메뉴 건너뛰기




Volumn 9, Issue 5, 2014, Pages

Structural insights into the evolution of a sexy protein: Novel topology and restricted backbone flexibility in a hypervariable pheromone from the red-legged salamander, plethodon shermani

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; PHEROMONE; PLETHODONTID MODULATING FACTOR; THREE FINGER PROTEIN; UNCLASSIFIED DRUG; AMPHIBIAN PROTEIN; DISULFIDE; PROTEIN BINDING; RECOMBINANT PROTEIN; SEX PHEROMONE;

EID: 84901321535     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0096975     Document Type: Article
Times cited : (18)

References (74)
  • 1
    • 36949092394 scopus 로고
    • 'Pheromones': A new term for a class of biologically active substances
    • Karlson P, Luscher M (1959) 'Pheromones': a new term for a class of biologically active substances. Nature 183: 55-56.
    • (1959) Nature , vol.183 , pp. 55-56
    • Karlson, P.1    Luscher, M.2
  • 2
    • 0015135938 scopus 로고
    • Androgen steroids associated with boar odour as an aid to the detection of oestrus in pig artificial insemination
    • Melrose DR, Reed HC, Patterson RL (1971) Androgen steroids associated with boar odour as an aid to the detection of oestrus in pig artificial insemination. The British Veterinary Journal 127: 497-502.
    • (1971) The British Veterinary Journal , vol.127 , pp. 497-502
    • Melrose, D.R.1    Reed, H.C.2    Patterson, R.L.3
  • 4
    • 0002635355 scopus 로고    scopus 로고
    • Chemical communication and pheromones: The types of chemical signals and the role of the vomeronasal system
    • Finger TE, Silver WL, Restrepo D, editors. New York: Wiley-Liss
    • Johnston RE (2000) Chemical communication and pheromones: the types of chemical signals and the role of the vomeronasal system. In: Finger TE, Silver WL, Restrepo D, editors. The Neurobiology of Taste and Smell. New York: Wiley-Liss. 101-127.
    • (2000) The Neurobiology of Taste and Smell , pp. 101-127
    • Johnston, R.E.1
  • 5
    • 0041706670 scopus 로고    scopus 로고
    • Molecular detection of pheromone signals in mammals: From genes to behaviour
    • DOI 10.1038/nrn1140
    • Dulac C, Torello AT (2003) Molecular detection of pheromone signals in mammals: from genes to behaviour. Nat Rev Neurosci 4: 551-562. (Pubitemid 37271366)
    • (2003) Nature Reviews Neuroscience , vol.4 , Issue.7 , pp. 551-562
    • Dulac, C.1    Torello, A.T.2
  • 8
  • 10
    • 0037154789 scopus 로고    scopus 로고
    • Loss of sex discrimination and male-male aggression in mice deficient for TRP2
    • DOI 10.1126/science.1069259
    • Stowers L, Holy TE, Meister M, Dulac C, Koentges G (2002) Loss of sex discrimination and male-male aggression in mice deficient for TRP2. Science 295: 1493-1500. (Pubitemid 34173998)
    • (2002) Science , vol.295 , Issue.5559 , pp. 1493-1500
    • Stowers, L.1    Holy, T.E.2    Meister, M.3    Dulac, C.4    Koentges, G.5
  • 11
    • 77954231077 scopus 로고    scopus 로고
    • The male mouse pheromone ESP1 enhances female sexual receptive behaviour through a specific vomeronasal receptor
    • Haga S, Hattori T, Sato T, Sato K, Matsuda S, et al. (2010) The male mouse pheromone ESP1 enhances female sexual receptive behaviour through a specific vomeronasal receptor. Nature 466: 118-122.
    • (2010) Nature , vol.466 , pp. 118-122
    • Haga, S.1    Hattori, T.2    Sato, T.3    Sato, K.4    Matsuda, S.5
  • 12
    • 84878378250 scopus 로고    scopus 로고
    • Structure of the mouse sex peptide pheromone ESP1 reveals a molecular basis for specific binding to the class C G-protein-coupled vomeronasal receptor
    • Yoshinaga S, Sato T, Hirakane M, Esaki K, Hamaguchi T, et al. (2013) Structure of the mouse sex peptide pheromone ESP1 reveals a molecular basis for specific binding to the class C G-protein-coupled vomeronasal receptor. Journal of Biological Chemistry 288: 16064-16072.
