메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Moonlighting peptides with emerging function

(16)  Rodríguez Plaza, Jonathan G a   Villalón Rojas, Amanda a   Herrera, Sur a   Garza Ramos, Georgina b   Torres Larios, Alfredo a   Amero, Carlos c   Zarraga Granados, Gabriela d   Gutiérrez Aguilar, Manuel a   Lara Ortiz, María Teresa a   Polanco Gonzalez, Carlos a,g   Uribe Carvajal, Salvador a   Coria, Roberto a   Peña Díaz, Antonio a   Bredesen, Dale E e,f   Castro Obregon, Susana d   del Rio, Gabriel a  


Author keywords

[No Author keywords available]

Indexed keywords

ALPHA PHEROMONE; HUNTER LIKE PEPTIDE; LZTI PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84863767872     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040125     Document Type: Article
Times cited : (16)

References (36)
  • 1
  • 2
    • 70349501959 scopus 로고    scopus 로고
    • Anticancer activity of targeted proapoptotic peptides and chemotherapy is highly improved by targeted cell surface calreticulin-inducer peptides
    • Obeid M, (2009) Anticancer activity of targeted proapoptotic peptides and chemotherapy is highly improved by targeted cell surface calreticulin-inducer peptides. Mol Cancer Ther 8: 2693-2707.
    • (2009) Mol Cancer Ther , vol.8 , pp. 2693-2707
    • Obeid, M.1
  • 4
    • 0032535999 scopus 로고    scopus 로고
    • Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model
    • Arap W, Pasqualini R, Ruoslahti E, (1998) Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model. Science 279: 377-380.
    • (1998) Science , vol.279 , pp. 377-380
    • Arap, W.1    Pasqualini, R.2    Ruoslahti, E.3
  • 5
  • 6
    • 2942703809 scopus 로고    scopus 로고
    • Reversal of obesity by targeted ablation of adipose tissue
    • Kolonin MG, Saha PK, Chan L, Pasqualini R, Arap W, (2004) Reversal of obesity by targeted ablation of adipose tissue. Nat Med 10: 625-632.
    • (2004) Nat Med , vol.10 , pp. 625-632
    • Kolonin, M.G.1    Saha, P.K.2    Chan, L.3    Pasqualini, R.4    Arap, W.5
  • 8
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery CJ, (1999) Moonlighting proteins. Trends Biochem Sci 24: 8-11.
    • (1999) Trends Biochem Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 9
    • 0042706146 scopus 로고    scopus 로고
    • Moonlighting proteins: old proteins learning new tricks
    • Jeffery CJ, (2003) Moonlighting proteins: old proteins learning new tricks. Trends Genet 19: 415-417.
    • (2003) Trends Genet , vol.19 , pp. 415-417
    • Jeffery, C.J.1
  • 10
    • 62949096122 scopus 로고    scopus 로고
    • Moonlighting proteins-an update
    • Jeffery CJ, (2009) Moonlighting proteins-an update. Mol Biosyst 5: 345-350.
    • (2009) Mol Biosyst , vol.5 , pp. 345-350
    • Jeffery, C.J.1
  • 11
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P, Szasz C, Buday L, (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30: 484-489.
    • (2005) Trends Biochem Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 12
    • 67650045816 scopus 로고    scopus 로고
    • Limitations of induced folding in molecular recognition by intrinsically disordered proteins
    • Hazy E, Tompa P, (2009) Limitations of induced folding in molecular recognition by intrinsically disordered proteins. Chemphyschem 10: 1415-1419.
    • (2009) Chemphyschem , vol.10 , pp. 1415-1419
    • Hazy, E.1    Tompa, P.2
  • 13
    • 33846687903 scopus 로고    scopus 로고
    • Developmental biology: moonlighting at the pole
    • Rusten TE, Stenmark H, (2007) Developmental biology: moonlighting at the pole. Nature 445: 497-499.
    • (2007) Nature , vol.445 , pp. 497-499
    • Rusten, T.E.1    Stenmark, H.2
  • 14
    • 68249102600 scopus 로고    scopus 로고
    • Mechanism of ligand-induced folding of a natively unfolded helixless variant of rabbit I-BABP
    • Rea AM, Thurston V, Searle MS, (2009) Mechanism of ligand-induced folding of a natively unfolded helixless variant of rabbit I-BABP. Biochemistry 48: 7556-7564.
    • (2009) Biochemistry , vol.48 , pp. 7556-7564
    • Rea, A.M.1    Thurston, V.2    Searle, M.S.3
  • 15
    • 9944225262 scopus 로고    scopus 로고
    • Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins
