Ario de Marco

Summary

Affiliation: European Institute of Oncology
Country: Italy

Publications

  1. ncbi The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformation
    Tina Schultz
    EMBL Scientific Core Facilities, Meyerhofstr 1, D 69117 Heidelberg, Germany
    Biochem Biophys Res Commun 355:234-9. 2007
  2. doi Molecular and chemical chaperones for improving the yields of soluble recombinant proteins
    Ario de Marco
    Biochemistry Unit, IFOM IEO Campus for Oncogenomics, Cogentech, Milano, Italy
    Methods Mol Biol 705:31-51. 2011
  3. pmc The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins
    Marisa Aliprandi
    Protein Chemistry Unit, Cogentech, IFOM IEO Campus for Oncogenomics, Via Adamello 16, 20139 Milan, Italy
    J Biomed Biotechnol 2010:658954. 2010
  4. doi User-friendly expression plasmids enable the fusion of VHHs to application-specific tags
    Ario de Marco
    University of Nova Gorica UNG, Rozna dolina, Nova Gorica, Slovenia
    Methods Mol Biol 911:507-22. 2012
  5. pmc Minimal information: an urgent need to assess the functional reliability of recombinant proteins used in biological experiments
    Ario de Marco
    Cogentech, Via Adamello 16, 20139, Milano, Italy
    Microb Cell Fact 7:20. 2008
  6. pmc Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli
    Ario de Marco
    Cogentech, IFOM IEO Campus for Oncogenomic, Via Adamello, 16 20139, Milano, Italy
    Microb Cell Fact 8:26. 2009
  7. doi Strategies for boosting the accumulation of correctly folded recombinant proteins expressed in Escherichia coli
    Ario de Marco
    University of Nova Gorica UNG, RoŽna Dolina Nova Gorica, Slovenia
    Methods Mol Biol 752:1-15. 2011
  8. ncbi Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
    Ario de Marco
    Scientific Core Facilities, EMBL, Meyerhofstrasse 1, D 69117 Heidelberg, Germany
    Nat Protoc 2:2632-9. 2007
  9. pmc Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli
    Ario de Marco
    EMBL Heidelberg, Heidelberg, Germany
    BMC Biotechnol 7:32. 2007
  10. ncbi Two-step metal affinity purification of double-tagged (NusA-His6) fusion proteins
    Ario de Marco
    IFOM IEO Campus for Oncogenomics, Via Adamello 16, I 20139, Milano, Italy
    Nat Protoc 1:1538-43. 2006