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 16064-16072
    • Yoshinaga, S.1    Sato, T.2    Hirakane, M.3    Esaki, K.4    Hamaguchi, T.5
  • 13
    • 0025262716 scopus 로고
    • Male courtship pheromones increase female receptivity in a plethodontid salamander
    • Houck LD, Reagan NL (1990) Male courtship pheromones increase female receptivity in a Plethodontid salamander. Animal Behaviour 39: 729-734. (Pubitemid 20427257)
    • (1990) Animal Behaviour , vol.39 , Issue.4 , pp. 729-734
    • Houck, L.D.1    Reagan, N.L.2
  • 14
    • 85005583730 scopus 로고
    • Sexual behavior, sexual interference, and sexual deference in salamanders Ambystoma maculatum, Ambystoma tigrinum, and Plethodon jordani
    • Arnold SJ (1976) Sexual behavior, sexual interference, and sexual deference in salamanders Ambystoma maculatum, Ambystoma tigrinum, and Plethodon jordani. Z Tierpsychol 42: 247-300.
    • (1976) Z Tierpsychol , vol.42 , pp. 247-300
    • Arnold, S.J.1
  • 15
    • 0000676369 scopus 로고    scopus 로고
    • Chemical analyses of courtship pheromones in a Plethodontid salamander
    • Johnston RE, Mu{combining double acute accent}ller-Schwarze D, Sorensen P, editors. New York: Kluwer Academic/Plenum
    • Feldhoff RC, Rollmann SM, Houck LD (1999) Chemical analyses of courtship pheromones in a Plethodontid salamander. In: Johnston RE, Mu{combining double acute accent}ller-Schwarze D, Sorensen P, editors. Advances in Chemical Signals in Vertebrates. New York: Kluwer Academic/Plenum. 117-125.
    • (1999) Advances in Chemical Signals in Vertebrates , pp. 117-125
    • Feldhoff, R.C.1    Rollmann, S.M.2    Houck, L.D.3
  • 16
    • 0033578813 scopus 로고    scopus 로고
    • Proteinaceous pheromone affecting female receptivity in a terrestrial salamander
    • Rollmann SM, Houck LD, Feldhoff RC (1999) Proteinaceous pheromone affecting female receptivity in a terrestrial salamander. Science 285: 1907-1909.
    • (1999) Science , vol.285 , pp. 1907-1909
    • Rollmann, S.M.1    Houck, L.D.2    Feldhoff, R.C.3
  • 19
    • 37849053991 scopus 로고    scopus 로고
    • Courtship pheromone-induced c-Fos-like immunolabeling in the female salamander brain
    • Laberge F, Feldhoff RC, Feldhoff PW, Houck LD (2008) Courtship pheromone-induced c-Fos-like immunolabeling in the female salamander brain. Neuroscience 151: 329-339.
    • (2008) Neuroscience , vol.151 , pp. 329-339
    • Laberge, F.1    Feldhoff, R.C.2    Feldhoff, P.W.3    Houck, L.D.4
  • 20
    • 84863473424 scopus 로고    scopus 로고
    • Proteomic and UTR analyses of a rapidly evolving hypervaraible family of vertebrate pheromones
    • Wilburn DB, Bowen KE, Gregg RG, Cai J, Feldhoff PW, et al. (2012) Proteomic and UTR analyses of a rapidly evolving hypervaraible family of vertebrate pheromones. Evolution 66: 2227-2239.
