메뉴 건너뛰기




Volumn 189, Issue , 2014, Pages 25-32

Characterization of an aphid-specific, cysteine-rich protein enriched in salivary glands

Author keywords

Aphid; Cysteine rich protein; Gene interference; Salivary gland; Zinc ion binding

Indexed keywords

CYSTEINE; GLOBULAR PROTEIN; MONOMER; PROTEIN ACYPI39568; SALIVA PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 84898649644     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2014.03.006     Document Type: Article
Times cited : (20)

References (51)
  • 2
    • 84898649636 scopus 로고    scopus 로고
    • Aphid saliva
    • P.W. Miles Aphid saliva Biol. Rev. 77 1999 71 85
    • (1999) Biol. Rev. , vol.77 , pp. 71-85
    • Miles, P.W.1
  • 4
    • 33644929267 scopus 로고    scopus 로고
    • Salivary secretions by aphids interacting with proteins of phloem wound responses
    • W.F. Tjallingii Salivary secretions by aphids interacting with proteins of phloem wound responses J. Exp. Bot. 57 2006 739 745
    • (2006) J. Exp. Bot. , vol.57 , pp. 739-745
    • Tjallingii, W.F.1
  • 6
    • 78649688383 scopus 로고    scopus 로고
    • A functional genomics approach identifies candidate effectors from the aphid species Myzus persicae (green peach aphid)
    • J.I. Bos, D. Prince, M. Pitino, M.E. Maffei, J. Win, and S.A. Hogenhout A functional genomics approach identifies candidate effectors from the aphid species Myzus persicae (green peach aphid) PLoS Genet. 6 2010 e1001216
    • (2010) PLoS Genet. , vol.6 , pp. 1001216
    • Bos, J.I.1    Prince, D.2    Pitino, M.3    Maffei, M.E.4    Win, J.5    Hogenhout, S.A.6
  • 7
    • 84864319400 scopus 로고    scopus 로고
    • Polymorphisms in salivary-gland transcripts of Russian wheat aphid biotypes 1 and 2
    • F. Cui, C.M. Smith, J. Reese, O. Edwards, and G. Reeck Polymorphisms in salivary-gland transcripts of Russian wheat aphid biotypes 1 and 2 Insect Sci. 19 2012 429 440
    • (2012) Insect Sci. , vol.19 , pp. 429-440
    • Cui, F.1    Smith, C.M.2    Reese, J.3    Edwards, O.4    Reeck, G.5
  • 8
    • 84881613997 scopus 로고    scopus 로고
    • The role of protein effectors in plant-aphid interactions
    • D.A. Elzing, and G. Jander The role of protein effectors in plant-aphid interactions Curr. Opin. Plant Biol. 16 2013 451 456
    • (2013) Curr. Opin. Plant Biol. , vol.16 , pp. 451-456
    • Elzing, D.A.1    Jander, G.2
  • 10
    • 64849087712 scopus 로고    scopus 로고
    • The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry
    • J.C. Carolan, C.I.J. Fitzroy, P.D. Ashton, A.E. Douglas, and T.L. Wilkinson The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry Proteomics 9 2009 2457 2467
    • (2009) Proteomics , vol.9 , pp. 2457-2467
    • Carolan, J.C.1    Fitzroy, C.I.J.2    Ashton, P.D.3    Douglas, A.E.4    Wilkinson, T.L.5
  • 11
    • 84874531848 scopus 로고    scopus 로고
    • Proteomic profiling of cereal aphid saliva reveals both ubiquitous and adaptive secreted proteins
    • S.A. Rao, J.C. Carolan, and T.L. Wilkinson Proteomic profiling of cereal aphid saliva reveals both ubiquitous and adaptive secreted proteins PLoS One 8 2013 e57413
    • (2013) PLoS One , vol.8 , pp. 57413
    • Rao, S.A.1    Carolan, J.C.2    Wilkinson, T.L.3
  • 12
    • 76649095683 scopus 로고    scopus 로고
    • Salivary proteins of Russian wheat aphid (Hemiptera: Aphididae)
    • W.R. Cooper, J.W. Dillwith, and G.J. Puterka Salivary proteins of Russian wheat aphid (Hemiptera: Aphididae) Environ. Entomol. 39 2010 223 231
    • (2010) Environ. Entomol. , vol.39 , pp. 223-231
    • Cooper, W.R.1    Dillwith, J.W.2    Puterka, G.J.3
  • 13
    • 79951643195 scopus 로고    scopus 로고
    • Comparisons of salivary proteins from five aphid (Hemiptera: Aphididae) species
    • W.R. Cooper, J.W. Dillwith, and G.J. Puterka Comparisons of salivary proteins from five aphid (Hemiptera: Aphididae) species Environ. Entomol. 40 2011 151 156
    • (2011) Environ. Entomol. , vol.40 , pp. 151-156
    • Cooper, W.R.1    Dillwith, J.W.2    Puterka, G.J.3
  • 14
    • 33750585000 scopus 로고    scopus 로고
    • RNAi knockdown of a salivary transcript leading to lethality in the pea aphid, Acyrthosiphon pisum
    • N.S. Mutti, Y. Park, J.C. Reese, and G.R. Reeck RNAi knockdown of a salivary transcript leading to lethality in the pea aphid, Acyrthosiphon pisum J. Insect Sci. 6 2006 1 7