    • Jeffery CJ, (2004) Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins. Curr Opin Struct Biol 14: 663-668.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 663-668
    • Jeffery, C.J.1
  • 16
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla US, Iyengar R, (1999) Emergent properties of networks of biological signaling pathways. Science 283: 381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 17
    • 0032497360 scopus 로고    scopus 로고
    • Synthesis, biological activity, and conformational analysis of peptidomimetic analogues of the Saccharomyces cerevisiae alpha-factor tridecapeptide
    • Zhang YL, Marepalli HR, Lu HF, Becker JM, Naider F, (1998) Synthesis, biological activity, and conformational analysis of peptidomimetic analogues of the Saccharomyces cerevisiae alpha-factor tridecapeptide. Biochemistry 37: 12465-12476.
    • (1998) Biochemistry , vol.37 , pp. 12465-12476
    • Zhang, Y.L.1    Marepalli, H.R.2    Lu, H.F.3    Becker, J.M.4    Naider, F.5
  • 18
    • 0027468091 scopus 로고
    • Conformational analysis of [D-Ala9]alpha-factor and [L-Ala9]alpha-factor in solution and in the presence of lipid
    • Gounarides JS, Broido MS, Becker JM, Naider FR, (1993) Conformational analysis of [D-Ala9]alpha-factor and [L-Ala9]alpha-factor in solution and in the presence of lipid. Biochemistry 32: 908-917.
    • (1993) Biochemistry , vol.32 , pp. 908-917
    • Gounarides, J.S.1    Broido, M.S.2    Becker, J.M.3    Naider, F.R.4
  • 19
    • 0022371697 scopus 로고
    • Biological activity and conformational isomerism in position 9 analogues of the des-1-tryptophan,3-beta-cyclohexylalanine-alpha-factor from Saccharomyces cerevisiae
    • Shenbagamurthi P, Kundu B, Raths S, Becker JM, Naider F, (1985) Biological activity and conformational isomerism in position 9 analogues of the des-1-tryptophan,3-beta-cyclohexylalanine-alpha-factor from Saccharomyces cerevisiae. Biochemistry 24: 7070-7076.
    • (1985) Biochemistry , vol.24 , pp. 7070-7076
    • Shenbagamurthi, P.1    Kundu, B.2    Raths, S.3    Becker, J.M.4    Naider, F.5
  • 20
    • 0028964831 scopus 로고
    • Systematic analysis of the Saccharomyces cerevisiae alpha-factor containing lactam constraints of different ring size
    • Yang W, McKinney A, Becker JM, Naider F, (1995) Systematic analysis of the Saccharomyces cerevisiae alpha-factor containing lactam constraints of different ring size. Biochemistry 34: 1308-1315.
    • (1995) Biochemistry , vol.34 , pp. 1308-1315
    • Yang, W.1    McKinney, A.2    Becker, J.M.3    Naider, F.4
  • 21
    • 0031877397 scopus 로고    scopus 로고
    • Structure-function analysis of the Saccharomyces cerevisiae tridecapeptide pheromone using alanine-scanned analogs
    • Abel MG, Zhang YL, Lu HF, Naider F, Becker JM, (1998) Structure-function analysis of the Saccharomyces cerevisiae tridecapeptide pheromone using alanine-scanned analogs. J Pept Res 52: 95-106.
    • (1998) J Pept Res , vol.52 , pp. 95-106
    • Abel, M.G.1    Zhang, Y.L.2    Lu, H.F.3    Naider, F.4    Becker, J.M.5
  • 22
    • 0023839137 scopus 로고
    • Evidence for preferential multiplication of the internal unit in tandem repeats of the mating factor alpha genes in Saccharomyces yeasts
    • Kitada K, Hishinuma F, (1988) Evidence for preferential multiplication of the internal unit in tandem repeats of the mating factor alpha genes in Saccharomyces yeasts. Curr Genet 13: 1-5.
    • (1988) Curr Genet , vol.13 , pp. 1-5
    • Kitada, K.1    Hishinuma, F.2
  • 23
    • 47049120414 scopus 로고    scopus 로고
    • The asexual yeast Candida glabrata maintains distinct a and alpha haploid mating types
    • Muller H, Hennequin C, Gallaud J, Dujon B, Fairhead C, (2008) The asexual yeast Candida glabrata maintains distinct a and alpha haploid mating types. Eukaryot Cell 7: 848-858.
    • (2008) Eukaryot Cell , vol.7 , pp. 848-858
    • Muller, H.1    Hennequin, C.2    Gallaud, J.3    Dujon, B.4    Fairhead, C.5
  • 24
    • 0035851161 scopus 로고    scopus 로고
    • Identification of residues of the Saccharomyces cerevisiae G protein-coupled receptor contributing to alpha-factor pheromone binding
    • Lee BK, Khare S, Naider F, Becker JM, (2001) Identification of residues of the Saccharomyces cerevisiae G protein-coupled receptor contributing to alpha-factor pheromone binding. J Biol Chem 276: 37950-37961.