Collaborators

Detail Information

Publications37

  1. ncbi The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformation
    Tina Schultz
    EMBL Scientific Core Facilities, Meyerhofstr 1, D 69117 Heidelberg, Germany
    Biochem Biophys Res Commun 355:234-9. 2007
    ..Di-myo-inositol1,1'-phosphate (DIP) seems to be a good candidate to test in in vivo applications, although the opportunity of using otsA/B overexpressing cells is simpler and less expensive...
  2. doi Molecular and chemical chaperones for improving the yields of soluble recombinant proteins
    Ario de Marco
    Biochemistry Unit, IFOM IEO Campus for Oncogenomics, Cogentech, Milano, Italy
    Methods Mol Biol 705:31-51. 2011
    ..The selection of aggregates with different degrees of complexity can be exploited to maximize the yields of native proteins at the end of the refolding process...
  3. pmc The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins
    Marisa Aliprandi
    Protein Chemistry Unit, Cogentech, IFOM IEO Campus for Oncogenomics, Via Adamello 16, 20139 Milan, Italy
    J Biomed Biotechnol 2010:658954. 2010
    ..Our successful localization of Twist2 protein using the SNAP-tag-based approach and the anti-Twist2-specific recombinant single-domain antibodies opens new research possibilities in this field...
  4. doi User-friendly expression plasmids enable the fusion of VHHs to application-specific tags
    Ario de Marco
    University of Nova Gorica UNG, Rozna dolina, Nova Gorica, Slovenia
    Methods Mol Biol 911:507-22. 2012
    ..Within this chapter, practical tips for the choice and expression of the most appropriate among the available plasmids are listed, keeping in mind the experimental conditions in which usually the fusion antibodies will be applied...
  5. pmc Minimal information: an urgent need to assess the functional reliability of recombinant proteins used in biological experiments
    Ario de Marco
    Cogentech, Via Adamello 16, 20139, Milano, Italy
    Microb Cell Fact 7:20. 2008
    ..This article has been envisaged as a proposal for aggregating scientists who share the opinion that the scientific community needs a platform for Minimum Information for Protein Functionality Evaluation (MIPFE)...
  6. pmc Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli
    Ario de Marco
    Cogentech, IFOM IEO Campus for Oncogenomic, Via Adamello, 16 20139, Milano, Italy
    Microb Cell Fact 8:26. 2009
    ..This article reviews the available strategies for exploiting the physiological mechanisms of bactera to produce properly folded disulfide-bonded proteins...
  7. doi Strategies for boosting the accumulation of correctly folded recombinant proteins expressed in Escherichia coli
    Ario de Marco
    University of Nova Gorica UNG, RoŽna Dolina Nova Gorica, Slovenia
    Methods Mol Biol 752:1-15. 2011
    ....
  8. ncbi Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
    Ario de Marco
    Scientific Core Facilities, EMBL, Meyerhofstrasse 1, D 69117 Heidelberg, Germany
    Nat Protoc 2:2632-9. 2007
    ..Applying such a strategy, we could increase the solubility of 70% of the tested constructs with yields of up to 42-fold more protein than in controls. The procedure takes 2 d...
  9. pmc Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli
    Ario de Marco
    EMBL Heidelberg, Heidelberg, Germany
    BMC Biotechnol 7:32. 2007
    ..We now assessed the effects of combined overproduction of the functionally cooperating chaperone network of the E. coli cytosol on the solubility of recombinant proteins...
  10. ncbi Two-step metal affinity purification of double-tagged (NusA-His6) fusion proteins
    Ario de Marco
    IFOM IEO Campus for Oncogenomics, Via Adamello 16, I 20139, Milano, Italy
    Nat Protoc 1:1538-43. 2006
    ..The purity of the target protein usually makes a further purification step unnecessary for most of the lab applications. It takes less than 5 hours to purify the protein from a 5 g pellet...
  11. doi Optimization of purification protocols based on the step-by-step monitoring of the protein aggregates in soluble fractions
    Ario de Marco
    University of Nova Gorica, Nova Gorica, Slovenia
    Methods Mol Biol 824:145-54. 2012
    ..The analysis is performed by means of simple lab equipment and starting from small sample volumes...
  12. doi Single-domain antibodies that compete with the natural ligand fibroblast growth factor block the internalization of the fibroblast growth factor receptor 1
    Gianluca Veggiani
    IFOM IEO Campus, Via Adamello 16, Milan, Italy
    Biochem Biophys Res Commun 408:692-6. 2011