    • (2006) J. Insect Sci. , vol.6 , pp. 1-7
    • Mutti, N.S.1    Park, Y.2    Reese, J.C.3    Reeck, G.R.4
  • 16
    • 84898613381 scopus 로고    scopus 로고
    • Cloning and expression profiling of a saliva protein family at different developmental stages in Acyrthosiphon pisum (Hemiptera: Aphididae)
    • Y. Zhang, G.X. Wu, K. Guo, W. Wang, X.P. Ding, S.M. Song, Y.Y. Xu, and F. Cui Cloning and expression profiling of a saliva protein family at different developmental stages in Acyrthosiphon pisum (Hemiptera: Aphididae) Acta Entomol. Sin. 54 2011 1445 1451
    • (2011) Acta Entomol. Sin. , vol.54 , pp. 1445-1451
    • Zhang, Y.1    Wu, G.X.2    Guo, K.3    Wang, W.4    Ding, X.P.5    Song, S.M.6    Xu, Y.Y.7    Cui, F.8
  • 17
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • T.N. Petersen, S. Brunak, G. von Heijne, and H. Nielsen SignalP 4.0: discriminating signal peptides from transmembrane regions Nat. Methods 8 2011 785 786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 21
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Y. Zhang I-TASSER server for protein 3D structure prediction BMC Bioinforma. 9 2008 40
    • (2008) BMC Bioinforma. , vol.9 , pp. 40
    • Zhang, Y.1
  • 22
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • A. Roy, A. Kucukural, and Y. Zhang I-TASSER: a unified platform for automated protein structure and function prediction Nat. Protoc. 5 2010 725 738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 23
    • 84864460609 scopus 로고    scopus 로고
    • COFACTOR: An accurate comparative algorithm for structure-based protein function annotation
    • A. Roy, J. Yang, and Y. Zhang COFACTOR: an accurate comparative algorithm for structure-based protein function annotation Nucleic Acids Res. 40 2012 W471 W477
    • (2012) Nucleic Acids Res. , vol.40
    • Roy, A.1    Yang, J.2    Zhang, Y.3
  • 24
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95 98 NT
    • T. Hall BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95 98 NT Nucleic Acids Symp. Ser. 41 1999 95 98
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.1
  • 25
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 28 2011 2731 2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 27
    • 0001196169 scopus 로고
    • Influence of the amino acid balance on the improvement of an artificial diet for a biotype of Acyrthosiphon pisum (Homoptera: Aphididae)
    • G. Febvay, B. Delobel, and Y. Rahbe Influence of the amino acid balance on the improvement of an artificial diet for a biotype of Acyrthosiphon pisum (Homoptera: Aphididae) Can. J. Zool. 66 1988 2449 2453
    • (1988) Can. J. Zool. , vol.66 , pp. 2449-2453
    • Febvay, G.1    Delobel, B.2    Rahbe, Y.3
  • 28
  • 29
    • 0037322912 scopus 로고    scopus 로고
    • The CRP/MLP/TLP family of LIM domain proteins: Acting by connecting
    • DOI 10.1002/bies.10226
    • R. Weiskirchen, and K. Günther The CRP/MLP/TLP family of LIM domain proteins: acting by connecting Bioessays 25 2003 152 162 (Pubitemid 36222386)
    • (2003) BioEssays , vol.25 , Issue.2 , pp. 152-162
    • Weiskirchen, R.1    Gunther, K.2
  • 32
    • 0036166750 scopus 로고    scopus 로고
    • EsMlp, a muscle-LIM protein gene, is up-regulated during cold exposure in the freeze-avoiding larvae of Epiblema scudderiana
    • T. Bilgen, T.E. English, D.C. McMullen, and K.B. Storey EsMlp, a muscle-LIM protein gene, is up-regulated during cold exposure in the freeze-avoiding larvae of Epiblema scudderiana Cryobiology 43 2001 11 20 (Pubitemid 33779291)
    • (2001) Cryobiology , vol.43 , Issue.1 , pp. 11-20
    • Bilgen, T.1    English, T.E.2    McMullen, D.C.3    Storey, K.B.4
  • 33
    • 4043092774 scopus 로고    scopus 로고
    • Structure and function of snake venom cysteine-rich secretory proteins
    • DOI 10.1016/j.toxicon.2004.05.023, PII S0041010104002090
    • Y. Yamazaki, and T. Morita Structure and function of snake venom cysteine-rich secretory proteins Toxicon 44 2004 227 231 (Pubitemid 39078338)
    • (2004) Toxicon , vol.44 , Issue.3 , pp. 227-231
    • Yamazaki, Y.1    Morita, T.2
  • 36
    • 34447290640 scopus 로고    scopus 로고
    • Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation
    • DOI 10.1111/j.1745-7262.2007.00283.x, The Epididymis: The Proceedings of the 4th Epididymal Workshop
