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Volumn 12, Issue , 2012, Pages

High abundance of Serine/Threonine-rich regions predicted to be hyper-O-glycosylated in the secretory proteins coded by eight fungal genomes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; SECRETORY PROTEIN; SERINE; THREONINE;

EID: 84866483646     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-12-213     Document Type: Article
Times cited : (38)

References (32)
  • 1
    • 0035077832 scopus 로고    scopus 로고
    • O-glycosylation of the mucin type
    • 11308013
    • O-glycosylation of the mucin type. Hanisch FG, Biol Chem 2001 382 143 149 11308013
    • (2001) Biol Chem , vol.382 , pp. 143-149
    • Hanisch, F.G.1
  • 2
    • 34347327263 scopus 로고    scopus 로고
    • Protein O-glycosylation in fungi: Diverse structures and multiple functions
    • DOI 10.1271/bbb.70080
    • Protein O-glycosylation in fungi: diverse structures and multiple functions. Goto M, Biosci Biotechnol Biochem 2007 71 1415 1427 10.1271/bbb.70080 17587671 (Pubitemid 47012011)
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , Issue.6 , pp. 1415-1427
    • Goto, M.1
  • 3
    • 67650159384 scopus 로고    scopus 로고
    • Protein O-mannosylation: Conserved from bacteria to humans
    • 10.1093/glycob/cwp066 19429925
    • Protein O-mannosylation: conserved from bacteria to humans. Lommel M, Strahl S, Glycobiology 2009 19 816 10.1093/glycob/cwp066 19429925
    • (2009) Glycobiology , vol.19 , pp. 816
    • Lommel, M.1    Strahl, S.2
  • 4
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: A model organism helps elucidate congenital human diseases
    • DOI 10.1002/anie.200601645
    • Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Lehle L, Strahl S, Tanner W, Angew Chem Int Ed Engl 2006 45 6802 6818 10.1002/anie.200601645 17024709 (Pubitemid 44654465)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.41 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 5
    • 72049102104 scopus 로고    scopus 로고
    • The O-Mannosyltransferase PMT4 Is essential for normal appressorium formation and penetration in Ustilago maydis
    • 10.1105/tpc.109.065839 19880800
    • The O-Mannosyltransferase PMT4 Is essential for normal appressorium formation and penetration in Ustilago maydis. Fernández-Álvarez A, Elías-Villalobos A, Ibeas JI, Plant Cell 2009 21 3397 3412 10.1105/tpc.109.065839 19880800
    • (2009) Plant Cell , vol.21 , pp. 3397-3412
    • Fernández-Álvarez, A.1    Elías-Villalobos, A.2    Ibeas, J.I.3
  • 8
    • 77955279149 scopus 로고    scopus 로고
    • The role of mucin-type O-glycans in eukaryotic development
    • 10.1016/j.semcdb.2010.02.001 20144722
    • The role of mucin-type O-glycans in eukaryotic development. Tabak LA, Semin Cell Dev Biol 2010 21 616 621 10.1016/j.semcdb.2010.02.001 20144722
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 616-621
    • Tabak, L.A.1
  • 10
    • 3042842452 scopus 로고    scopus 로고
    • Bioinformatic identification of polymerizing and transmembrane mucins in the puffer fish Fugu rubripes
    • DOI 10.1093/glycob/cwh066
    • Bioinformatic identification of polymerizing and transmembrane mucins in the puffer fish Fugu rubripes. Lang T, Alexandersson M, Hansson GC, Samuelsson T, Glycobiology 2004 14 521 527 10.1093/glycob/cwh066 15044386 (Pubitemid 38868266)
    • (2004) Glycobiology , vol.14 , Issue.6 , pp. 521-527
    • Lang, T.1    Alexandersson, M.2    Hansson, G.C.3    Samuelsson, T.4
  • 11
    • 28944444705 scopus 로고    scopus 로고
    • Botrytis cinerea endo-β-1,4-glucanase Cel5A is expressed during infection but is not required for pathogenesis
    • DOI 10.1016/j.pmpp.2005.06.005, PII S0885576505001244
    • Botrytis cinerea endo-ß-1,4-glucanase Cel5A is expressed during infection but is not required for pathogenesis. Espino JJ, Brito N, Noda J, González C, Physiol Mol Plant Pathol 2005 66 213 221 10.1016/j.pmpp.2005. 06.005 (Pubitemid 41785477)
    • (2005) Physiological and Molecular Plant Pathology , vol.66 , Issue.6 , pp. 213-221
    • Espino, J.J.1    Brito, N.2    Noda, J.3    Gonzalez, C.4
  • 12
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • DOI 10.1093/glycob/cwh151
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. Julenius K, Molgaard A, Gupta R, Brunak S, Glycobiology 2005 15 153 164 15385431 (Pubitemid 40227920)
    • (2005) Glycobiology , vol.15 , Issue.2 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 14
    • 73649139554 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation-putting the pieces together
    • 10.1111/j.1742-4658.2009.07429.x 19919547
    • Mucin-type O-glycosylation-putting the pieces together. Jensen PH, Kolarich D, Packer NH, FEBS J 2010 277 81 94 10.1111/j.1742-4658.2009.07429.x 19919547
    • (2010) FEBS J , vol.277 , pp. 81-94
    • Jensen, P.H.1    Kolarich, D.2    Packer, N.H.3
  • 17
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics
    • 10.1093/nar/gkn663 18838391
    • The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B, Nucl Acids Res 2009 37 233 D238 10.1093/nar/gkn663 18838391