    ..This achievement indicates that these antibodies have a capacity to modulate the receptor physiology and, therefore, constitute powerful reagents for basic research and a potential lead for therapeutic applications...
  13. ncbi The solubility and stability of recombinant proteins are increased by their fusion to NusA
    Valeria De Marco
    EMBL Heidelberg, Meyerhofstrasse 1, D 69117 Heidelberg, Germany
    Biochem Biophys Res Commun 322:766-71. 2004
    ..Structural analysis indicated that the purified proteins were monodispersed and correctly folded. NusA has been used to raise antibodies that have been successfully used for Western blot and immunoprecipitation of NusA fusion proteins...
  14. doi Immunological applications of single-domain llama recombinant antibodies isolated from a naïve library
    Ana Monegal
    Consortium for Genomic Technologies, Biochemistry Unit, IFOM IEO Campus, Via Adamello 16, 20139 Milano, Italy
    Protein Eng Des Sel 22:273-80. 2009
    ....
  15. ncbi Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning
    Ario de Marco
    EMBL Heidelberg, Meyerhofstrasse 1, 69117 Heidelberg, Germany
    J Biotechnol 109:45-52. 2004
    ....
  16. doi Antibody-mediated purification of co-expressed antigen-antibody complexes
    Sergio Bossi
    Protein Chemistry Unit, Cogentech IFOM IEO Campus for Oncogenomics, Via Adamello 16, 20139 Milano, Italy
    Protein Expr Purif 72:55-8. 2010
    ..The described method may offer a suitable alternative for the purification of proteins intended for crystallization trials and it may also be used as a general purification protocol for both antigens and recombinant antibodies...
  17. pmc Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    Ario de Marco
    Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Cell Stress Chaperones 10:329-39. 2005
    ....
  18. doi Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidase
    Gianluca Veggiani
    Protein Chemistry Unit, Cogentech, Milano, Italy
    Protein Expr Purif 79:111-4. 2011
    ..Therefore, the described method represents a valid solution to produce inexpensively large amounts of single domain antibodies for in vitro applications and we expect it will be suitable for the production of other antibody fragments...
  19. ncbi Fusion tags and chaperone co-expression modulate both the solubility and the inclusion body features of the recombinant CLIPB14 serine protease
    Andrea Schrödel
    EMBL, Meyerhofstr 1, D 69117 Heidelberg, Germany
    J Biotechnol 120:2-10. 2005
    ..In conclusion, it is possible to tune the quality of the inclusion bodies by choosing the suitable combination of tag and chaperone co-expression that minimize the non-productive side reactions during refolding...
  20. ncbi Induced fit of passenger proteins fused to Archaea maltose binding proteins
    He Huang
    Protein Expression Core Facility, EMBL, Meyerhofstr 1, D 69117 Heidelberg, Germany
    Biochem Biophys Res Commun 344:25-9. 2006
    ....
  21. ncbi Automated protein analysis by online detection of laser-induced fluorescence in slab gels and 3-D geometry gels
    Robert Ventzki
    Scientific Core Facilities, Services and Technology Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Electrophoresis 27:3338-48. 2006
    ..In combination with the expected large capacity of 384 or 1,536 samples, this makes the instrument a valuable tool for high-throughput comparative screening applications...
  22. ncbi Comparative analysis of protein aggregates by blue native electrophoresis and subsequent sodium dodecyl sulfate-polyacrylamide gel electrophoresis in a three-dimensional geometry gel
    Josef Stegemann
    Scientific Core Facilities, Services and Technology Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Proteomics 5:2002-9. 2005
    ..It should be feasible to quickly gain a diagnostic picture during amyloid-related neurodegenerative disease development or to observe drug effects on protein aggregation...
  23. pmc Monodispersity of recombinant Cre recombinase correlates with its effectiveness in vivo
    Paola Capasso
    Cogentech Consortium for Genomics Technologies, Via Adamello 16, 20139 Milan, Italy
    BMC Biotechnol 9:80. 2009
    ..However, the recovery of active TAT-Cre remains a demanding process and its specific activity varies significantly among batches, making difficult data comparison...
  24. doi Methodologies for the isolation of alternative binders with improved clinical potentiality over conventional antibodies
    Ario de Marco
    University of Nova Gorica UNG, RoŽna Dolina Nova Gorica, Slovenia
    Crit Rev Biotechnol 33:40-8. 2013
    ..The term binder will be preferred when possible to include those molecules, such as peptides or affibodies, with at least some proven practical uses...
