. 3-25
    • Lipinski, C.1    Lombardo, F.2    Dominy, B.3    Feeney, P.4
  • 10
    • 13344282654 scopus 로고    scopus 로고
    • Drug-like properties: guiding principles for design-or chemical prejudice?
    • Leeson P, Davis A, Steele J (2004) Drug-like properties: guiding principles for design-or chemical prejudice? Drug Discov Today Technol 1: 189-195.
    • (2004) Drug Discov Today Technol , vol.1 , pp. 189-195
    • Leeson, P.1    Davis, A.2    Steele, J.3
  • 12
    • 2942564021 scopus 로고    scopus 로고
    • Pursuing the leadlikeness concept in pharmaceutical research
    • Hann MM, Oprea TI (2004) Pursuing the leadlikeness concept in pharmaceutical research. Curr Opin Chem Biol 8: 255-263.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 255-263
    • Hann, M.M.1    Oprea, T.I.2
  • 13
    • 9744232909 scopus 로고    scopus 로고
    • Time-related differences in the physical property profiles of oral drugs
    • Leeson PD, Davis AM (2004) Time-related differences in the physical property profiles of oral drugs. J Med Chem 47: 6338-6348.
    • (2004) J Med Chem , vol.47 , pp. 6338-6348
    • Leeson, P.D.1    Davis, A.M.2
  • 14
    • 44949134801 scopus 로고    scopus 로고
    • The impact of natural products upon modern drug discovery
    • Ganesan A (2008) The impact of natural products upon modern drug discovery. Curr Opin Chem Biol 12: 306-317.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 306-317
    • Ganesan, A.1
  • 15
    • 11144320699 scopus 로고    scopus 로고
    • Navigating chemical space for biology and medicine
    • Lipinski CA, Hopkins A (2004) Navigating chemical space for biology and medicine. Nature 432: 855-861.
    • (2004) Nature , vol.432 , pp. 855-861
    • Lipinski, C.A.1    Hopkins, A.2
  • 16
    • 1842532337 scopus 로고    scopus 로고
    • Chemogenomics: an emerging strategy for rapid target and drug discovery
    • Bredel M, Jacoby E (2004) Chemogenomics: an emerging strategy for rapid target and drug discovery. Nat Rev Genet 5: 262-275.
    • (2004) Nat Rev Genet , vol.5 , pp. 262-275
    • Bredel, M.1    Jacoby, E.2
  • 18
    • 20444455036 scopus 로고    scopus 로고
    • Target-family-oriented focused libraries for kinases-conceptual design aspects and commercial availability
    • Prien O (2005) Target-family-oriented focused libraries for kinases-conceptual design aspects and commercial availability. ChemBioChem 6: 500-505.
    • (2005) ChemBioChem , vol.6 , pp. 500-505
    • Prien, O.1
  • 19
    • 12344257734 scopus 로고    scopus 로고
    • Target-based compound library design and synthesis
    • Player MR (2004) Target-based compound library design and synthesis. Drug Discov Today Targets 3: 48-50.
    • (2004) Drug Discov Today Targets , vol.3 , pp. 48-50
    • Player, M.R.1
  • 21
    • 0142147275 scopus 로고    scopus 로고
    • Generating diverse skeletons of small molecules combinatorially
    • Burke MD, Berger EM, Schreiber SL (2003) Generating diverse skeletons of small molecules combinatorially. Science 302: 613-618.
    • (2003) Science , vol.302 , pp. 613-618
    • Burke, M.D.1    Berger, E.M.2    Schreiber, S.L.3
  • 22
    • 20444383539 scopus 로고    scopus 로고
    • Assessment of structural diversity in combinatorial synthesis
    • Fergus S, Bender A, Spring DR (2005) Assessment of structural diversity in combinatorial synthesis. Curr Opin Chem Biol 9: 304-309.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 304-309
    • Fergus, S.1    Bender, A.2    Spring, D.R.3
  • 23
    • 34247526874 scopus 로고    scopus 로고
    • Establishment of an open access compound management facility in Australia to stimulate applied, basic and translational biomedical research
    • Camp D (2007) Establishment of an open access compound management facility in Australia to stimulate applied, basic and translational biomedical research. Drug Discov World 8: 61-66.