    • (2009) Nucl Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 18
    • 18744414791 scopus 로고    scopus 로고
    • Identification of GPI anchor attachment signals by a Kohonen self-organizing map
    • DOI 10.1093/bioinformatics/bti299
    • Identification of GPI anchor attachment signals by a Kohonen self-organizing map. Fankhauser N, Maser P, Bioinformatics 2005 21 1846 1852 10.1093/bioinformatics/bti299 15691858 (Pubitemid 40668020)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 1846-1852
    • Fankhauser, N.1    Maser, P.2
  • 19
    • 1442348239 scopus 로고    scopus 로고
    • A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • DOI 10.1016/j.jmb.2004.01.025, PII S002228360400083X
    • A Sensitive Predictor for Potential GPI Lipid Modification Sites in Fungal Protein Sequences and its Application to Genome-wide Studies for Aspergillus nidulans, Candida albicans Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe. Eisenhaber B, Schneider G, Wildpaner M, Eisenhaber F, J Mol Biol 2004 337 243 253 10.1016/j.jmb.2004.01.025 15003443 (Pubitemid 38293395)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.2 , pp. 243-253
    • Eisenhaber, B.1    Schneider, G.2    Wildpaner, M.3    Eisenhaber, F.4
  • 20
    • 0031778695 scopus 로고    scopus 로고
    • Sed1p is a major cell wall protein of Saccharomyces cerevisiae in the stationary phase and is involved in lytic enzyme resistance
    • Sed1p is a major cell wall protein of Saccharomyces cerevisiae in the stationary phase and is involved in lytic enzyme resistance. Shimoi H, Kitagaki H, Ohmori H, Iimura Y, Ito K, J Bacteriol 1998 180 3381 3387 9642191 (Pubitemid 28307212)
    • (1998) Journal of Bacteriology , vol.180 , Issue.13 , pp. 3381-3387
    • Shimoi, H.1    Kitagaki, H.2    Ohmori, H.3    Iimura, Y.4    Ito, K.5
  • 21
    • 0347927334 scopus 로고    scopus 로고
    • An eight-cysteine-containing CFEM domain unique to a group of fungal membrane proteins
    • DOI 10.1016/S0968-0004(03)00025-2
    • An eight-cysteine-containing CFEM domain unique to a group of fungal membrane proteins. Kulkarni RD, Kelkar HS, Dean RA, Trends Biochem Sci 2003 28 118 121 10.1016/S0968-0004(03)00025-2 12633989 (Pubitemid 36293846)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.3 , pp. 118-121
    • Kulkarni, R.D.1    Kelkar, H.S.2    Dean, R.A.3
  • 22
    • 0034109113 scopus 로고    scopus 로고
    • Morphogenesis, adhesive properties, and antifungal resistance depend on the Pmt6 protein mannosyltransferase in the fungal pathogen Candida albicans
    • DOI 10.1128/JB.182.11.3063-3071.2000
    • Morphogenesis, adhesive properties, and antifungal resistance depend on the Pmt6 protein mannosyltransferase in the fungal pathogen candida albicans. Timpel C, Zink S, Strahl-Bolsinger S, Schroppel K, Ernst J, J Bacteriol 2000 182 3063 3071 10.1128/JB.182.11.3063-3071.2000 10809683 (Pubitemid 30326919)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3063-3071
    • Timpel, C.1    Zink, S.2    Strahl-Bolsinger, S.3    Schroppel, K.4    Ernst, J.5
  • 24
    • 0033046659 scopus 로고    scopus 로고
    • Composition and enzymatic activity of the extracellular matrix secreted by germlings of Botrytis cinerea
    • Composition and enzymatic activity of the extracellular matrix secreted by germlings of Botrytis cinerea. Doss RP, Appl Environ Microbiol 1999 65 404 408 9925560 (Pubitemid 29075075)
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.2 , pp. 404-408
    • Doss, R.P.1
  • 25
    • 0035872908 scopus 로고    scopus 로고
    • The possible function of the glucan sheath of Botrytis cinerea: Effects on the distribution of enzyme activities
    • DOI 10.1016/S0378-1097(01)00165-3, PII S0378109701001653
    • The possible function of the glucan sheath of Botrytis cinerea: effects on the distribution of enzyme activities. Gil-ad NL, Bar-Nun N, Mayer AM, FEMS Microbiol Lett 2001 199 109 113 10.1111/j.1574-6968.2001.tb10659.x 11356576 (Pubitemid 32455472)
    • (2001) FEMS Microbiology Letters , vol.199 , Issue.1 , pp. 109-113
    • Gil-Ad, N.L.1    Bar-Nun, N.2    Mayer, A.M.3
  • 26
    • 0036430075 scopus 로고    scopus 로고
    • Modular domain structure in the Candida glabrata adhesin Epa1p, a β1,6 glucan-cross-linked cell wall protein
    • DOI 10.1046/j.1365-2958.2002.03166.x
    • Modular domain structure in the Candida glabrata adhesin Epa1p, a beta1,6 glucan-cross-linked cell wall protein. Frieman MB, McCaffery JM, Cormack BP, Mol Microbiol 2002 46 479 492 10.1046/j.1365-2958.2002.03166.x 12406223 (Pubitemid 35340958)
    • (2002) Molecular Microbiology , vol.46 , Issue.2 , pp. 479-492
    • Frieman, M.B.1    McCaffery, J.M.2    Cormack, B.P.3
  • 31
    • 84874249063 scopus 로고    scopus 로고
    • Fasta2tab http://darwin.biochem.okstate.edu/fasta2tab
    • Fasta2tab
  • 32
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Improved prediction of signal peptides: Signal 3.0. Bendtsen JD, Nielsen H, von Heijne G, Brunak S, J Mol Biol 2004 340 783 795 10.1016/j.jmb.2004.05.028 15223320 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.