Biochemistry Unit

Publications

• de Marco A, Volrath S, Bruyere T, Law M, Fonné-Pfister R (2000)
  Recombinant maize protoporphyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones.
  Prot Expr Purif 20, 81-86
• Doglio L, de Marco A, Schleich S, Krijnse Locker J (2002)
  The vaccinia virus E8R gene product: a viral membrane protein that is made early in infection and packaged into virions' core.
  J Virol 76, 9773-9786
• De Marco V, de Marco A, Correia JJ, Goldie KN, Hoenger A (2003)
  Dimerization properties of a Xenopus laevis kinesin-II C-terminal stalk fragment.
  EMBO Rep 4, 717-722
• de Marco A, Volrath S, Law M, Fonné-Pfister R (2003)
  Correct identification of the chloroplastic protoporphyrinogen IX oxidase N-terminus places the biochemical data in frame.
  Biochem Biophys Res Commun 309, 873-878
• de Marco A, Casatta E, Savaresi S, Geerlof A (2004)
  Recombinant proteins fused to thermostable partners can be purified by heat incubation.
  J Biotechnol 107, 125-133
• de Marco A, De Marco V (2004)
  Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning.
  J Biotechnol 109, 45-42
• De Marco V, Stier G, Blandin S, de Marco A (2004)
  Comparison of NusA and GST as fusion partners for recombinant expression in E. coli.
  Biochem Biophys Res Commun 322, 766-771
• de Marco A (2004)
  A step ahead: combining protein purification and correct folding selection.
  Microbial Cell Factories 3, 12
• Stegemann J, Ventzki R, Schrödel A, de Marco A (2005)
  Comparative analysis of protein aggregates by blue native electrophoresis and subsequent SDS-PAGE in a three-dimensional geometry gel.
  Proteomics 5, 2002-2009
• Schrödel A, de Marco A (2005)
  Identification and characterization of recombinant protein aggregates.
  BMC Biochemistry 6:10
• Schrödel A, Volz J, de Marco A (2005)
  Fusion tags and chaperone co-expression modulate both the solubility and the inclusion body features of the recombinant clipB14 serine protease.
  J Biotechnol 120, 2-10
• Franz C, Askjaer P, Antonin W, Lopez Iglesias C, Haselmann U, Schelder M, de Marco A, Wilm M, Antony C, Mattaj IW (2005)
  Nup155 is essential for nuclear envelope and nuclear pore complex formation in nematodes and vertebrates.
  EMBO J, 24, 3519-3531
• de Marco A, Vigh L, Diamant S, Goloubinoff P (2005)
  Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.
  Cell Stress Chaperones, 10, 329-339
• Dümmler A, Lawrence A-M, de Marco A (2005)
  Rational cloning simplify the screening of the optimal conditions for soluble recombinant protein production.
  Microbial Cell Factories 4, 34
• Huang H, Liu J, de Marco A (2006)
  Induced fit of passenger proteins fused to Archaea maltose-binding proteins.
  Biochem Biophys Res Commun, 344, 25-29
• Ventzki R, Stegemann J, Martinez L, de Marco A (2006)
  Automated protein analysis by online detection of laser-induced fluorescence in slab gels and 3 D geometry gels.
  Electrophoresis, 27, 3338-3348
• Schultz T, Martinez L, de Marco A (2006)
  The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter.
  Microbial Cell Factories, 5:28
• de Marco A (2006)
  Two-step metal affinity purification of double tagged (NusA-His6) fusion proteins.
  Nature Protocols, 1:1538-1543
• Olichon A, Schweizer D, Muyldermans S, de Marco A (2007)
  Heating represents a rapid purification method for recovering correctly folded thermo tolerant VH and VHH domains.
  BMC Biotechnology, 7:7
• Schultz T, Liu J, Capasso P, de Marco A (2007)
  The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformation.
  Biochem Biophys Res Commun, 335:234-239
• de Marco A, Deuerling E, Mogk A, Tomoyasu T, Bukau B (2007)
  Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli.
  BMC Biotechnology, 7:32
• Arena S, Isella C, Martini M, de Marco A, Medico E, Bardelli A (2007)
  Knock-in of oncogenic KRAS does not transform mouse somatic cells but triggers a transcriptional response that classifies human cancers.
  Cancer Res 67:8468-8476
• de Marco A (2007)
  Protocol for preparing proteins with improved solubility by co-expression with molecular chaperones in Escherichia coli.
  Nature Protocols, 2:2632-2639
• Nataliello A, Santarella R, Doglia SM, de Marco A (2008)
  Physical and chemical perturbations induce the formation of protein aggregates with different structural features.
  Protein Expr Purif 58:356-361
• de Marco A (2008)
  Minimal Information: an urgent need to assess the functional reliability of recombinant proteins used in biological experiments.
  Microbial Cell Factories 7:20
• Nataliello A, Liu J, Ami D, Doglia SM, de Marco A (2009)
  The osmolyte betaine promotes protein misfolding and disruption of protein aggregates.
  Proteins, in press and available on line
• Ami D, Nataliello A, Schultz T, Gatti-Lafranconi P, Lotti M, Doglia SM, de Marco A (2009)
  Protein misfolding induces rearrangements in bacterial membranes.
  BBA Mol Biol 1794:263-9
• Monegal A, Huang H, Ami D, Martinelli C, Aliprandi M, Capasso P, Francavilla C, Ossolengo G, de Marco A (2009)
  Immunological applications of single domain llama recombinant antibodies isolated from a large naïve library.
  Prot Engineer Des Sel, in press
• de Marco A, Sevastianovich Y, Cole J (2009)
  Minimal Information for Protein Functional Evaluation (MIPFE) Workshop.
  New Biotechnol, in press