    • (2012) Evolution , vol.66 , pp. 2227-2239
    • Wilburn, D.B.1    Bowen, K.E.2    Gregg, R.G.3    Cai, J.4    Feldhoff, P.W.5
  • 21
    • 84901335806 scopus 로고    scopus 로고
    • Individual Variation in Pheromone Isoform Ratios of the Red-Legged Salamander, Plethodon shermani
    • East ML, Dehnhard M, editors. New York: Springer
    • Chouinard AJ, Wilburn DB, Houck LD, Feldhoff RC (2013) Individual Variation in Pheromone Isoform Ratios of the Red-Legged Salamander, Plethodon shermani. In: East ML, Dehnhard M, editors. Chemical Signals in Vertebrates 12. New York: Springer. 99-115.
    • (2013) Chemical Signals in Vertebrates , vol.12 , pp. 99-115
    • Chouinard, A.J.1    Wilburn, D.B.2    Houck, L.D.3    Feldhoff, R.C.4
  • 22
    • 77954398484 scopus 로고    scopus 로고
    • Rapid evolution of Plethodontid modulating factor (PMF), a hypervariable salamander courtship pheromone, is driven by positive selection
    • Palmer CA, Picard AL, Watts RA, Houck LD, Arnold SJ (2010) Rapid evolution of Plethodontid modulating factor (PMF), a hypervariable salamander courtship pheromone, is driven by positive selection. Journal of Molecular Evolution 70: 427-440.
    • (2010) Journal of Molecular Evolution , vol.70 , pp. 427-440
    • Palmer, C.A.1    Picard, A.L.2    Watts, R.A.3    Houck, L.D.4    Arnold, S.J.5
  • 23
    • 0033198876 scopus 로고    scopus 로고
    • Snake venom a-neurotoxins and other 'three-finger' proteins
    • Tsetlin V (1999) Snake venom a-neurotoxins and other 'three-finger' proteins. European Journal of Biochemistry 264: 281-286.
    • (1999) European Journal of Biochemistry , vol.264 , pp. 281-286
    • Tsetlin, V.1
  • 24
    • 15544369378 scopus 로고    scopus 로고
    • From genome to "venome": Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
    • Fry BG (2005) From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Research 15: 403-420.
    • (2005) Genome Research , vol.15 , pp. 403-420
    • Fry, B.G.1
  • 25
    • 0024456866 scopus 로고
    • CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells
    • Davies A, Simmons DL, Hale G, Harrison RA, Tighe H, et al. (1989) CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells. The Journal of Experimental Medicine 170: 637-654. (Pubitemid 19226653)
    • (1989) Journal of Experimental Medicine , vol.170 , Issue.3 , pp. 637-654
    • Davies, A.1    Simmons, D.L.2    Hale, G.3    Harrison, R.A.4    Tighe, H.5    Lachmann, P.J.6    Waldmann, H.7
  • 26
  • 27
    • 70349632590 scopus 로고    scopus 로고
    • Solution structure and phylogenetics of Prod1, a member of the three-finger protein superfamily implicated in salamander limb regeneration
    • Garza-Garcia A, Harris R, Esposito D, Gates PB, Driscoll PC (2009) Solution structure and phylogenetics of Prod1, a member of the three-finger protein superfamily implicated in salamander limb regeneration. PLoS ONE 4: e7123.
    • (2009) PLoS ONE , vol.4
    • Garza-Garcia, A.1    Harris, R.2    Esposito, D.3    Gates, P.B.4    Driscoll, P.C.5
  • 28
    • 0037079014 scopus 로고    scopus 로고
    • The structure of the protein universe and genome evolution
    • DOI 10.1038/nature01256
    • Koonin EV, Wolf YI, Karev GP (2002) The structure of the protein universe and genome evolution. Nature 420: 218-223. (Pubitemid 35340133)
    • (2002) Nature , vol.420 , Issue.6912 , pp. 218-223
    • Koonin, E.V.1    Wolf, Y.I.2    Karev, G.P.3
  • 30
    • 84876578144 scopus 로고    scopus 로고
    • New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures
    • Sillitoe I, Cuff AL, Dessailly BH, Dawson NL, Furnham N, et al. (2013) New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures. Nucleic Acids Research 41: D490-D498.
