Position: Permanent Staff
Email: a.hochkoeppler@unibo.it
Phone: 051 2093-671
Location: Bologna
Gene silencing in prokaryotes.
Enzymes structure and kinetics.
Overexpression and purification of proteins.
Protein engineering.
Synthetic Biology.
Industrial enzymes.
1982: Degree in Crop Sciences, at the University of Bologna (110 cum laude/110). Title: "Effect of Sowing Season on Productivity of Vicia faba".
1983-1987: PhD in Crop Sciences, at the University of Bologna. Title: "Investigations on soybean: a) inoculation of soil with Rhizobium japonicum; b) solubilization of soybean mitochondria in reverse micelles". Advisor: Prof. G. Venturi (University of Bologna); co-advisor: Prof. P.L. Luisi (Federal Institute of Technology, Zurich, Switzerland).
1987-1998: Studies and research activity at: Institute for Industrial Crops (Bologna, Italy); Institute for Plant Physiology (CNR, Milano, Italy); Federal Institute of Technology (Zurich, Switzerland); Department of Biology, University of Bologna (Bologna, Italy); Max Planck Institute for Biophysical Chemistry (Göttingen, Germany); Institut für Biologie II, University of Freiburg (Freiburg, Germany); Department of Chemistry and Biochemistry, University of Arizona (USA).
1998: fellow of the “Advanced Bacterial Genetics” course, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USA.
1998-present: Associate Professor at the Department of Industrial Chemistry of the University of Bologna.
Lactate-Induced HBEGF Shedding and EGFR Activation: Paving the Way to a New Anticancer Therapeutic Opportunity
- Rossi V. - Alejandro Hochkoeppler - Govoni M. - Di Stefano G.Peptides inhibiting the assembly of monomeric human l-lactate dehydrogenase into catalytically active homotetramer decrease the synthesis of lactate in cultured cells
- Alessandra Stefan - Gentilucci L. - Ruffolo F. - Rossi V. - Sordi S. - He T. - di Stefano G. - Santino F. - Brigotti M. - Scotti C. - Iamele L. - de Jonge H. - Piaz F.D. - Santarcangelo D.R. - Alejandro HochkoepplerThe catalytic action of human D-lactate dehydrogenase is severely inhibited by oxalate and is impaired by mutations triggering D-lactate acidosis
- Alessandra Stefan - Mucchi A. - Alejandro HochkoepplerThe four subunits of rabbit skeletal muscle lactate dehydrogenase do not exert their catalytic action additively
- Rossi M. - Tomaselli F. - Alejandro HochkoepplerThe Mycobacterium tuberculosis protein tyrosine phosphatase MptpA features a pH dependent activity overlapping the bacterium sensitivity to acidic conditions
- Kovermann M. - Alessandra Stefan - Palazzetti C. - Immler F. - Dal Piaz F. - Bernardi L. - Cimone V. - Bellone M.L. - Alejandro HochkoepplerTrehalose counteracts the dissociation of tetrameric rabbit lactate dehydrogenase induced by acidic pH conditions
- Simongini M. - Puglisi A. - Genovese F. - Alejandro HochkoepplerAmberlite XAD-4 is a convenient tool for removing Triton X-100 and Sarkosyl from protein solutions
- Scutteri L. - Maltoni G. - Alejandro HochkoepplerHigh-yield production in Escherichia coli and convenient purification of a candidate vaccine against SARS-CoV-2
- Maltoni G. - Scutteri L. - Mensitieri F. - Piaz F.D. - Alejandro HochkoepplerAllosteric transitions of rabbit skeletal muscle lactate dehydrogenase induced by pH-dependent dissociation of the tetrameric enzyme
- Iacovino L.G. - Rossi M. - Di Stefano G. - Rossi V. - Binda C. - Brigotti M. - Tomaselli F. - Pasti A.P. - Dal Piaz F. - Cerini S. - Alejandro HochkoepplerHuman lactate dehydrogenase A undergoes allosteric transitions under pH conditions inducing the dissociation of the tetrameric enzyme
- Pasti A.P. - Rossi V. - Di Stefano G. - Brigotti M. - Alejandro HochkoepplerConsorzio interuniversitario per lo sviluppo dei Sistemi a Grande Interfase
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