    • (2007) Drug Discov World , vol.8 , pp. 61-66
    • Camp, D.1
  • 24
    • 38649136965 scopus 로고    scopus 로고
    • Progress towards establishing an open access molecular screening capability in the Australasian region
    • Camp D, Avery VM, Street I, Quinn RJ (2007) Progress towards establishing an open access molecular screening capability in the Australasian region. ACS Chem Biol 2: 764-767.
    • (2007) ACS Chem Biol , vol.2 , pp. 764-767
    • Camp, D.1    Avery, V.M.2    Street, I.3    Quinn, R.J.4
  • 25
    • 69949158926 scopus 로고    scopus 로고
    • Antimalarial activity of azafluorenone alkaloids from the Australian tree Mitrephora diversifolia
    • Mueller D, Davis RA, Duffy S, Avery VM, Camp D, Quinn RJ (2009) Antimalarial activity of azafluorenone alkaloids from the Australian tree Mitrephora diversifolia. J Nat Prod 72: 1538-1540.
    • (2009) J Nat Prod , vol.72 , pp. 1538-1540
    • Mueller, D.1    Davis, R.A.2    Duffy, S.3    Avery, V.M.4    Camp, D.5    Quinn, R.J.6
  • 26
    • 72149105588 scopus 로고    scopus 로고
    • (+)-7-Bromotrypargine, an antimalarial beta-carboline from the Australian marine Sponge, Ancorina sp
    • Davis RA, Duffy S, Avery VM, Camp D, Hooper JNA, Quinn RJ (2010) (+)-7-Bromotrypargine, an antimalarial beta-carboline from the Australian marine Sponge, Ancorina sp. Tetrahedron Lett 51: 583-585.
    • (2010) Tetrahedron Lett , vol.51 , pp. 583-585
    • Davis, R.A.1    Duffy, S.2    Avery, V.M.3    Camp, D.4    Hooper, J.N.A.5    Quinn, R.J.6
  • 27
    • 77951605067 scopus 로고    scopus 로고
    • Antitrypanosomal cyclic polyketide peroxides from the Australian marine sponge Plakortis sp
    • Feng Y, Davis RA, Sykes ML, Avery VM, Camp D, Quinn RJ (2010) Antitrypanosomal cyclic polyketide peroxides from the Australian marine sponge Plakortis sp. J Nat Prod 73: 716-719.
    • (2010) J Nat Prod , vol.73 , pp. 716-719
    • Feng, Y.1    Davis, R.A.2    Sykes, M.L.3    Avery, V.M.4    Camp, D.5    Quinn, R.J.6
  • 30
    • 70350072336 scopus 로고    scopus 로고
    • S-glycosyl primary sulfonamides-a new structural class for selective inhibition of cancer-associated carbonic anhydrases
    • Lopez M, Paul B, Hofmann A, Innocenti A, Vullo D, Supuran C, Poulsen S (2009) S-glycosyl primary sulfonamides-a new structural class for selective inhibition of cancer-associated carbonic anhydrases. J Med Chem 52: 6421-6432.
    • (2009) J Med Chem , vol.52 , pp. 6421-6432
    • Lopez, M.1    Paul, B.2    Hofmann, A.3    Innocenti, A.4    Vullo, D.5    Supuran, C.6    Poulsen, S.7
  • 31
    • 33845687339 scopus 로고    scopus 로고
    • New anthelmintics for livestock: the time is right
    • Besier B (2007) New anthelmintics for livestock: the time is right. Trends Parasitol 23: 21-24.
    • (2007) Trends Parasitol , vol.23 , pp. 21-24
    • Besier, B.1
  • 32
    • 70849098084 scopus 로고    scopus 로고
    • Where are the parasites?
    • Kutz S, Dobson A, Hoberg E (2009) Where are the parasites? Science 326: 1187-1188.