    • (2013) Nucleic Acids Research , vol.41
    • Sillitoe, I.1    Cuff, A.L.2    Dessailly, B.H.3    Dawson, N.L.4    Furnham, N.5
  • 32
    • 44349135549 scopus 로고    scopus 로고
    • Conserved structural determinants in three-fingered protein domains
    • DOI 10.1111/j.1742-4658.2008.06473.x
    • Galat A, Gross G, Drevet P, Sato A, Menez A (2008) Conserved stuctural determinants in three-fingered protein domains. FEBS Journal 275: 3207-3225. (Pubitemid 351743595)
    • (2008) FEBS Journal , vol.275 , Issue.12 , pp. 3207-3225
    • Galat, A.1    Gross, G.2    Drevet, P.3    Sato, A.4    Menez, A.5
  • 33
    • 0032891247 scopus 로고    scopus 로고
    • Structural and phylogenetic characterization of human SLURP-1, the first secreted mammalian member of the Ly-6/uPAR protein superfamily
    • Adermann K, Wattler F, Wattler S, Heine G, Meyer M, et al. (1999) Structural and phylogenetic characterization of human SLURP-1, the first secreted mammalian member of the Ly-6/uPAR protein superfamily. Protein Science 8: 810-819. (Pubitemid 29165411)
    • (1999) Protein Science , vol.8 , Issue.4 , pp. 810-819
    • Adermann, K.1    Wattler, F.2    Wattler, S.3    Heine, G.4    Meyer, M.5    Forssmann, W.-G.6    Nehls, M.7
  • 34
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu H, Freitas MA (2009) MassMatrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data. Proteomics 9: 1548-1555.
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 35
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer WPC, Crameri A, Ha KD, Brennan TM, Heyneker HL (1995) Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164: 49-53.
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.C.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 36
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C, Andrade-Navarro M (2008) K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Structural Biology 8: 25.
    • (2008) BMC Structural Biology , vol.8 , pp. 25
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.2
  • 38
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solution
    • Piotto M, Saudek V, Sklenar V (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solution. Journal of Biomolecular NMR 2: 661-665.
    • (1992) Journal of Biomolecular NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 39
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program Dyana
    • Güntert P, Mumenthaler C, Wüthrich K (1997) Torsion angle dynamics for NMR structure calculation with the new program Dyana. Journal of Molecular Biology 273: 283-298.
    • (1997) Journal of Molecular Biology , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 40
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. Journal of Molecular Biology 319: 209-227. (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 41
    • 68349093958 scopus 로고    scopus 로고
    • TALOS plus: A hybrid method for predicting protein torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS plus: a hybrid method for predicting protein torsion angles from NMR chemical shifts. Journal of Biomolecular NMR 44: 213-223.
    • (2009) Journal of Biomolecular NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 42
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • Sharma D, Rajarathnam K (2000) 13C NMR chemical shifts can predict disulfide bond formation. Journal of Biomolecular NMR 18: 165-171.
    • (2000) Journal of Biomolecular NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 43
    • 0033997901 scopus 로고    scopus 로고
    • The influence of DNA binding on the backbone dynamics of the yeast cell- cycle protein Mbp1
    • DOI 10.1023/A:1008374129366
    • McIntosh PB, Taylor IA, Frenkiel TA, Smerdon SJ, Lane AN (2000) The influence of DNA binding on the backbone dynamics of the yeast cell-cycle protein Mbp1*. Journal of biomolecular NMR 16: 183-196. (Pubitemid 30217107)
    • (2000) Journal of Biomolecular NMR , vol.16 , Issue.3 , pp. 183-196
    • McIntosh, P.B.1    Taylor, I.A.2    Frenkiel, T.A.3    Smerdon, S.J.4    Lane, A.N.5
  • 44
    • 27544456339 scopus 로고    scopus 로고
    • A simple method to predict protein flexibility using secondary chemical shifts
    • DOI 10.1021/ja054842f
    • Berjanskii MV, Wishart DS (2005) A simple method to predict protein flexibility using secondary chemical shifts. Journal of American Chemical Society 127: 14970-14971. (Pubitemid 41547332)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.43 , pp. 14970-14971
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 45
    • 48449095267 scopus 로고    scopus 로고
    • PVS: A web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery
    • Garcia-Boronat M, Diez-Rivero CM, Reinherz EL, Reche PA (2008) PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery. Nucleic Acids Research 36: W35-41.
