Marina Lotti

Summary

Affiliation: University of Milano-Bicocca
Country: Italy

Publications

  1. pmc Why and how protein aggregation has to be studied in vivo
    Diletta Ami
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Piazza della Scienza 2, 20126, Milano, Italy
    Microb Cell Fact 12:17. 2013
  2. doi request reprint Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins
    Marina Lotti
    Dipartimento di Biotecnologie e Bioscienze, Università Statale Milano Bicocca, Milan, Italy
    Mol Biosyst 8:105-13. 2012
  3. doi request reprint Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation
    Pietro Gatti-Lafranconi
    Department of Biotechnology and Biosciences, State University of Milano Bicocca, Piazza della Scienza 2, I 20126 Milano, Italy
    J Mol Biol 395:155-66. 2010
  4. doi request reprint How disorder influences order and vice versa--mutual effects in fusion proteins containing an intrinsically disordered and a globular protein
    Ilaria Sambi
    Dipartimento di Biotecnologie e Bioscienze, Universita di Milano Bicocca, Milano, Italy
    FEBS J 277:4438-51. 2010
  5. pmc Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain
    Stefania Brocca
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Milan, Italy
    Biophys J 100:2243-52. 2011
  6. doi request reprint In vivo aggregation of bovine beta-lactoglobulin is affected by Cys at position 121
    Gaetano Invernizzi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milano, Italy
    Protein Expr Purif 62:111-5. 2008
  7. doi request reprint Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies
    Silvia Maria Doglia
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milano, Italia
    Biotechnol J 3:193-201. 2008
  8. pmc Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila
    Federica Parravicini
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Milan, Italy
    PLoS ONE 8:e56254. 2013
  9. doi request reprint Defining structural domains of an intrinsically disordered protein: Sic1, the cyclin-dependent kinase inhibitor of Saccharomyces cerevisiae
    Stefania Brocca
    Department of Biotechnology and Biosciences, Universita di Milano Bicocca, P zza della Scienza 2, 20126, Milan, Italy
    Mol Biotechnol 47:34-42. 2011
  10. ncbi request reprint Comparison of bovine and porcine beta-lactoglobulin: a mass spectrometric analysis
    Gaetano Invernizzi
    Department of Biotechnology and Biosciences, University Milano Bicocca, Piazza della Scienza 2, 20126 Milan, Italy
    J Mass Spectrom 41:717-27. 2006

