메뉴 건너뛰기




Volumn 51, Issue 20, 2012, Pages 4198-4205

Replacement of disulfides by amide bonds in the relaxin-like factor (RLF/INSL3) reveals a role for the A11-b10 link in transmembrane signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; AMIDE BOND; AMIDE FUNCTIONALITIES; BINDING AFFINITIES; DISULFIDE BONDS; INTRACELLULAR CAMP; MOLECULAR SURFACES; N-TERMINALS; PEPTIDE BONDS; POLYPEPTIDE CHAIN; RECEPTOR BINDING; SIGNAL ACTIVATION; SIGNAL TRANSMISSION; TRANS-MEMBRANE SIGNALING; TRANSMEMBRANES;

EID: 84861387642     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300352x     Document Type: Review
Times cited : (10)

References (23)
  • 1
    • 0027365039 scopus 로고
    • Cloning of a cDNA for a novel insulin-like peptide of the testicular Leydig cells
    • Adham, I. M., Burkhardt, E., Benahmed, M., and Engel, W. (1993) Cloning of a cDNA for a novel insulin-like peptide of the testicular Leydig cells J. Biol. Chem. 268, 26668-26672
    • (1993) J. Biol. Chem. , vol.268 , pp. 26668-26672
    • Adham, I.M.1    Burkhardt, E.2    Benahmed, M.3    Engel, W.4
  • 2
    • 0029022502 scopus 로고
    • A novel Leydig cell cDNA-derived protein is a relaxin-like factor (RLF)
    • Büllesbach, E. E. and Schwabe, C. (1995) A novel Leydig cell cDNA-derived protein is a relaxin-like factor (RLF) J. Biol. Chem. 270, 16011-16015
    • (1995) J. Biol. Chem. , vol.270 , pp. 16011-16015
    • Büllesbach, E.E.1    Schwabe, C.2
  • 4
    • 80052082999 scopus 로고    scopus 로고
    • Structural insights into agonist-induced activation of G-protein-coupled receptors
    • Deupi, X. and Standfuss, J. (2011) Structural insights into agonist-induced activation of G-protein-coupled receptors Curr. Opin. Struct. Biol. 21, 541-551
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 541-551
    • Deupi, X.1    Standfuss, J.2
  • 5
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR
    • Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., and Wuthrich, K. (2012) Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR Science (New York, N. Y.) 335, 1106-1110
    • (2012) Science (New York, N. Y.) , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wuthrich, K.5
  • 6
    • 17644415042 scopus 로고    scopus 로고
    • LGR8 signal activation by the relaxin-like factor
    • Büllesbach, E. E. and Schwabe, C. (2005) LGR8 signal activation by the relaxin-like factor J. Biol. Chem. 280, 14586-14590
    • (2005) J. Biol. Chem. , vol.280 , pp. 14586-14590
    • Büllesbach, E.E.1    Schwabe, C.2
  • 7
    • 33748746259 scopus 로고    scopus 로고
    • The mode of interaction of the relaxin-like factor (RLF) with the leucine-rich repeat G protein-activated receptor 8
    • Büllesbach, E. E. and Schwabe, C. (2006) The mode of interaction of the relaxin-like factor (RLF) with the leucine-rich repeat G protein-activated receptor 8 J. Biol. Chem. 281, 26136-26143
    • (2006) J. Biol. Chem. , vol.281 , pp. 26136-26143
    • Büllesbach, E.E.1    Schwabe, C.2
  • 8
    • 34548242158 scopus 로고    scopus 로고
    • Structure of the Transmembrane Signal Initiation Site of the Relaxin-Like Factor (RLF/INSL3)
    • Büllesbach, E. E. and Schwabe, C. (2007) Structure of the Transmembrane Signal Initiation Site of the Relaxin-Like Factor (RLF/INSL3) Biochemistry 46, 9722-9727
    • (2007) Biochemistry , vol.46 , pp. 9722-9727
    • Büllesbach, E.E.1    Schwabe, C.2
  • 9
    • 0033621158 scopus 로고    scopus 로고
    • Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
    • Hackeng, T. M., Griffin, J. H., and Dawson, P. E. (1999) Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology Proc. Natl. Acad. Sci. U. S. A. 96, 10068-10073
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10068-10073
    • Hackeng, T.M.1    Griffin, J.H.2    Dawson, P.E.3
  • 10
    • 10044234108 scopus 로고    scopus 로고
    • "One-Pot" preparation of N-carbamate protected amino acids via azide
    • Cruz, L. J., Beteta, N. G., Ewenson, A., and Albericio, F. (2004) "One-Pot" preparation of N-carbamate protected amino acids via azide Org. Process Res. Dev. 8, 920-924