    • (2009) Science , vol.326 , pp. 1187-1188
    • Kutz, S.1    Dobson, A.2    Hoberg, E.3
  • 34
    • 0023885305 scopus 로고
    • The protein kinase family: conserved features and deduced phylogeny of the catalytic domains
    • Hanks SK, Quinn AM, Hunter T (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241: 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 35
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: insights into catalysis and regulation
    • Barford D, Das A, Egloff M (1998) The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct 27: 133-164.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.2    Egloff, M.3
  • 36
    • 34548770004 scopus 로고    scopus 로고
    • Trichostrongylus vitrinus (Nematoda: Strongylida): molecular characterisation and transcriptional analysis of Tv-stp-1, a serine/threonine phosphatase gene
    • Hu M, Abs El-Osta YG, Campbell BE, Boag PR, Nisbet AJ, Beveridge I, Gasser RB (2007) Trichostrongylus vitrinus (Nematoda: Strongylida): molecular characterisation and transcriptional analysis of Tv-stp-1, a serine/threonine phosphatase gene. Exp Parasitol 117: 22-34.
    • (2007) Exp Parasitol , vol.117 , pp. 22-34
    • Hu, M.1    Abs El-Osta, Y.G.2    Campbell, B.E.3    Boag, P.R.4    Nisbet, A.J.5    Beveridge, I.6    Gasser, R.B.7
  • 37
    • 77954382782 scopus 로고    scopus 로고
    • Campbell B, Rabelo E, Hofmann A, Hu M, Gasser R (2010) Characterization of a Caenorhabditis elegans glc seven-like phosphatase (gsp) orthologue from Haemonchus contortus (Nematoda). Mol Cell Probes (in press).
  • 38
    • 77956877912 scopus 로고    scopus 로고
    • Campbell BE, McCluskey A, Hofmann A, Gasser R (2010) Serine/threonine phosphatases in socioeconomically important parasitic nematodes-prospects as novel drug targets? Biotechnol Adv (in press).
  • 39
    • 77956058090 scopus 로고    scopus 로고
    • Nolan MJ, Hofmann A, Jex AR, Gasser RB (2010) A theoretical study to establish the relationship between the three-dimensional structure of triose-phosphate isomerase of Giardia duodenalis and point mutations in the respective gene. Mol Cell Probes (in press).
  • 41
    • 0028020563 scopus 로고
    • Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18
    • Muchowski PJ, Zhang L, Chang ER, Soule HR, Plow EF, Moyle M (1994) Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18. J Biol Chem 269: 26419-26423.
    • (1994) J Biol Chem , vol.269 , pp. 26419-26423
    • Muchowski, P.J.1    Zhang, L.2    Chang, E.R.3    Soule, H.R.4    Plow, E.F.5    Moyle, M.6
  • 42
    • 13844275516 scopus 로고    scopus 로고
    • X-ray structure of Na-ASP-2, a pathogenesis-related-1 protein from the nematode parasite, Necator americanus, and a vaccine antigen for human hookworm infection
    • Asojo OA, Goud G, Dhar K, Loukas A, Zhan B, Deumic V, Liu S, Borgstahl GEO, Hotez PJ (2005) X-ray structure of Na-ASP-2, a pathogenesis-related-1 protein from the nematode parasite, Necator americanus, and a vaccine antigen for human hookworm infection. J Mol Biol 346: 801-814.
    • (2005) J Mol Biol , vol.346 , pp. 801-814
    • Asojo, O.A.1    Goud, G.2    Dhar, K.3    Loukas, A.4    Zhan, B.5    Deumic, V.6    Liu, S.7    Borgstahl, G.E.O.8    Hotez, P.J.9
  • 45
    • 0034669054 scopus 로고    scopus 로고
    • Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction
    • Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A (2000) Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction. EMBO J 19: 6207-6217.
    • (2000) EMBO J , vol.19 , pp. 6207-6217
    • Hofmann, A.1    Zdanov, A.2    Genschik, P.3    Ruvinov, S.4    Filipowicz, W.5    Wlodawer, A.6
  • 46
    • 28944436002 scopus 로고    scopus 로고
    • Structural conservation and functional versatility: allostery as a common annexin feature
    • J. Bandorowicz-Pikula (Ed.), Georgetown: Landes Bioscience
    • Hofmann A, Huber R (2003) Structural conservation and functional versatility: allostery as a common annexin feature. In: Bandorowicz-Pikula J (ed) Annexins: biological importance and annexin-related pathologies. Landes Bioscience, Georgetown.