    • (2008) Nucleic Acids Research , vol.36
    • Garcia-Boronat, M.1    Diez-Rivero, C.M.2    Reinherz, E.L.3    Reche, P.A.4
  • 46
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J, Higgins D, Gibson T (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Research 22: 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0027448780 scopus 로고
    • Disulfide structures of highly bridged peptides: A new strategy for analysis
    • Gray WR (1993) Disulfide structures of highly bridged peptides: A new strategy for analysis. Protein Science 2: 1732-1748.
    • (1993) Protein Science , vol.2 , pp. 1732-1748
    • Gray, W.R.1
  • 49
    • 36248939782 scopus 로고    scopus 로고
    • "Forbidden" disulfides: Their role as redox switches
    • DOI 10.2174/138920307782411464
    • Wouters MA, George RA, Haworth NL (2007) "Forbidden" disulfides: their role as redox switches. Current Protein and Peptide Science 8: 484-495. (Pubitemid 350130983)
    • (2007) Current Protein and Peptide Science , vol.8 , Issue.5 , pp. 484-495
    • Wouters, M.A.1    George, R.A.2    Haworth, N.L.3
  • 51
    • 0034013918 scopus 로고    scopus 로고
    • Chemical engineering of a three-fingered toxin with anti-a7 neuronal acetylcholine receptor activity
    • Mourier G, Servent D, Zinn-Justin S, Ménez A (2000) Chemical engineering of a three-fingered toxin with anti-a7 neuronal acetylcholine receptor activity. Protein Engineering 13: 217-225. (Pubitemid 30237597)
    • (2000) Protein Engineering , vol.13 , Issue.3 , pp. 217-225
    • Mourier, G.1    Servent, D.2    Zinn-Justin, S.3    Menez, A.4
  • 52
    • 0032564439 scopus 로고    scopus 로고
    • Characterization of the extracellular ligand-binding domain of the type II activin receptor
    • DOI 10.1021/bi981939o
    • Greenwald J, Le V, Corrigan A, Fischer W, Komives E, et al. (1998) Characterization of the extracellular ligand-binding domain of the type II activin receptor. Biochemistry 37: 16711-16718. (Pubitemid 28543932)
    • (1998) Biochemistry , vol.37 , Issue.47 , pp. 16711-16718
    • Greenwald, J.1    Le, V.2    Corrigan, A.3    Fischer, W.4    Komives, E.5    Vale, W.6    Choe, S.7
  • 53
    • 2942616880 scopus 로고    scopus 로고
    • Evidence showing an intermolecular interaction between KChIP proteins and Taiwan cobra cardiotoxins
    • DOI 10.1016/j.bbrc.2004.05.064, PII S0006291X04010538
    • Lin Y-L, Lin S-R, Wu TT, Chang L-S (2004) Evidence showing an intermolecular interaction between KChIP proteins and Taiwan cobra cardiotoxins. Biochemical and Biophysical Research Communications 319: 720-724. (Pubitemid 38739380)
    • (2004) Biochemical and Biophysical Research Communications , vol.319 , Issue.3 , pp. 720-724
    • Lin, Y.-L.1    Lin, S.-R.2    Wu, T.T.3    Chang, L.-S.4
  • 54
    • 0029069121 scopus 로고
    • NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom
    • Albrand J, Blackledge M, Pascaud F, Hollecker M, Marion D (1995) NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom. Biochemistry 34: 5923-5937.
    • (1995) Biochemistry , vol.34 , pp. 5923-5937
    • Albrand, J.1    Blackledge, M.2    Pascaud, F.3    Hollecker, M.4    Marion, D.5
  • 56
    • 0000680926 scopus 로고
    • The action of snake venoms on nerve and muscles
    • Lee CY, editor. Berlin: Springer-Verlag
    • Chang CC (1979) The action of snake venoms on nerve and muscles. In: Lee CY, editor. Snake Venoms, Handbook of Experimental Pharmacology. Berlin: Springer-Verlag. 309-376.
