메뉴 건너뛰기




Volumn 585, Issue 8, 2011, Pages 1197-1202

NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster

Author keywords

Conformation; Drosophila; Fruit fly; NMR spectroscopy; Peptide; Secondary structure; Sex peptide

Indexed keywords

HYDROXYPROLINE; PEPTIDE HORMONE; SEX PEPTIDE; UNCLASSIFIED DRUG;

EID: 79954443913     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.03.040     Document Type: Article
Times cited : (9)

References (26)
  • 1
    • 40149089398 scopus 로고    scopus 로고
    • Sexual behaviour: A receptor for sex control in Drosophila females
    • E. Kubli Sexual behaviour: a receptor for sex control in Drosophila females Curr. Biol. 18 2008 R210 R212
    • (2008) Curr. Biol. , vol.18
    • Kubli, E.1
  • 2
    • 77953826385 scopus 로고    scopus 로고
    • Sexual behavior: Dietary food switch induced by sex
    • E. Kubli Sexual behavior: dietary food switch induced by sex Curr. Biol. 20 2010 R474 R476
    • (2010) Curr. Biol. , vol.20
    • Kubli, E.1
  • 3
    • 38049005548 scopus 로고    scopus 로고
    • A receptor that mediated the post-mating switch in Drosophila reproductive behaviour
    • N. Yapici, Y.-J. Kim, C. Ribeiro, and B.J. Dickson A receptor that mediated the post-mating switch in Drosophila reproductive behaviour Nature 451 2007 33 37
    • (2007) Nature , vol.451 , pp. 33-37
    • Yapici, N.1    Kim, Y.-J.2    Ribeiro, C.3    Dickson, B.J.4
  • 4
    • 60449095388 scopus 로고    scopus 로고
    • Sensory neurons in the Drosophila female reproductive tract regulate female reproductive behavior
    • M. Häsemeyer, N. Yapici, U. Heberlein, and B.J. Dickson Sensory neurons in the Drosophila female reproductive tract regulate female reproductive behavior Neuron 61 2009 511 518
    • (2009) Neuron , vol.61 , pp. 511-518
    • Häsemeyer, M.1    Yapici, N.2    Heberlein, U.3    Dickson, B.J.4
  • 5
    • 70350509607 scopus 로고    scopus 로고
    • The Drosophila G protein-coupled receptor methuselah exhibits a promiscuous response to peptides
    • W.W. Ja, G.B. Carvalho, M. Madrigal, R.W. Roberts, and S. Benzer The Drosophila G protein-coupled receptor methuselah exhibits a promiscuous response to peptides Protein Sci. 18 2009 2203 2208
    • (2009) Protein Sci. , vol.18 , pp. 2203-2208
    • Ja, W.W.1    Carvalho, G.B.2    Madrigal, M.3    Roberts, R.W.4    Benzer, S.5
  • 6
    • 35448953619 scopus 로고    scopus 로고
    • The hydroxyproline motif of male sex peptide elicits the innate immune response in Drosophila females
    • DOI 10.1111/j.1742-4658.2007.06088.x
    • E.V. Domanitskaya, H.F. Liu, S.J. Chen, and E. Kubli The hydroxyproline motif of male sex peptide elicits the innate immune response in Drosophila females FEBS J. 274 2007 5659 5668 (Pubitemid 47622079)
    • (2007) FEBS Journal , vol.274 , Issue.21 , pp. 5659-5668
    • Domanitskaya, E.V.1    Liu, H.2    Chen, S.3    Kubli, E.4
  • 7
    • 24944516187 scopus 로고    scopus 로고
    • Drosophila sex-peptide stimulates female innate immune system after mating via the toll and Imd pathways
    • DOI 10.1016/j.cub.2005.08.048, PII S096098220500967X
    • J. Peng, P. Zipperlen, and E. Kubli Drosophila sex-peptide stimulates female innate immune system after mating via the Toll and Imd pathways Curr. Biol. 15 2005 1690 1694 (Pubitemid 41323749)
    • (2005) Current Biology , vol.15 , Issue.18 , pp. 1690-1694
    • Peng, J.1    Zipperlen, P.2    Kubli, E.3
  • 8
    • 0024299504 scopus 로고
    • A male accessory gland peptide that regulates reproductive behavior of female D. melanogaster
    • P.S. Chen, E. Stumm-Zollinger, T. Aigaki, J. Balmer, M. Bienz, and P. Böhlen A male accessory gland peptide that regulates reproductive behavior of female D. melanogaster Cell 54 1988 291 298
    • (1988) Cell , vol.54 , pp. 291-298
    • Chen, P.S.1    Stumm-Zollinger, E.2    Aigaki, T.3    Balmer, J.4    Bienz, M.5    Böhlen, P.6
  • 9
    • 0000623499 scopus 로고
    • The Drosophila melanogaster sex-peptide: A molecular analysis of structure-function relationships
    • T. Schmidt, Y. Choffat, S. Klauser, and E. Kubli The Drosophila melanogaster sex-peptide: a molecular analysis of structure-function relationships J. Insect Physiol. 39 1993 361 368
    • (1993) J. Insect Physiol. , vol.39 , pp. 361-368
    • Schmidt, T.1    Choffat, Y.2    Klauser, S.3    Kubli, E.4
  • 10
    • 0038705112 scopus 로고    scopus 로고