    • D.J. Cohen, V.G. Da Ros, D. Busso, D.A. Ellerman, J.A. Maldera, N. Goldweic, and P.S. Cuasnicú Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation Asian J. Androl. 9 2007 528 532 (Pubitemid 47046159)
    • (2007) Asian Journal of Andrology , vol.9 , Issue.4 , pp. 528-532
    • Cohen, D.J.1    Da Ros, V.G.2    Busso, D.3    Ellerman, D.A.4    Maldera, J.A.5    Goldweic, N.6    Cuasnicu, P.S.7
  • 37
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • DOI 10.1006/jmbi.1999.3161
    • S. Busby, and R. Ebright Transcription activation by catabolite activator protein (CAP) J. Mol. Biol. 293 1999 199 213 (Pubitemid 29516164)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 38
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • DOI 10.1006/jmbi.1995.0635
    • J. Darlix, M. Lapadat-Tapolsky, H. de Rocquigny, and B.P. roques First glimpses at structure function relationships of the nucleocapsid protein of retrovirused J. Mol. Biol. 254 1995 523 537 (Pubitemid 26001788)
    • (1995) Journal of Molecular Biology , vol.254 , Issue.4 , pp. 523-537
    • Darlix, J.-L.1    Lapadat-Tapolsky, M.2    De Rocquigny, H.3    Roques, B.P.4
  • 39
    • 0028244266 scopus 로고
    • Multiple genetic determinants of barley stripe mosaic virus influence lesion phenotype on Chenopodium amaranticolor
    • I. Petty, R. donald, and A. Jackson Multiple genetic determinants of barley stripe mosaic virus influence lesion phenotype on Chenopodium amaranticolor Virology 198 1994 218 226
    • (1994) Virology , vol.198 , pp. 218-226
    • Petty, I.1    Donald, R.2    Jackson, A.3
  • 40
    • 0026697174 scopus 로고
    • Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain
    • T.H. Bestor Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain EMBO J. 11 1992 2611 2617
    • (1992) EMBO J. , vol.11 , pp. 2611-2617
    • Bestor, T.H.1
  • 43
    • 0025247728 scopus 로고
    • The trithorax gene, a trans-acting regulator of the bithorax complex in Drosophila, encodes a protein with zinc-binding domains
    • A.M. Mazo, D.H. Huang, B.A. Mozer, and I.B. Dawid The trithorax gene, a trans-acting regulator of the bithorax complex in Drosophila, encodes a protein with zinc-binding domains Proc. Natl. Acad. Sci. U. S. A. 87 1990 2112 2116
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2112-2116
    • Mazo, A.M.1    Huang, D.H.2    Mozer, B.A.3    Dawid, I.B.4
  • 44
    • 0038492426 scopus 로고    scopus 로고
    • MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein
    • Z.B. Xia MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein Proc. Natl. Acad. Sci. U. S. A. 100 2003 8342 8347
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8342-8347
    • Xia, Z.B.1
  • 46
    • 0026576377 scopus 로고
    • The cysteine-rich protein gene family of Giardia lamblia
    • R.D. Adam, Y.M. Yang, and T.E. Nash The cysteine-rich protein gene family of Giardia lamblia Mol. Cell. Biol. 12 1992 1194 1201
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1194-1201
    • Adam, R.D.1    Yang, Y.M.2    Nash, T.E.3
  • 47
    • 0038558159 scopus 로고    scopus 로고
    • The CXC motif: A functional mimic of protein disulfide isomerase
    • DOI 10.1021/bi026993q
    • K.J. Woycechowsky, and R.T. Raines The CXC motif: a functional mimic of protein disulfide isomerase Biochemistry 42 2003 5387 5394 (Pubitemid 36560435)
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5387-5394
    • Woycechowsky, K.J.1    Raines, R.T.2
  • 50
    • 70349492918 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding
    • G. Cacciapuoti, I. Peluso, F. Fuccio, and M. Porcelli Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding FEBS J. 276 2009 5799 5805
    • (2009) FEBS J. , vol.276 , pp. 5799-5805
    • Cacciapuoti, G.1    Peluso, I.2    Fuccio, F.3    Porcelli, M.4
  • 51
    • 84886260142 scopus 로고    scopus 로고
    • An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1 cartilage-associated protein cyclophilin B the CXXXC motif reveals disulfide isomerase activity in vitro
    • Y. Ishikawa, and H.P. Bächinger An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1 cartilage-associated protein cyclophilin B the CXXXC motif reveals disulfide isomerase activity in vitro J. Biol. Chem. 288 2013 31437 31446
    • (2013) J. Biol. Chem. , vol.288 , pp. 31437-31446
    • Ishikawa, Y.1    Bächinger, H.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.