    • (1979) Snake Venoms, Handbook of Experimental Pharmacology , pp. 309-376
    • Chang, C.C.1
  • 57
    • 0027973761 scopus 로고
    • Toxins from mamba venoms: Small proteins with selectivities for different subtypes of muscarinic acetylcholine receptors
    • DOI 10.1016/0165-6147(94)90092-2
    • Jerusalinsky D, Harvey AL (1994) Toxins from mamba venoms: small proteins with selectivities for different subtypes of muscarinic acetylcholine receptors. Trends in Pharmacological Sciences 15: 424-430. (Pubitemid 24360513)
    • (1994) Trends in Pharmacological Sciences , vol.15 , Issue.11 , pp. 424-430
    • Jerusalinsky, D.1    Harvey, A.L.2
  • 58
    • 0001163775 scopus 로고
    • Fasciculins, anti-cholinesterase toxins from mamba venoms: Biochemistry and pharmacology
    • Harvey AL, editor. New York: Pergamon Press
    • Cervenansky C, Dajas F, Harvey AL, Karlsson E (1991) Fasciculins, anti-cholinesterase toxins from mamba venoms: biochemistry and pharmacology. In: Harvey AL, editor. Snake Toxins. New York: Pergamon Press. 303-321.
    • (1991) Snake Toxins , pp. 303-321
    • Cervenansky, C.1    Dajas, F.2    Harvey, A.L.3    Karlsson, E.4
  • 59
    • 0026650803 scopus 로고
    • Mambin, a potent glycoprotein IIb-IIIa antagonist and platet aggregation inhibitor structurally related to the short neurotoxins
    • McDowell RS, Dennis MS, Louie A, Shuster M, Mulkerrin MG, et al. (1992) Mambin, a potent glycoprotein IIb-IIIa antagonist and platet aggregation inhibitor structurally related to the short neurotoxins. Biochemistry 31: 4766-4772.
    • (1992) Biochemistry , vol.31 , pp. 4766-4772
    • McDowell, R.S.1    Dennis, M.S.2    Louie, A.3    Shuster, M.4    Mulkerrin, M.G.5
  • 60
    • 33646351297 scopus 로고    scopus 로고
    • Non-cytotoxic cobra cardiotoxin A5 binds to avb3 integrin and inhibits bone resorption
    • Wu P-L, Lee S-C, Chuang C-C, Mori S, Akakura N, et al. (2006) Non-cytotoxic cobra cardiotoxin A5 binds to avb3 integrin and inhibits bone resorption. Journal of Biological Chemistry 281: 7937-7945.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 7937-7945
    • Wu, P.-L.1    Lee, S.-C.2    Chuang, C.-C.3    Mori, S.4    Akakura, N.5
  • 61
    • 0028306665 scopus 로고
    • X-ray structure at 1.55 Å of toxin c, a cardiotoxin from Naja nigricollis venom: Crystal packing reveals a model for insertion into membranes
    • Bilwes A, Rees B, Moras D, Ménez R, Ménez A (1994) X-ray structure at 1.55 Å of toxin c, a cardiotoxin from Naja nigricollis venom: crystal packing reveals a model for insertion into membranes. Journal of Molecular Biology 239: 122-136.
    • (1994) Journal of Molecular Biology , vol.239 , pp. 122-136
    • Bilwes, A.1    Rees, B.2    Moras, D.3    Ménez, R.4    Ménez, A.5
  • 62
    • 77956063164 scopus 로고    scopus 로고
    • Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets
    • Kini RM, Doley R (2010) Structure, function and evolution of three-finger toxins: mini proteins with multiple targets. Toxicon 56: 855-867.
