Research Topics
Genomes and GenesSpecies | Ario de MarcoSummaryAffiliation: European Institute of Oncology Country: Italy Publications
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Detail Information
Publications
The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformationTina 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...- Molecular and chemical chaperones for improving the yields of soluble recombinant proteinsArio 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... - Optimization of purification protocols based on the step-by-step monitoring of the protein aggregates in soluble fractionsArio 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... - Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coliArio 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... - Minimal information: an urgent need to assess the functional reliability of recombinant proteins used in biological experimentsArio 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)... - Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coliArio 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... - Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coliArio 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... - Two-step metal affinity purification of double-tagged (NusA-His6) fusion proteinsArio 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... - Strategies for boosting the accumulation of correctly folded recombinant proteins expressed in Escherichia coliArio de Marco
University of Nova Gorica UNG, RoŽna Dolina Nova Gorica, Slovenia
Methods Mol Biol 752:1-15. 2011.... - Single-domain antibodies that compete with the natural ligand fibroblast growth factor block the internalization of the fibroblast growth factor receptor 1Gianluca 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... - The solubility and stability of recombinant proteins are increased by their fusion to NusAValeria 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... - The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteinsMarisa 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... - Antibody-mediated purification of co-expressed antigen-antibody complexesSergio 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... - Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidaseGianluca 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... - Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperonesArio de Marco
Protein Expression Unit, European Molecular Biology Laboratory, Heidelberg, Germany
Cell Stress Chaperones 10:329-39. 2005.... - Automated protein analysis by online detection of laser-induced fluorescence in slab gels and 3-D geometry gelsRobert 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... - Induced fit of passenger proteins fused to Archaea maltose binding proteinsHe Huang
Protein Expression Core Facility, EMBL, Meyerhofstr. 1, D-69117 Heidelberg, Germany
Biochem Biophys Res Commun 344:25-9. 2006.... - Comparative analysis of protein aggregates by blue native electrophoresis and subsequent sodium dodecyl sulfate-polyacrylamide gel electrophoresis in a three-dimensional geometry gelJosef 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... - Monodispersity of recombinant Cre recombinase correlates with its effectiveness in vivoPaola 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... - Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuningArio de Marco
EMBL Heidelberg, Meyerhofstrasse 1, 69117 Heidelberg, Germany
J Biotechnol 109:45-52. 2004.... - Immunological applications of single-domain llama recombinant antibodies isolated from a naïve libraryAna Monegal
Consortium for Genomic Technologies, Biochemistry Unit, IFOM IEO Campus, Via Adamello 16, 20139 Milano, Italy
Protein Eng Des Sel 22:273-80. 2009.... - Single domain antibodies with VH hallmarks are positively selected during panning of llama (Lama glama) naïve librariesAna 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... - Heating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domainsAurelien 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... - The binding of NCAM to FGFR1 induces a specific cellular response mediated by receptor traffickingChiara Francavilla
IFOM FIRC Institute of Molecular Oncology, IFOM IEO Campus, Milano, Italy
J Cell Biol 187:1101-16. 2009.... - Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organizationFabrizio 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... - Screening optimized protein purification protocols by coupling small-scale expression and mini-size exclusion chromatographyElisa 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... - Biotechnological applications of recombinant single-domain antibody fragmentsArio 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.... - Recombinant proteins fused to thermostable partners can be purified by heat incubationArio de Marco
European Molecular Biology Laboratory, Heidelberg, Germany
J Biotechnol 107:125-33. 2004..We proved that it can be easily automated... - Dimerization properties of a Xenopus laevis kinesin-II carboxy-terminal stalk fragmentValeria De Marco
European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
EMBO Rep 4:717-22. 2003.... - Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebratesCerstin 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... - Characterization of the aggregates formed during recombinant protein expression in bacteriaAndrea 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... - Correct identification of the chloroplastic protoporphyrinogen IX oxidase N-terminus places the biochemical data in frameArio de Marco
Biochemistry, Syngenta Crop Protection AG, P O Box, Basel, CH 4002, Switzerland
Biochem Biophys Res Commun 309:873-8. 2003.... - Physical and chemical perturbations induce the formation of protein aggregates with different structural featuresAntonino 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...