    • (2003) Annexins: Biological Importance and Annexin-Related Pathologies
    • Hofmann, A.1    Huber, R.2
  • 47
    • 0027145153 scopus 로고
    • The crystal structure of a new high-calcium form of annexin V
    • Sopkova J, Renouard M, Lewit-Bentley A (1993) The crystal structure of a new high-calcium form of annexin V. J Mol Biol 234: 816-825.
    • (1993) J Mol Biol , vol.234 , pp. 816-825
    • Sopkova, J.1    Renouard, M.2    Lewit-Bentley, A.3
  • 48
    • 33947595016 scopus 로고    scopus 로고
    • Apo and calcium-bound crystal structures of alpha-11 giardin, an unusual annexin from Giardia lamblia
    • Pathuri P, Nguyen ET, Svard SG, Luecke H (2007) Apo and calcium-bound crystal structures of alpha-11 giardin, an unusual annexin from Giardia lamblia. J Mol Biol 368: 493-508.
    • (2007) J Mol Biol , vol.368 , pp. 493-508
    • Pathuri, P.1    Nguyen, E.T.2    Svard, S.G.3    Luecke, H.4
  • 49
    • 58149333150 scopus 로고    scopus 로고
    • Apo and calcium-bound crystal structures of cytoskeletal protein alpha-14 giardin (annexin E1) from the intestinal protozoan parasite Giardia lamblia
    • Pathuri P, Nguyen ET, Ozorowski G, Svärd SG, Luecke H (2009) Apo and calcium-bound crystal structures of cytoskeletal protein alpha-14 giardin (annexin E1) from the intestinal protozoan parasite Giardia lamblia. J Mol Biol 385: 1098-1112.
    • (2009) J Mol Biol , vol.385 , pp. 1098-1112
    • Pathuri, P.1    Nguyen, E.T.2    Ozorowski, G.3    Svärd, S.G.4    Luecke, H.5
  • 50
    • 28944433676 scopus 로고    scopus 로고
    • Annexins in the plant kingdom-perspectives and potentials
    • Hofmann A (2004) Annexins in the plant kingdom-perspectives and potentials. Annexins 1: 51-61.
    • (2004) Annexins , vol.1 , pp. 51-61
    • Hofmann, A.1
  • 52
    • 49649087001 scopus 로고    scopus 로고
    • The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum indicates different mechanisms of membrane binding in plant and animal annexins
    • Hu N, Yusof A, Winter A, Osman A, Reeve A, Hofmann A (2008) The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum indicates different mechanisms of membrane binding in plant and animal annexins. J Biol Chem 283: 18314-18322.
    • (2008) J Biol Chem , vol.283 , pp. 18314-18322
    • Hu, N.1    Yusof, A.2    Winter, A.3    Osman, A.4    Reeve, A.5    Hofmann, A.6
  • 53
    • 33745619239 scopus 로고    scopus 로고
    • Biochemical characterization of annexin B1 from Cysticercus cellulosae
    • Winter A, Yusof AM, Gao E, Yan HL, Hofmann A (2006) Biochemical characterization of annexin B1 from Cysticercus cellulosae. FEBS J 273: 3238-3247.
    • (2006) FEBS J , vol.273 , pp. 3238-3247
    • Winter, A.1    Yusof, A.M.2    Gao, E.3    Yan, H.L.4    Hofmann, A.5
  • 54
    • 0025292330 scopus 로고
    • Purification and characterization of six annexins from human placenta
    • Römisch J, Heimburger N (1990) Purification and characterization of six annexins from human placenta. Biol Chem Hoppe Seyler 371: 383-388.