Collaborators

Detail Information

Publications25

  1. pmc Why and how protein aggregation has to be studied in vivo
    Diletta Ami
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Piazza della Scienza 2, 20126, Milano, Italy
    Microb Cell Fact 12:17. 2013
    ..Here, we discuss the use of several biochemical and biophysical approaches that can be employed to monitor protein aggregation within intact cells, focusing in particular on bacteria that are widely employed as microbial cell factories...
  2. doi request reprint Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins
    Marina Lotti
    Dipartimento di Biotecnologie e Bioscienze, Università Statale Milano Bicocca, Milan, Italy
    Mol Biosyst 8:105-13. 2012
    ..The impact of the artificial fusion on the conformational and functional properties of the resulting proteins is discussed...
  3. doi request reprint Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation
    Pietro Gatti-Lafranconi
    Department of Biotechnology and Biosciences, State University of Milano Bicocca, Piazza della Scienza 2, I 20126 Milano, Italy
    J Mol Biol 395:155-66. 2010
    ..This reduction of lid movements is suggested to be accompanied by a concomitant increase in the mobility of other protein regions, thus accounting for the observed broadening of substrate specificity...
  4. doi request reprint How disorder influences order and vice versa--mutual effects in fusion proteins containing an intrinsically disordered and a globular protein
    Ilaria Sambi
    Dipartimento di Biotecnologie e Bioscienze, Universita di Milano Bicocca, Milano, Italy
    FEBS J 277:4438-51. 2010
    ....
  5. pmc Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain
    Stefania Brocca
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Milan, Italy
    Biophys J 100:2243-52. 2011
    ..Comparison between the fragment and the full-length protein suggests that chain length is crucial to the stabilization of compact states of this IDP. The two proteins are compared by a length-independent compaction index...
  6. doi request reprint In vivo aggregation of bovine beta-lactoglobulin is affected by Cys at position 121
    Gaetano Invernizzi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milano, Italy
    Protein Expr Purif 62:111-5. 2008
    ..Our results underline the key contribution of the unpaired cysteine residue during the oxidative folding pathway and indicate BLG as a useful tool for the study of protein aggregation in vivo...
  7. doi request reprint Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies
    Silvia Maria Doglia
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milano, Italia
    Biotechnol J 3:193-201. 2008
    ..Examples are reported concerning the study of kinetics of aggregation and structure of aggregates as a function of expression levels, temperature and co-expression of chaperones...
  8. pmc Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila
    Federica Parravicini
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Milan, Italy
    PLoS ONE 8:e56254. 2013
    ..Overall, a strict interaction of the SpAAP domains seems to be mandatory for the preservation of their reciprocal structural integrity and may witness their co-evolution...
  9. doi request reprint Defining structural domains of an intrinsically disordered protein: Sic1, the cyclin-dependent kinase inhibitor of Saccharomyces cerevisiae
    Stefania Brocca
    Department of Biotechnology and Biosciences, Universita di Milano Bicocca, P zza della Scienza 2, 20126, Milan, Italy
    Mol Biotechnol 47:34-42. 2011
    ..Circular dichroism (CD) measurements and nuclear magnetic resonance (NMR) spectra of N- and C-terminal fragments confirm their disordered nature but reveal minor structural differences that may reflect their distinct functional roles...
  10. ncbi request reprint Comparison of bovine and porcine beta-lactoglobulin: a mass spectrometric analysis
    Gaetano Invernizzi
    Department of Biotechnology and Biosciences, University Milano Bicocca, Piazza della Scienza 2, 20126 Milan, Italy
    J Mass Spectrom 41:717-27. 2006
    ..Equilibrium folding intermediates of both proteins are detected. Finally, conditions are found that promote dissociation of the BLG dimer at pH 6 into folded monomers...
  11. ncbi request reprint Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    Diletta Ami
    Dipartimento di Biotecnologie e Bioscienze, Universita di Milano Bicocca, Piazza della Scienza 2, 20126 Milan, Italy
    FEBS Lett 579:3433-6. 2005
    ..Furthermore, insights on the residual native-like structure of the expressed protein within IB--both isolated and inside cells--were obtained by the secondary structure analysis of the Amide I band in the IB FT-IR spectra...
  12. pmc Laboratory evolution of copper tolerant yeast strains
    Giusy Manuela Adamo
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Piazza della Scienza 2, 20126 Milano, Italy
    Microb Cell Fact 11:1. 2012
    ..Moreover, they can contribute to the study of human diseases related to impairments of copper metabolism. In this study, we investigated the molecular and physiological factors that confer copper tolerance to strains of baker's yeasts...
  13. doi request reprint Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase
    Pietro Gatti-Lafranconi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Piazza della Scienza 2, Milan, Italy
    FEBS Lett 582:2313-8. 2008
    ..Biophysical measurements did not indicate any obvious difference between the improved variant and the wild type enzyme in terms of loss of secondary structure upon heat treatment, nor a shift in the apparent melting temperature...
  14. doi request reprint Relevance of metal ions for lipase stability: structural rearrangements induced in the Burkholderia glumae lipase by calcium depletion
    Gaetano Invernizzi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milano, Italy
    J Struct Biol 168:562-70. 2009
    ....
  15. doi request reprint Deactivation and unfolding are uncoupled in a bacterial lipase exposed to heat, low pH and organic solvents
    Gaetano Invernizzi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milano, Italy
    J Biotechnol 141:42-6. 2009
    ..In particular, no denaturation at all could be elicited by dimethyl formamide (DMF), isopropanol, and dimethyl sulfoxide (DMSO) up to 80%, in spite of a reduction of enzyme activity to 60-75%...
  16. doi request reprint Electrospray-ionization mass spectrometry as a tool for fast screening of protein structural properties
    Rita Grandori
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Milan, Italy
    Biotechnol J 4:73-87. 2009
    ....
  17. doi request reprint Promiscuity, stability and cold adaptation of a newly isolated acylaminoacyl peptidase
    Electra A S Brunialti
    Dipartimento di Biotecnologie e Bioscienze, Universita di Milano Bicocca, 20126 Milano, Italy
    Biochimie 93:1543-54. 2011
    ..2 × 10(3) s(-1) M(-1), respectively. Despite some properties cannot be explained with current models, results report on the relevance of structural and catalytic properties for the successful adaptation to cold temperatures...
  18. pmc Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    Antonino Natalello
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Piazza della Scienza 2, 20126 Milano, Italy
    Biochem J 385:511-7. 2005
    ..Glycosidic structures of the high mannose type were found, with mannoses ranging from 8 to 25 residues...
  19. doi request reprint Plasma-induced graft-polymerization of polyethylene glycol acrylate on polypropylene films: chemical characterization and evaluation of the protein adsorption
    Stefano Zanini
    Dipartimento di Fisica G Occhialini, Universita degli Studi di Milano Bicocca, p za della Scienza, 3 I 20126 Milano, Italy
    J Colloid Interface Sci 341:53-8. 2010
    ....
  20. pmc Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1
    Stefania Brocca
    Department of Biotechnology and Biosciences, University of Milano Bicocca, Milan, Italy
    Proteins 76:731-46. 2009
    ..The mutations S201A and S201E, which are known to affect Sic1 function, do not have significant effects on the conformational properties of the pure protein...
  21. ncbi request reprint Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase
    Gianluca Santarossa
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Italy
    FEBS Lett 579:2383-6. 2005
    ..Moreover, mutations conferred to PFL higher temperature stability. On the other hand, replacement of the serine at position 141 by glycine destabilized the protein...
  22. ncbi request reprint Heterologous expression of bovine and porcine beta-lactoglobulins in Pichia pastoris: towards a comparative functional characterisation
    Gaetano Invernizzi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Piazza della Scienza 2, Milan, Italy
    J Biotechnol 109:169-78. 2004
    ..Recombinant lipocalins were purified by ion-exchange chromatography from the culture medium. A preliminary NMR characterisation showed that both proteins were correctly folded...
  23. pmc Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes
    Stefania Brocca
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, 20126 Milano, Italy
    Protein Sci 12:2312-9. 2003
    ..On the other hand, a specific shift in the chain-length specificity was not observed. Chimeric proteins displayed different sensitivity to detergents in the reaction medium...
  24. ncbi request reprint Monitoring the transport of recombinant Candida rugosa lipase by a green fluorescent protein-lipase fusion
    Simone Passolunghi
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Piazza della Scienza 2, 20126 Milano, Italy
    Biotechnol Lett 25:1945-8. 2003
    ..This analytical tool enables a rapid monitoring of product localization and amount, based on GFP-associated fluorescence...
  25. pmc Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm
    Riccardo Villa
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi di Milano Bicocca, Piazza della Scienza 2, Milano, Italy
    Microb Cell Fact 8:32. 2009
    ..abstract:..