    • (2010) Toxicon , vol.56 , pp. 855-867
    • Kini, R.M.1    Doley, R.2
  • 63
    • 33846416949 scopus 로고    scopus 로고
    • A new vertebrate courtship pheromone, PMF, affects female receptivity in a terrestrial salamander
    • DOI 10.1016/j.anbehav.2006.07.008, PII S0003347206004209
    • Houck LD, Palmer CA, Watts RA, Arnold SJ, Feldhoff PW, et al. (2007) A new vertebrate courtship pheromone that affects female receptivity in a terrestrial salamander. Animal Behaviour 73: 315-320. (Pubitemid 46149574)
    • (2007) Animal Behaviour , vol.73 , Issue.2 , pp. 315-320
    • Houck, L.D.1    Palmer, C.A.2    Watts, R.A.3    Arnold, S.J.4    Feldhoff, P.W.5    Feldhoff, R.C.6
  • 65
    • 77953891235 scopus 로고    scopus 로고
    • Darcin: A male pheromone that stimulates female memory and sexual attraction to an individual male's odour
    • Roberts S, Simpson D, Armstrong S, Davidson A, Robertson D, et al. (2010) Darcin: a male pheromone that stimulates female memory and sexual attraction to an individual male's odour. BMC Biology 8: 75.
    • (2010) BMC Biology , vol.8 , pp. 75
    • Roberts, S.1    Simpson, D.2    Armstrong, S.3    Davidson, A.4    Robertson, D.5
  • 66
    • 47149101500 scopus 로고    scopus 로고
    • Dynamic instability of the major urinary protein gene family revealed by genomic and phenotypic comparisons between C57 and I29 strain mice
    • Mudge JM, Armstrong SD, McLaren K, Beynon RJ, Hurst JL, et al. (2008) Dynamic instability of the major urinary protein gene family revealed by genomic and phenotypic comparisons between C57 and I29 strain mice. Genome Biology 9: R91.
    • (2008) Genome Biology , vol.9
    • Mudge, J.M.1    Armstrong, S.D.2    McLaren, K.3    Beynon, R.J.4    Hurst, J.L.5
  • 67
    • 84859841055 scopus 로고    scopus 로고
    • Expression of vomeronasal receptors and related signaling molecules in the nasal cavity of a caudate amphibian (Plethodon shermani)
    • Kiemnec-Tyburczy KM, Woodley SK, Watts RA, Arnold SJ, Houck LD (2012) Expression of vomeronasal receptors and related signaling molecules in the nasal cavity of a caudate amphibian (Plethodon shermani). Chemical Senses 37: 335-346.
    • (2012) Chemical Senses , vol.37 , pp. 335-346
    • Kiemnec-Tyburczy, K.M.1    Woodley, S.K.2    Watts, R.A.3    Arnold, S.J.4    Houck, L.D.5
  • 68
    • 65949108430 scopus 로고    scopus 로고
    • Sensing odorants and pheromones with chemosensory receptors
    • Touhara K, Vosshall LB (2009) Sensing odorants and pheromones with chemosensory receptors. Annual Review of Physiology 71: 307-332.
    • (2009) Annual Review of Physiology , vol.71 , pp. 307-332
    • Touhara, K.1    Vosshall, L.B.2
  • 69
    • 80054043805 scopus 로고    scopus 로고
    • Molecular organization of vomeronasal chemoreception
    • Isogai Y, Si S, Pont-Lezica L, Tan T, Kapoor V, et al. (2011) Molecular organization of vomeronasal chemoreception. Nature 478: 241-245.
    • (2011) Nature , vol.478 , pp. 241-245
    • Isogai, Y.1    Si, S.2    Pont-Lezica, L.3    Tan, T.4    Kapoor, V.5
  • 71
    • 70549099965 scopus 로고    scopus 로고
    • Structural requirements for the activation of vomeronasal sensory neurons by MHC peptides
    • Leinders-Zufall T, Ishii T, Mombaerts P, Zufall F, Boehm T (2009) Structural requirements for the activation of vomeronasal sensory neurons by MHC peptides. Nat Neurosci 12: 1551-1558.
    • (2009) Nat Neurosci , vol.12 , pp. 1551-1558
    • Leinders-Zufall, T.1    Ishii, T.2    Mombaerts, P.3    Zufall, F.4    Boehm, T.5
  • 73
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.