    • (1990) Biol Chem Hoppe Seyler , vol.371 , pp. 383-388
    • Römisch, J.1    Heimburger, N.2
  • 55
    • 0141867659 scopus 로고    scopus 로고
    • Characterisation of alpha-1 giardin: an immunodominant Giardia lamblia annexin with glycosaminoglycan-binding activity
    • Weiland M, Palm J, Griffiths W, McCaffery J, Svärd S (2003) Characterisation of alpha-1 giardin: an immunodominant Giardia lamblia annexin with glycosaminoglycan-binding activity. Int J Parasitol 33: 1341-1351.
    • (2003) Int J Parasitol , vol.33 , pp. 1341-1351
    • Weiland, M.1    Palm, J.2    Griffiths, W.3    McCaffery, J.4    Svärd, S.5
  • 56
    • 0035148547 scopus 로고    scopus 로고
    • Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surface
    • Capila I, Hernaiz M, Mo Y, Mealy T, Campos B, Dedman J, Linhardt R, Seaton B (2001) Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surface. Structure 9: 57-64.
    • (2001) Structure , vol.9 , pp. 57-64
    • Capila, I.1    Hernaiz, M.2    Mo, Y.3    Mealy, T.4    Campos, B.5    Dedman, J.6    Linhardt, R.7    Seaton, B.8
  • 57
    • 77958184452 scopus 로고    scopus 로고
    • Hofmann A, Osman A, Leow CY, Driguez P, Jones M (2010) Parasite annexins-new molecules with potential for drug and vaccine development. BioEssays (in press).
  • 58
    • 0030700864 scopus 로고    scopus 로고
    • Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor
    • Kaneko N, Ago H, Matsuda R, Inagaki E, Miyano M (1997) Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor. J Mol Biol 274: 16-20.
    • (1997) J Mol Biol , vol.274 , pp. 16-20
    • Kaneko, N.1    Ago, H.2    Matsuda, R.3    Inagaki, E.4    Miyano, M.5
  • 60
    • 1942486365 scopus 로고    scopus 로고
    • Annexin 1: more than an anti-phospholipase protein
    • Parente L, Solito E (2004) Annexin 1: more than an anti-phospholipase protein. Inflamm Res 53: 125-132.
    • (2004) Inflamm Res , vol.53 , pp. 125-132
    • Parente, L.1    Solito, E.2
  • 61
    • 0026762751 scopus 로고
    • Annexin I-mediated vesicular aggregation: mechanism and role in human neutrophils
    • Meers P, Mealy T, Pavlotsky N, Tauber AI (1992) Annexin I-mediated vesicular aggregation: mechanism and role in human neutrophils. Biochemistry 31: 6372-6382.
    • (1992) Biochemistry , vol.31 , pp. 6372-6382
    • Meers, P.1    Mealy, T.2    Pavlotsky, N.3    Tauber, A.I.4
  • 63
    • 65249168645 scopus 로고    scopus 로고
    • Annexin I and annexin II n-terminal peptides binding to s100 protein family members: specificity and thermodynamic characterization
    • Streicher WW, Lopez MM, Makhatadze GI (2009) Annexin I and annexin II n-terminal peptides binding to s100 protein family members: specificity and thermodynamic characterization. Biochemistry 48: 2788-2798.
    • (2009) Biochemistry , vol.48 , pp. 2788-2798
    • Streicher, W.W.1    Lopez, M.M.2    Makhatadze, G.I.3
  • 64
    • 41449095709 scopus 로고    scopus 로고
    • Membrane-induced folding and structure of membrane-bound annexin A1 N-terminal peptides-implications for annexin-induced membrane aggregation
    • Hu N, Bradshaw J, Lauter H, Buckingham J, Solito E, Hofmann A (2008) Membrane-induced folding and structure of membrane-bound annexin A1 N-terminal peptides-implications for annexin-induced membrane aggregation. Biophys J 94: 1773-1781.
