POPOLO, LAURA MARIA
POPOLO, LAURA MARIA
Dipartimento di Bioscienze
A capture method based on the VC1 domain reveals new binding properties of the human receptor for advanced glycation end products (RAGE)
2017 G. Degani, A.A. Altomare, M. Colzani, C. Martino, A. Mazzolari, G. Fritz, G. Vistoli, L. Popolo, G. Aldini
A cystein rich domain related to the plant CBM43 is essential for the beta (1,3)glucanosyltransferase activity of the GAS family of protein in Saccharomyces cerevisiae
2007 E. Ragni, O. Palomares, E. Rolli, J. Calderon, L. Popolo
A cysteine-enriched motif related to the plant carbohydrate binding module 43 is essential for the functionality of family GH72+ glucanosyltransferases
2006 C. Carotti, E. Ragni, O. Palomares, C. Gissi, T. Fontaine, J.P. Latgé, L. Popolo
A cysteine-rich domain related to the plant CBM43 is essential for the beta(1,3)-glucanosyltransferase activity of Gas family of proteins of Saccharomyces cerevisiae
2007 E. Ragni, O. Palomares, E. Rolli, J. Calderon, L. Popolo
A genome-wide transcriptional analysis of the response to hyphal wall stress in Candida albicans
2015 G. Degani, E. Ragni, P. Botias, J.M. Rodriguez Pena, J. Arroyo, W. Fonzi, L. Popolo
A new high resolution mass spectrometry application for the comprehensive analysis of the ligand-binding properties of rage
2012 D. De Maddis, G. Degani, A. Pancotti, G. Vistoli, S. Romeo, M. Carini, L. Popolo, G. Aldini
Advanced lipoxidation end products (ALEs) as RAGE binders : Mass spectrometric and computational studies to explain the reasons why
2018 M. Mol, G. Degani, C. Coppa, G. Baron, L. Popolo, M. Carini, G. Aldini, G. Vistoli, A. Altomare
An improved expression system for the Vc1 ligand binding domain of the receptor for advanced glycation end products in Pichia pastoris
2015 G. Degani, M. Colzani, A. Tettamanzi, L. Sorrentino, A. Aliverti, G. Fritz, G. Aldini, L. Popolo
Apis mellifera RidA, a novel member of the canonical YigF/YER057c/UK114 imine deiminase superfamily of enzymes pre-empting metabolic damage
2022 C. Visentin, G. Rizzi, G. Degani, S. Digiovanni, G. Robecchi, A. Barbiroli, L. Popolo, M.A. Vanoni, S. Ricagno
CAMP PROMOTES THE SYNTHESIS IN EARLY G1 OF GP115, A YEAST GLYCOPROTEIN CONTAINING GLYCOSYL-PHOSPHATIDYLINOSITOL
1990 R. GRANDORI, L. POPOLO, M. VAI, L. ALBERGHINA
Candida albicans homologue of GGP1/GAS1 gene is functional in Saccharomyces cerevisiae and contains the determinants for glycosylphosphatidylinositol attachment
1996 M. Vai, I. Orlandi, P. Cavadini, L. Alberghina, L. Popolo
Catalytic properties of Phr family members of cell wall glucan remodeling enzymes : implications for the adaptation of Candida albicans to ambient pH
2015 K. Kováčová, G. Degani, E. Stratilová, V. Farkaš, L. Popolo
Catalytic properties of the Gas family β-(1,3)-glucanosyltransferases active in fungal cell-wall biogenesis as determined by a novel fluorescent assay
2011 M. Mazan, E. Ragni, L. Popolo, V. Farkas
Cell Biology, Protein Processing, and Cell Signaling
2013 R.J. Kaufman, L. Popolo
Cell wall glucan remodeling is required for Candida albicans adhesion and invasion
2010 J. Calderon, M. Zavrel, E. Ragni, W.A. Fonzi, S. Rupp, L. Popolo
CHANGES IN THE PROTEIN-SYNTHESIS PATTERN DURING A NUTRITIONAL SHIFT-DOWN TRANSITION IN SACCHAROMYCES-CEREVISIAE
1990 F. RODRIGUEZ, L. POPOLO, M. VAI, E. LACANA, L. ALBERGHINA
Characterization of recombinant forms of the yeast Gas1 protein and identification of residues essential for glucanosyltransferase activity and folding
2004 C. Carotti, E. Ragni, O. Palomares, T. Fontaine, G. Tedeschi, R. Rodriguez, J.P. Latgé, M. Vai, L.M. Popolo
Chitin synthesis in a gas1 mutant of saccharomyces cerevisiae
2000 M.H. Valdivieso, L. Ferrario, M. Vai, A. Duran, L. Popolo
Cloning and characterization of a cDNA encoding glyceraldehyde-3-phosphate dehydrogenase from the fission yeast Schizosaccharomyces pombe
1996 I. Orlandi, L. Popolo, P. Cavadini, M. Vai, S.E. Marre
Cloning, sequencing and regulation of a cDNA encoding a small heat-shock protein from Schizosaccharomyces pombe
1996 I. Orlandi, P. Cavadini, L. Popolo, M. Vai