  25. doi Single domain antibodies with VH hallmarks are positively selected during panning of llama (Lama glama) naïve libraries
    Ana Monegal
    Cogentech Protein Chemistry Unit, IFOM IEO Campus, Via Adamello 16, 20139 Milano, Italy
    Dev Comp Immunol 36:150-6. 2012
    ..These data suggest that the thermodynamically favored VHHs can be lost during biopanning, as previously observed for DARPins and in contrast to the recombinant antibodies in scFv format...
  26. pmc Heating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domains
    Aurelien Olichon
    Cell Biology Unit, EMBL Meyerhofstr 1, D 69117, Heidelberg, Germany
    BMC Biotechnol 7:7. 2007
    ..Their heat tolerance is a particularly interesting feature because it has been recently related to both high yields during recombinant expression and selective purification of folded protein...
  27. pmc Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization
    Fabrizio Villa
    Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy
    Proc Natl Acad Sci U S A 106:20204-9. 2009
    ..Overall, the structure of the Haspin kinase domain reveals an active conformation that is poised for substrate recognition and phosphorylation in the absence of external regulators...
  28. pmc The binding of NCAM to FGFR1 induces a specific cellular response mediated by receptor trafficking
    Chiara Francavilla
    IFOM FIRC Institute of Molecular Oncology, IFOM IEO Campus, Milano, Italy
    J Cell Biol 187:1101-16. 2009
    ....
  29. ncbi Recombinant proteins fused to thermostable partners can be purified by heat incubation
    Ario de Marco
    European Molecular Biology Laboratory, Heidelberg, Germany
    J Biotechnol 107:125-33. 2004
    ..We proved that it can be easily automated...
  30. doi Conflict of interests: multiple signal peptides with diverging goals
    Annunziata Venuto
    University of Nova Gorica UNG, PO Box 301, Rožna Dolina Nova Gorica 5000, Slovenia
    J Cell Biochem 114:510-3. 2013
    ..However, misleading or cumbersome results may be generated when expressing recombinant proteins with modified signal peptides or single domains of larger proteins...
  31. doi Screening optimized protein purification protocols by coupling small-scale expression and mini-size exclusion chromatography
    Elisa Sala
    Cogentech, IFOM IEO Campus for Oncogenomics, Milano, Italy
    Protein Expr Purif 74:231-5. 2010
    ..SEC is also useful to identify low molecular mass contaminants that can be underestimated as they migrate together with the front of the acrylamide gel...
  32. pmc Biotechnological applications of recombinant single-domain antibody fragments
    Ario de Marco
    University of Nova Gorica UNG, Vipavska 13, PO Box 301 SI 5000, RoŽna Dolina Nova Gorica, Slovenia
    Microb Cell Fact 10:44. 2011
    ....
  33. pmc Dimerization properties of a Xenopus laevis kinesin-II carboxy-terminal stalk fragment
    Valeria De Marco
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
    EMBO Rep 4:717-22. 2003
    ....
  34. pmc Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates
    Cerstin Franz
    European Molecular Biology Laboratory, Heidelberg, Germany
    EMBO J 24:3519-31. 2005
    ..Time-course experiments indicated that Nup155 is recruited to chromatin at the time of NE sealing, suggesting that nuclear pore complex assembly has to progress to a relatively late stage before NE membrane assembly occurs...
  35. pmc Characterization of the aggregates formed during recombinant protein expression in bacteria
    Andrea Schrödel
    EMBL, Protein Expression Core Facility, Meyerhofstr, 1, D 69117, Heidelberg Germany
    BMC Biochem 6:10. 2005
    ..coli. A sucrose step gradient succeeded in separating aggregate subclasses of a GFP-GST fusion protein with specific biochemical and biophysical features, providing a novel approach for studying recombinant protein aggregates...
  36. doi Physical and chemical perturbations induce the formation of protein aggregates with different structural features
    Antonino Natalello
    Dipartimento di Biotecnologie e Bioscienze, Universita degli Studi Milano Bicocca, Piazza della Scienza 2, 20126 Milano, Italy
    Protein Expr Purif 58:356-61. 2008
    ..In conclusion, great caution should be taken in inferring conclusions on protein aggregation and disaggregation in vivo from results obtained using aggregates produced under non-physiological perturbations...
  37. ncbi Correct identification of the chloroplastic protoporphyrinogen IX oxidase N-terminus places the biochemical data in frame
    Ario de Marco
    Biochemistry, Syngenta Crop Protection AG, P O Box, Basel, CH 4002, Switzerland
    Biochem Biophys Res Commun 309:873-8. 2003
    ....