    • (2008) Biophys J , vol.94 , pp. 1773-1781
    • Hu, N.1    Bradshaw, J.2    Lauter, H.3    Buckingham, J.4    Solito, E.5    Hofmann, A.6
  • 65
    • 33847103184 scopus 로고    scopus 로고
    • Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling
    • Burgoyne R (2007) Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling. Nat Rev Neurosci 8: 182-193.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 182-193
    • Burgoyne, R.1
  • 66
    • 0035959948 scopus 로고    scopus 로고
    • Regulated expression of the neuronal calcium sensor-1 gene during long-term potentiation in the dentate gyrus in vivo
    • Genin A, Davis S, Meziane H, Doyere V, Jeromin A, Roder J, Mallet J, Laroche S (2001) Regulated expression of the neuronal calcium sensor-1 gene during long-term potentiation in the dentate gyrus in vivo. Neuroscience 106: 571-577.
    • (2001) Neuroscience , vol.106 , pp. 571-577
    • Genin, A.1    Davis, S.2    Meziane, H.3    Doyere, V.4    Jeromin, A.5    Roder, J.6    Mallet, J.7    Laroche, S.8
  • 67
    • 0037401498 scopus 로고    scopus 로고
    • Group I mGlu receptors regulate the expression of the neuronal calcium sensor protein VILIP-1 in vitro and in vivo: implications for mGlu receptor-dependent hippocampal plasticity
    • Braunewell K, Brackmann M, Manahan-Vaughan D (2003) Group I mGlu receptors regulate the expression of the neuronal calcium sensor protein VILIP-1 in vitro and in vivo: implications for mGlu receptor-dependent hippocampal plasticity. Neuropharmacology 44: 707-715.
    • (2003) Neuropharmacology , vol.44 , pp. 707-715
    • Braunewell, K.1    Brackmann, M.2    Manahan-Vaughan, D.3
  • 68
    • 0036813090 scopus 로고    scopus 로고
    • Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor
    • Kabbani N, Negyessy L, Lin R, Goldman-Rakic P, Levenson R (2002) Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor. J Neurosci 22: 8476-8486.
    • (2002) J Neurosci , vol.22 , pp. 8476-8486
    • Kabbani, N.1    Negyessy, L.2    Lin, R.3    Goldman-Rakic, P.4    Levenson, R.5
  • 69
    • 0038377518 scopus 로고    scopus 로고
    • IL1 receptor accessory protein like, a protein involved in X-linked mental retardation, interacts with Neuronal Calcium Sensor-1 and regulates exocytosis
    • Bahi N, Friocourt G, Carrié A, Graham ME, Weiss JL, Chafey P, Fauchereau F, Burgoyne RD, Chelly J (2003) IL1 receptor accessory protein like, a protein involved in X-linked mental retardation, interacts with Neuronal Calcium Sensor-1 and regulates exocytosis. Hum Mol Genet 12: 1415-1425.
    • (2003) Hum Mol Genet , vol.12 , pp. 1415-1425
    • Bahi, N.1    Friocourt, G.2    Carrié, A.3    Graham, M.E.4    Weiss, J.L.5    Chafey, P.6    Fauchereau, F.7    Burgoyne, R.D.8    Chelly, J.9
  • 71
    • 0042515289 scopus 로고    scopus 로고
    • Overexpression of the calcium sensor visinin-like protein-1 leads to a cAMP-mediated decrease of in vivo and in vitro growth and invasiveness of squamous cell carcinoma cells
    • Mahloogi H, Gonzalez-Guerrico AM, Lopez De Cicco R, Bassi DE, Goodrow T, Braunewell KH, Klein-Szanto AJ (2003) Overexpression of the calcium sensor visinin-like protein-1 leads to a cAMP-mediated decrease of in vivo and in vitro growth and invasiveness of squamous cell carcinoma cells. Cancer Res 63: 4997-5004.
    • (2003) Cancer Res , vol.63 , pp. 4997-5004
    • Mahloogi, H.1    Gonzalez-Guerrico, A.M.2    de cicco, L.R.3    Bassi, D.E.4    Goodrow, T.5    Braunewell, K.H.6    Klein-Szanto, A.J.7
  • 72
    • 33845313646 scopus 로고    scopus 로고
    • PI(3, 4, 5)P3 and PI(4, 5)P2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo WD, Inoue T, Park WS, Kim ML, Park BO, Wandless TJ, Meyer T (2006) PI(3, 4, 5)P3 and PI(4, 5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314: 1458-1461.
