Stefano Pascarella

Stefano Pascarella received the “laurea” degree in biology in 1984 and the Ph.D. degree in biochemistry in 1989 at the University of Rome La Sapienza. During the Ph.D. course, he spent a short period as a Visiting Scientist at Department of Biochemistry, Medical College of Virginia, Richmond, Va, USA. From 1990 to 1991, he worked as a postdoctor at the European Biology Laboratory in Heidelberg, Germany, in the Biocomputing Unit supported by EMBO and European Commission fellowships. In 1991, he was appointed Researcher of the Faculty of Sciences of the University of Roma La Sapienza. In 2000, he was appointed an Associate Professor and a Full Professor of Biochemistry in 2001 at the same university. He teaches biochemistry and bioinformatics in the Biology and Biotechnology courses. He is Member of the Italian Society of Biochemistry and Molecular Biology. His scientific interests are currently focussed on the in silico analysis of protein structures to understand their structure-function relationships. The main topics of his current research are the analysis of the structural and functional properties of pyridoxal-phosphate dependent enzymes and the understanding of protein molecular adaptation to extreme conditions.

Biography Updated on 24 October 2007

Personal Home Page

http://w3.uniroma1.it/bio_chem/sito_biochimica/EN/Personale/main.html

Articles in Scholarly Journals [Incomplete List]

  1. Structural adaptation to low temperatures − analysis of the subunit interface of oligomeric psychrophilic enzymes
    FEBS Journal, vol. 274, no. 17, pp. 4595–4608, 2007
  2. A consensus procedure improving solvent accessibility prediction
    Journal of Computational Chemistry, vol. 27, no. 5, pp. 621–626, 2006
  3. CAMPO, SCR_FIND and CHC_FIND: a suite of web tools for computational structural biology
    Nucleic Acids Research, vol. 33, no. Web Server, pp. W50–W55, 2005
  4. In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family
    FEBS Journal, vol. 272, no. 4, pp. 929–941, 2005
  5. Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold-type I, pyridoxal-5'-phosphate-dependent enzymes
    Protein Science, vol. 13, no. 11, pp. 2992–3005, 2004
  6. Kinetic properties of native and mutagenized isoforms of mitochondrial alcohol dehydrogenase III purified from
    Biochimie, vol. 86, no. 9-10, pp. 705–712, 2004
  7. Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, vol. 1647, no. 1-2, pp. 214–219, 2003
  8. Improvement in prediction of solvent accessibility by probability profiles
    Protein Engineering Design and Selection, vol. 16, no. 12, pp. 987–992, 2003
  9. Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes
    Proteins: Structure, Function, and Genetics, vol. 47, no. 2, pp. 236–249, 2002
  10. Structural plasticity of thermophilic serine hydroxymethyltransferases
    Proteins: Structure, Function, and Genetics, vol. 50, no. 1, pp. 122–134, 2002
  11. Selective inhibition of human mast cell tryptase by gabexate mesylate, an antiproteinase drug
    Biochemical Pharmacology, vol. 61, no. 3, pp. 271–276, 2001
  12. l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions
    European Journal of Biochemistry, vol. 268, no. 24, pp. 6508–6525, 2001
  13. Structural adaptation of enzymes to low temperatures
    Protein Engineering Design and Selection, vol. 14, no. 3, pp. 141–148, 2001
  14. Biochemistry, vol. 39, no. 4, pp. 658–666, 2000
  15. Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling
    European Journal of Biochemistry, vol. 267, no. 9, pp. 2790–2802, 2000
  16. Characterization of five new low-molecular-mass trypsin inhibitors from white mustard (Sinapis alba L.) seed
    European Journal of Biochemistry, vol. 267, no. 21, pp. 6486–6492, 2000
  17. Characterization of low-molecular-mass trypsin isoinhibitors from oil-rape (Brassica napus var. oleifera) seed
    European Journal of Biochemistry, vol. 261, no. 1, pp. 275–284, 1999
  18. The T-Knot Motif Revisited
    Biological Chemistry, vol. 380, no. 10, pp. 1247–1250, 1999
  19. Easy method to predict solvent accessibility from multiple protein sequence alignments
    Proteins: Structure, Function, and Genetics, vol. 32, no. 2, pp. 190–199, 1998
  20. Fast-reacting Thiols in Rat Hemoglobins Can Intercept Damaging Species in Erythrocytes More Efficiently Than Glutathione
    Journal of Biological Chemistry, vol. 273, no. 30, pp. 19198–19206, 1998
  21. Stability of aspartate aminotransferase from Sulfolobus solfataricus
    Protein Engineering Design and Selection, vol. 10, no. 3, pp. 237–248, 1997
  22. A databank (3D-ali) collecting related protein sepquences and structures
    "Protein Engineering, Design and Selection", vol. 9, no. 3, pp. 249–251, 1996
  23. Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzymes
    FEBS Letters, vol. 331, no. 1-2, pp. 145–149, 1993
  24. Analysis of insertions/deletions in protein structures
    Journal of Molecular Biology, vol. 224, no. 2, pp. 461–471, 1992
  25. Biochemistry, vol. 31, no. 1, pp. 155–162, 1992
  26. A simple microcomputer program for predicting the secondary structure of proteins
    Computer Methods and Programs in Biomedicine, vol. 24, no. 3, pp. 207–208, 1987