    • Sex-peptides bind to two molecularly different targets in Drosophila melanogaster females
    • DOI 10.1002/neu.10218
    • Z. Ding, I. Haussmann, M. Ottiger, and E. Kubli Sex-peptides bind to two molecularly different targets in Drosophila melanogaster females J. Neurobiol. 55 2003 372 384 (Pubitemid 36566154)
    • (2003) Journal of Neurobiology , vol.55 , Issue.3 , pp. 372-384
    • Ding, Z.1    Haussmann, I.2    Ottiger, M.3    Kubli, E.4
  • 11
    • 0042830851 scopus 로고    scopus 로고
    • Sex-peptides: Seminal peptides of the Drosophila male
    • DOI 10.1007/s00018-003-3052
    • E. Kubli Sex-peptides: seminal peptides of the Drosophila male Cell Mol. Life Sci. 60 2003 1689 1704 (Pubitemid 37041365)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.8 , pp. 1689-1704
    • Kubli, E.1
  • 12
    • 13444250122 scopus 로고    scopus 로고
    • Gradual release of sperm bound sex-peptide controls female postmating behavior in Drosophila
    • DOI 10.1016/j.cub.2005.01.034
    • J. Peng, S. Chen, S. B̧sser, H. Liu, T. Honegger, and E. Kubli Gradual release of sperm bound sex-peptide controls female postmating behavior in Drosophila Curr. Biol. 15 2005 207 213 (Pubitemid 40205700)
    • (2005) Current Biology , vol.15 , Issue.3 , pp. 207-213
    • Peng, J.1    Chen, S.2    Busser, S.3    Liu, H.4    Honegger, T.5    Kubli, E.6
  • 13
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • C. Bartels, T.-h. Xia, M. Billeter, P. Güntert, and K. Wüthrich The program XEASY for computer-supported NMR spectral analysis of biological macromolecules J. Biomol. NMR 6 1995 1 10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    X, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 14
    • 44049114111 scopus 로고
    • Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets
    • T. Szyperski, P. Güntert, G. Otting, and K. Wüthrich Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets J. Mag. Res. 99 1992 552 560
    • (1992) J. Mag. Res. , vol.99 , pp. 552-560
    • Szyperski, T.1    Güntert, P.2    Otting, G.3    Wüthrich, K.4
  • 15
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • DOI 10.1006/jmbi.1997.1284
    • P. Guntert, C. Mumenthaler, and K. Wuthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298 (Pubitemid 27460230)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 16
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 17
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comp. 4 2008 435 447
    • (2008) J. Chem. Theory Comp. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 18
    • 0029181728 scopus 로고
    • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • D.S. Wishart, C.G. Bigam, A. Holm, R.S. Hodges, and B.D. Sykes 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects J. Biomol. NMR 5 1995 67 81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 19
    • 75749113781 scopus 로고    scopus 로고
    • NMR chemical shift data and ab initio shielding calculations: Emerging tools for protein structure determination
    • F.A.A. Mulder, and M. Filatov NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination Chem. Soc. Rev. 39 2010 578 590
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 578-590
    • Mulder, F.A.A.1    Filatov, M.2
  • 22
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • M.W. Macarthur, and J.M. Thornton Influence of proline residues on protein conformation J. Mol. Biol. 218 1991 397 412 (Pubitemid 121003355)
    • (1991) Journal of Molecular Biology , vol.218 , Issue.2 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 23
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • DOI 10.1006/jmbi.1993.1047
    • A.A. Adzhubei, and M.J.E. Sternberg Left-handed polyproline-Ii helices commonly occur in globular-proteins J. Mol. Biol. 229 1993 472 493 (Pubitemid 23080393)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.2 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 24
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 26
    • 0028394633 scopus 로고
    • Analysis of proton chemical shifts in regular secondary structure or proteins
    • K. Ösapay, and D.A. Case Analysis of proton chemical shifts in regular secondary structure or proteins J. Biomol. NMR 4 1994 215 230
    • (1994) J. Biomol. NMR , vol.4 , pp. 215-230
    • Ösapay, K.1    Case, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.