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1    Inoue, T.2    Park, W.S.3    Kim, M.L.4    Park, B.O.5    Wandless, T.J.6    Meyer, T.7
  • 73
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: complex roles at the cell surface
    • Czech MP (2000) PIP2 and PIP3: complex roles at the cell surface. Cell 100: 603-606.
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 74
    • 77956871673 scopus 로고    scopus 로고
    • Tang K, Hofmann A, Freund C, Danker K (2009) The cytoplasmic tail of the alpha1 integrin subunit associates with phosphoinositides. Submitted.
  • 75
    • 27444440907 scopus 로고    scopus 로고
    • High-affinity interaction of the N-terminal myristoylation motif of the neuronal calcium sensor protein hippocalcin with phosphatidylinositol 4,5-bisphosphate
    • O'Callaghan DW, Haynes LP, Burgoyne RD (2005) High-affinity interaction of the N-terminal myristoylation motif of the neuronal calcium sensor protein hippocalcin with phosphatidylinositol 4, 5-bisphosphate. Biochem J 391: 231-238.
    • (2005) Biochem J , vol.391 , pp. 231-238
    • O'Callaghan, D.W.1    Haynes, L.P.2    Burgoyne, R.D.3
  • 76
    • 73949123049 scopus 로고    scopus 로고
    • VILIP-1, a novel regulator of the guanylate cyclase transduction system in neurons
    • Braunewell KH, Brackmann M, Hofmann A (2006) VILIP-1, a novel regulator of the guanylate cyclase transduction system in neurons. Calcium Bind Proteins 1: 12-15.
    • (2006) Calcium Bind Proteins , vol.1 , pp. 12-15
    • Braunewell, K.H.1    Brackmann, M.2    Hofmann, A.3
  • 77
    • 33947627759 scopus 로고    scopus 로고
    • Structure, function and expression of members of the vilip (visinin-like protein) subfamily of neuronal calcium sensor proteins
    • P. Philippov and K. Koch (Eds.), Hauppauge: Nova Science Publisher
    • Brackmann M, Hofmann A, Braunewell KH (2006) Structure, function and expression of members of the vilip (visinin-like protein) subfamily of neuronal calcium sensor proteins. In: Philippov P, Koch K (eds) Neuronal calcium sensor proteins. Nova Science Publisher, Hauppauge.
    • (2006) Neuronal Calcium Sensor Proteins
    • Brackmann, M.1    Hofmann, A.2    Braunewell, K.H.3
  • 79
    • 0035903111 scopus 로고    scopus 로고
    • Identification of proximate regions in a complex of retinal guanylyl cyclase 1 and guanylyl cyclase-activating protein-1 by a novel mass spectrometry-based method
    • Krylov D, Hurley J (2001) Identification of proximate regions in a complex of retinal guanylyl cyclase 1 and guanylyl cyclase-activating protein-1 by a novel mass spectrometry-based method. J Biol Chem 276: 30648-30654.
    • (2001) J Biol Chem , vol.276 , pp. 30648-30654
    • Krylov, D.1    Hurley, J.2
  • 80
    • 61449093805 scopus 로고    scopus 로고
    • Regulatory elements and functional implication for the formation of dimeric visinin-like protein-1
    • Chen K, Wang L, Chang L (2009) Regulatory elements and functional implication for the formation of dimeric visinin-like protein-1. J Pept Sci 15: 89-94.
    • (2009) J Pept Sci , vol.15 , pp. 89-94
    • Chen, K.1    Wang, L.2    Chang, L.3
  • 81
    • 70349424226 scopus 로고    scopus 로고
    • Coronin structure and implications
    • C. Clemen, L. Eichinger, and V. Rybakin (Eds.), Austin: Landes Bioscience
    • McArdle B, Hofmann A (2008) Coronin structure and implications. In: Clemen C, Eichinger L, Rybakin V (eds) The coronin family of proteins. Landes Bioscience, Austin.
