Amyloid-like properties of Saccharomyces cerevisiae cell wall glucantransferase Bgl2p

References

• Lesage G, Bussey H. Cell wall assembly in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 2006; 70:317 - 343
   PubMed Web of Science ®Google Scholar
• Kapteyn JC, Van Den Ende H, Klis FM. The contribution of cell wall proteins to the organization of the yeast cell wall. Biochim Biophys Acta 1999; 1426:373 - 383
   PubMed Web of Science ®Google Scholar
• Mrša V, Tanner W. Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall. Yeast 1999; 15:813 - 820
   PubMed Web of Science ®Google Scholar
• Klebl F, Tanner W. Molecular cloning of a cell wall exo-beta-1,3-glucanase from Saccharomyces cerevisiae. J Bacteriol 1989; 171:6259 - 6264
   PubMed Web of Science ®Google Scholar
• Popolo L, Vai M. The Gas1 glycoprotein, a putative wall polymer cross-linker. Biochim Biophys Acta 1999; 1426:385 - 400
   PubMed Web of Science ®Google Scholar
• Wösten HA, de Vocht ML. Hydrophobins, the fungal coat unravelled. Biochim Biophys Acta 2000; 1469:79 - 86
   PubMed Web of Science ®Google Scholar
• Gebbink MF, Claessen D, Bouma B, Dijkhuizen L, Wösten HA. Amyloids— a functional coat for microorganisms. Nature Rev Microbiol 2005; 3:333 - 341
   PubMed Web of Science ®Google Scholar
• Wösten HA. Hydrophobins: multipurpose proteins. Annu Rev Microbiol 2001; 55:625 - 646
   PubMed Web of Science ®Google Scholar
• Ter-Avanesyan M, Derkatch I, Baskakov I, Kushnirov V. Unraveling prion structures and biological functions. Genome Biol 2005; 6:366
   PubMed Web of Science ®Google Scholar
• Sarthy AV, McGonigal T, Coen M, Frost DJ, Meulbroek JA, Goldman RC. Phenotype in Candida albicans of a disruption of the BGL2 gene encoding a 1,3-beta-glucosyltransferase. Microbiology 1997; 143:367 - 376
   PubMed Web of Science ®Google Scholar
• Pitarch A, Jiménez A, Nombela C, Gil C. Decoding serological response to Candida cell wall immunome into novel diagnostic, prognostic, and therapeutic candidates for systemic candidiasis by proteomic and bioinformatic analyses. Mol Cell Proteomics 2006; 5:79 - 96
   PubMed Web of Science ®Google Scholar
• Nilsson MR. Techniques to study amyloid fibril formation in vitro. Methods 2004; 34:151 - 160
   PubMed Web of Science ®Google Scholar
• Chapman MR, Robinson LS, Pinkner JS, Roth R, Heuser J, Hammar M, Normark S, Hultgren SJ. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 2002; 295:851 - 855
   PubMed Web of Science ®Google Scholar
• Claessen D, Rink R, de Jong W, Siebring J, de Vreugd P, Boersma FG, Dijkhuizen L, Wosten HA. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev 2003; 17:1714 - 1726
   PubMed Web of Science ®Google Scholar
• Kalebina TS, Laurinavichiute DK, Packeiser AN, Morenkov OS, Ter-Avanesyan MD, Kulaev IS. Correct GPI-anchor synthesis is required for the incorporation of endoglucanase/glucanosyltransferase Bgl2p into the Saccharomyces cerevisiae cell wall. FEMS Microbiol Lett 2002; 210:81 - 85
   PubMed Web of Science ®Google Scholar
• Wösten HA, van Wetter MA, Lugones LG, van der Mei HC, Busscher HJ, Wessels JG. How a fungus escapes the water to grow into the air. Curr Biol 1999; 9:85 - 88
   PubMed Web of Science ®Google Scholar
• Mrša V, Klebl F, Tanner W. Purification and characterization of the Saccharomyces cerevisiae BGL2 gene product, a cell wall endo-beta-1,3-glucanase. J Bacteriol 1993; 175:2102 - 2106
   PubMed Web of Science ®Google Scholar
• Kalebina TS, Farkaš V, Laurinavichiute DK, Gorlovoy PM, Fominov GV, Bartek P, Kulaev IS. Deletion of BGL2 results in an increased chitin level in the cell wall of Saccharomyces cerevisiae. Antonie Leeuwenhoek 2003; 84:179 - 184