    • (2004) Org. Process Res. Dev. , vol.8 , pp. 920-924
    • Cruz, L.J.1    Beteta, N.G.2    Ewenson, A.3    Albericio, F.4
  • 11
    • 0026559336 scopus 로고
    • Synthesis of bombyxin-IV, an insulin superfamily peptide from the silkworm, bombyx mori, by stepwise and selective formation of three disulfide bridges
    • Maruyama, K., Nagata, K., Tanaka, M., Nagasawa, H., Isogai, A., Ishizaki, H., and Suzuki, A. (1992) Synthesis of bombyxin-IV, an insulin superfamily peptide from the silkworm, bombyx mori, by stepwise and selective formation of three disulfide bridges J. Protein Chem. 11, 1-12
    • (1992) J. Protein Chem. , vol.11 , pp. 1-12
    • Maruyama, K.1    Nagata, K.2    Tanaka, M.3    Nagasawa, H.4    Isogai, A.5    Ishizaki, H.6    Suzuki, A.7
  • 12
    • 0025870325 scopus 로고
    • Total synthesis of human relaxin and human relaxin derivatives by solid phase peptide synthesis and site-directed chain combination
    • Büllesbach, E. E. and Schwabe, C. (1991) Total synthesis of human relaxin and human relaxin derivatives by solid phase peptide synthesis and site-directed chain combination J. Biol. Chem. 266, 10754-10761
    • (1991) J. Biol. Chem. , vol.266 , pp. 10754-10761
    • Büllesbach, E.E.1    Schwabe, C.2
  • 13
    • 0025014627 scopus 로고
    • PyBop: A new peptide coupling reagent devoid of toxic by-products
    • Coste, J., Le-Nguyen, D., and Castro, B. (1990) PyBop: A new peptide coupling reagent devoid of toxic by-products Tetrahedron Lett. 31, 205-208
    • (1990) Tetrahedron Lett. , vol.31 , pp. 205-208
    • Coste, J.1    Le-Nguyen, D.2    Castro, B.3
  • 14
    • 2542509060 scopus 로고    scopus 로고
    • Specific, high-affinity relaxin-like factor receptors
    • Büllesbach, E. E. and Schwabe, C. (1999) Specific, high-affinity relaxin-like factor receptors J. Biol. Chem. 274, 22354-22358
    • (1999) J. Biol. Chem. , vol.274 , pp. 22354-22358
    • Büllesbach, E.E.1    Schwabe, C.2
  • 15
    • 0013583354 scopus 로고
    • Cyclic AMP and cyclic GMP
    • (Jaffe, B. M. and Behrman, H. R. Eds.) pp, Academic Press, New York.
    • Steiner, A. L. (1979) Cyclic AMP and cyclic GMP, in Methods of Hormone Radioimmunoassay (Jaffe, B. M. and Behrman, H. R., Eds.) pp 3-17, Academic Press, New York.
    • (1979) Methods of Hormone Radioimmunoassay , pp. 3-17
    • Steiner, A.L.1
  • 17
    • 57649134244 scopus 로고    scopus 로고
    • The solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor (RLF)
    • Büllesbach, E. E., Hass, M. A. S., Jensen, M. R., Hansen, D. F., Kristensen, S., Schwabe, C., and Led, J. J. (2008) The solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor (RLF) Biochemistry 47, 13308-13317
    • (2008) Biochemistry , vol.47 , pp. 13308-13317
    • Büllesbach, E.E.1    Hass, M.A.S.2    Jensen, M.R.3    Hansen, D.F.4    Kristensen, S.5    Schwabe, C.6    Led, J.J.7
  • 18
    • 85004754595 scopus 로고
    • Side reactions in peptide synthesis
    • Bodanszky, M. and Martinez, J. (1981) Side reactions in peptide synthesis Synthesis 333-356
    • (1981) Synthesis , pp. 333-356
    • Bodanszky, M.1    Martinez, J.2
  • 19
    • 3042658646 scopus 로고    scopus 로고
    • Synthetic cross-links arrest the C-terminal region of the relaxin-like factor (RLF) in an active conformation
    • Büllesbach, E. E. and Schwabe, C. (2004) Synthetic cross-links arrest the C-terminal region of the relaxin-like factor (RLF) in an active conformation Biochemistry 43, 8021-8028
    • (2004) Biochemistry , vol.43 , pp. 8021-8028
    • Büllesbach, E.E.1    Schwabe, C.2
  • 20
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L. and Wallace, B. A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases Biopolymers 89, 392-400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 21
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L. and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32, W668-673
    • (2004) Nucleic Acids Res. , vol.32 , pp. 668-673
    • Whitmore, L.1    Wallace, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.