    • (2008) The Coronin Family of Proteins
    • McArdle, B.1    Hofmann, A.2
  • 82
    • 58149164565 scopus 로고    scopus 로고
    • Phylogenetic, structural and functional relationships between WD- and Kelch-repeat proteins
    • Hudson AM, Cooley L (2008) Phylogenetic, structural and functional relationships between WD- and Kelch-repeat proteins. Subcell Biochem 48: 6-19.
    • (2008) Subcell Biochem , vol.48 , pp. 6-19
    • Hudson, A.M.1    Cooley, L.2
  • 83
    • 58149161238 scopus 로고    scopus 로고
    • Diversity of WD-repeat proteins
    • Smith TF (2008) Diversity of WD-repeat proteins. Subcell Biochem 48: 20-30.
    • (2008) Subcell Biochem , vol.48 , pp. 20-30
    • Smith, T.F.1
  • 85
    • 0035664074 scopus 로고    scopus 로고
    • WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases
    • Li D, Roberts R (2001) WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell Mol Life Sci 58: 2085-2097.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 2085-2097
    • Li, D.1    Roberts, R.2
  • 86
    • 33644798295 scopus 로고    scopus 로고
    • The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes
    • Appleton B, Wu P, Wiesmann C (2006) The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes. Structure 14: 87-96.
    • (2006) Structure , vol.14 , pp. 87-96
    • Appleton, B.1    Wu, P.2    Wiesmann, C.3
  • 87
    • 0033198781 scopus 로고    scopus 로고
    • The coronin family of actin-associated proteins
    • de Hostos EL (1999) The coronin family of actin-associated proteins. Trends Cell Biol 9: 345-350.
    • (1999) Trends Cell Biol , vol.9 , pp. 345-350
    • de Hostos, E.L.1
  • 88
    • 21244477562 scopus 로고    scopus 로고
    • Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking
    • Rybakin V, Clemen C (2005) Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking. BioEssays 27: 625-632.
    • (2005) BioEssays , vol.27 , pp. 625-632
    • Rybakin, V.1    Clemen, C.2
  • 90
    • 19644384351 scopus 로고    scopus 로고
    • Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules
    • Gatfield J, Albrecht I, Zanolari B, Steinmetz M, Pieters J (2005) Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules. Mol Biol Cell 16: 2786-2798.
    • (2005) Mol Biol Cell , vol.16 , pp. 2786-2798
    • Gatfield, J.1    Albrecht, I.2    Zanolari, B.3    Steinmetz, M.4    Pieters, J.5
  • 91
    • 70349415120 scopus 로고    scopus 로고
    • Coronin: the double-edged sword of actin dynamics
    • C. Clemen, L. Eichinger, and V. Rybakin (Eds.), Georgetown: Landes Bioscience
    • Gandhi M, Goode B (2008) Coronin: the double-edged sword of actin dynamics. In: Clemen C, Eichinger L, Rybakin V (eds) The coronin family of proteins. Landes Bioscience, Georgetown.
    • (2008) The Coronin Family of Proteins
    • Gandhi, M.1    Goode, B.2
  • 93
    • 24744433765 scopus 로고    scopus 로고
    • Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility
    • Cai L, Holoweckyj N, Schaller M, Bear J (2005) Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility. J Biol Chem 280: 31913-31923.
    • (2005) J Biol Chem , vol.280 , pp. 31913-31923
    • Cai, L.1    Holoweckyj, N.2    Schaller, M.3    Bear, J.4
  • 94
    • 0037073706 scopus 로고    scopus 로고
    • Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus
    • Spoerl Z, Stumpf M, Noegel AA, Hasse A (2002) Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus. J Biol Chem 277: 48858-48867.
    • (2002) J Biol Chem , vol.277 , pp. 48858-48867
    • Spoerl, Z.1    Stumpf, M.2    Noegel, A.A.3    Hasse, A.4
  • 95
    • 0034667414 scopus 로고    scopus 로고
    • The new architectonics: an invitation to structural biology
    • Schutt CE, Lindberg U (2000) The new architectonics: an invitation to structural biology. Anat Rec 261: 198-216.
    • (2000) Anat Rec , vol.261 , pp. 198-216
    • Schutt, C.E.1    Lindberg, U.2


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