    • (2001) J Biol Chem , vol.276 , pp. 37950-37961
    • Lee, B.K.1    Khare, S.2    Naider, F.3    Becker, J.M.4
  • 25
    • 0023139708 scopus 로고
    • Conformations of yeast alpha-mating factor and analog peptides as bound to phospholipid bilayer. Correlation of membrane-bound conformation with physiological activity
    • Wakamatsu K, Okada A, Miyazawa T, Masui Y, Sakakibara S, et al. (1987) Conformations of yeast alpha-mating factor and analog peptides as bound to phospholipid bilayer. Correlation of membrane-bound conformation with physiological activity. Eur J Biochem 163: 331-338.
    • (1987) Eur J Biochem , vol.163 , pp. 331-338
    • Wakamatsu, K.1    Okada, A.2    Miyazawa, T.3    Masui, Y.4    Sakakibara, S.5
  • 26
    • 0018928567 scopus 로고
    • Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone
    • Hartwell LH, (1980) Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J Cell Biol 85: 811-822.
    • (1980) J Cell Biol , vol.85 , pp. 811-822
    • Hartwell, L.H.1
  • 27
    • 0037007151 scopus 로고    scopus 로고
    • Pheromone induces programmed cell death in S. cerevisiae
    • Severin FF, Hyman AA, (2002) Pheromone induces programmed cell death in S. cerevisiae. Curr Biol 12: R233-235.
    • (2002) Curr Biol , vol.12
    • Severin, F.F.1    Hyman, A.A.2
  • 28
    • 33746628909 scopus 로고    scopus 로고
    • Multiple signaling pathways regulate yeast cell death during the response to mating pheromones
    • Zhang NN, Dudgeon DD, Paliwal S, Levchenko A, Grote E, et al. (2006) Multiple signaling pathways regulate yeast cell death during the response to mating pheromones. Mol Biol Cell 17: 3409-3422.
    • (2006) Mol Biol Cell , vol.17 , pp. 3409-3422
    • Zhang, N.N.1    Dudgeon, D.D.2    Paliwal, S.3    Levchenko, A.4    Grote, E.5
  • 31
    • 0027248360 scopus 로고
    • Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3
    • Low PS, Rathinavelu P, Harrison ML, (1993) Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3. J Biol Chem 268: 14627-14631.
    • (1993) J Biol Chem , vol.268 , pp. 14627-14631
    • Low, P.S.1    Rathinavelu, P.2    Harrison, M.L.3
  • 32
    • 0023040601 scopus 로고
    • Nuclear-magnetic-resonance studies on the conformation of membrane-bound alpha-mating factor. Transferred nuclear Overhauser effect analysis
    • Wakamatsu K, Okada A, Suzuki M, Higashijima T, Masui Y, et al. (1986) Nuclear-magnetic-resonance studies on the conformation of membrane-bound alpha-mating factor. Transferred nuclear Overhauser effect analysis. Eur J Biochem 154: 607-615.
    • (1986) Eur J Biochem , vol.154 , pp. 607-615
    • Wakamatsu, K.1    Okada, A.2    Suzuki, M.3    Higashijima, T.4    Masui, Y.5
  • 33
    • 0037444667 scopus 로고    scopus 로고
    • Matrix volume measurements challenge the existence of diazoxide/glibencamide-sensitive KATP channels in rat mitochondria
    • Das M, Parker JE, Halestrap AP, (2003) Matrix volume measurements challenge the existence of diazoxide/glibencamide-sensitive KATP channels in rat mitochondria. J Physiol 547: 893-902.
    • (2003) J Physiol , vol.547 , pp. 893-902
    • Das, M.1    Parker, J.E.2    Halestrap, A.P.3
  • 34
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, R.W Woody, (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287: 252-60.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 35
    • 0029595442 scopus 로고
    • SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C, Deleage G, (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 11: 681-684.
    • (1995) Comput Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    de leage, G.2
  • 36
    • 0035853462 scopus 로고    scopus 로고
    • APAP, a sequence-pattern recognition approach identifies substance P as a potential apoptotic peptide
    • del Rio G, Castro-Obregon S, Rao R, Ellerby HM, Bredesen DE, (2001) APAP, a sequence-pattern recognition approach identifies substance P as a potential apoptotic peptide. FEBS Lett 494: 213-219.
    • (2001) FEBS Lett , vol.494 , pp. 213-219
    • del Rio, G.1    Castro-Obregon, S.2    Rao, R.3    Ellerby, H.M.4    Bredesen, D.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.