   PubMed Web of Science ®Google Scholar
• Cappellaro C, Mrša V, Tanner W. New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating. J Bacteriol 1998; 180:5030 - 5037
   PubMed Web of Science ®Google Scholar
• Chaffin WL, Lopez-Ribot JL, Casanova M, Gozalbo D, Martinez JP. Cell wall and secreted proteins of Candida albicans: identification, function and expression. Microbiol Mol Biol Rev 1998; 62:130 - 180
   PubMed Web of Science ®Google Scholar
• Mouyna I, Hartland RP, Fontaine T, Diaquin M, Simenel C, Delepierre M, Henrissat B, Latgé JP. A 1,3-beta-glucanosyltransferase isolated from the cell wall of Aspergillus fumigatus is a homologue of the yeast Bgl2p. Microbiology 1998; 144:3171 - 3180
   PubMed Web of Science ®Google Scholar
• Galzitskaya OV, Garbuzynskiy SO, Lobanov MY. A search for amyloidogenic regions in protein chains. Mol Biol (Moscow) 2006; 40:821 - 828
   Web of Science ®Google Scholar
• Galzitskaya OV, Garbuzynskiy SO, Lobanov MY. Is it possible to predict amyloidogenic regions from sequence alone?. Journal of Bioinformatics and Computational Biology 2006; 4:373 - 388
   PubMedGoogle Scholar
• Galzitskaya OV, Garbuzynskiy SO, Lobanov MY. Prediction of amyloidogenic and disordered regions in protein chains. PLoS Computational Biology 2006; 2:177
   PubMed Web of Science ®Google Scholar
• Saunders WS, Hoyt MA. Kinesin-related proteins required for structural integrity of the mitotic spindle. Cell 1992; 70:451 - 458
   PubMed Web of Science ®Google Scholar
• Scopes RK. Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 1974; 59:277 - 282
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680 - 685
   PubMed Web of Science ®Google Scholar
• Morenkov OS, Mantsyghin Yu A, Sergeev VA, Sobko Yu A, Morenkova MA, Panchenko OA. The isolation and characteristics of monoclonal antibodies to the glycoprotein GII of Aujeszky's disease virus and their use for the epitopic mapping of GII. Vopr Virusol (Russ) 1994; 4:174 - 177
   Google Scholar
• LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease {beta}-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 1993; 2:404 - 410
   PubMed Web of Science ®Google Scholar
• Lobley A, Whitmore L, Wallace BA. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002; 18:211 - 212
   PubMed Web of Science ®Google Scholar
• Whitmore L, Wallace BA. DICHROWEB, an online server for protein secondary structure analysis from circular dichroism spectroscopic data. Nucleic Acids Research 2004; 32:668 - 673
   PubMed Web of Science ®Google Scholar
• Balbirnie M, Grothe R, Eisenberg DS. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Proc Natl Acad Sci USA 2001; 98:2375 - 2380
   PubMed Web of Science ®Google Scholar
• Blanchard BJ, Chen A, Rozeboom LM, Stafford KA, Weigele P, Ingram VM. Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule. Proc Natl Acad Sci U S A 2004; 101:14326 - 14332
   PubMed Web of Science ®Google Scholar
• Hirota-Nakaoka N, Hasegawa K, Naiki H, Goto Y. Dissolution of beta2-microglobulin amyloid fibrils by dimethylsulfoxide. J Biochem 2003; 134:159 - 164
   PubMed Web of Science ®Google Scholar
• Manavalan P, Johnson WC Jr. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal Biochem 1987; 167:76 - 85
   PubMed Web of Science ®Google Scholar
• Sreerama N, Woody RW. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 1993; 209:32 - 44
   PubMed Web of Science ®Google Scholar
• Provencher SW, Glockner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 1981; 20:33 - 37
   PubMed Web of Science ®Google Scholar