Unfolding of cardosin A in organic solvents and detection of intermediaries

[1]  V. Shnyrov,et al.  Effect of acetonitrile on Cynara cardunculus L. cardosin A stability. , 2006, International journal of biological macromolecules.

[2]  S. Krueger,et al.  Comparison of solution structures and stabilities of native, partially unfolded and partially refolded pepsin. , 2006, Biochemistry.

[3]  Cláudia S Oliveira,et al.  Evaluation of cardosin A as a probe for limited proteolysis in non-aqueous environments—complex substrates hydrolysis , 2006 .

[4]  P. Halling,et al.  Evaluation of cardosin A as a proteolytic probe in the presence of organic solvents , 2004 .

[5]  P. Halling What can we learn by studying enzymes in non-aqueous media? , 2004, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[6]  O. Stepanenko,et al.  Conformational change of the dimeric DsbC molecule induced by GdnHCl. A study by intrinsic fluorescence. , 2004, Biochemistry.

[7]  Cláudia S Oliveira,et al.  Reverse hydrolysis by cardosin A: specificity considerations , 2004 .

[8]  V. Shnyrov,et al.  Thermostability of cardosin A from Cynara cardunculus L. , 2003 .

[9]  Luis Alberto Campos,et al.  The active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH , 2003, FEBS letters.

[10]  J. Cooper,et al.  Aspartic proteinases in disease: a structural perspective. , 2002, Current drug targets.

[11]  C. Soares,et al.  Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.* , 1999, The Journal of Biological Chemistry.

[12]  A. C. Sarmento,et al.  Cardosins A and B, two new enzymes available for peptide synthesis , 1998 .

[13]  A. Levashov,et al.  Enzyme stability in systems with organic solvents. , 1998, Biochemistry. Biokhimiia.

[14]  S. Hubbard,et al.  The structural aspects of limited proteolysis of native proteins. , 1998, Biochimica et biophysica acta.

[15]  P. Vrabel,et al.  Analysis of the mechanism and kinetics of thermal inactivation of enzymes: Critical assessment of isothermal inactivation experiments , 1996 .

[16]  J. Saraiva,et al.  Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength , 1996 .

[17]  J. Tang,et al.  Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L. , 1996, European journal of biochemistry.

[18]  P. Halling,et al.  Biocatalyst behaviour in low-water systems , 1995 .

[19]  R. Lencki,et al.  Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: I. First‐order behaviour , 1992, Biotechnology and bioengineering.

[20]  E. Pires,et al.  Stability performance ofCynara cardunculus L. acid protease in aqueous-organic biphasic systems , 1992, Biotechnology Letters.

[21]  A. Klibanov,et al.  The effect of water on enzyme action in organic media. , 1988, The Journal of biological chemistry.

[22]  J. Papamatheakis,et al.  Anomalous behavior of the major avian myeloblastosis virus glycoprotein in the presence of sodium dodecyl sulfate , 1978, Journal of virology.

[23]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[24]  K. Nakanishi,et al.  Stability of immobilized thermolysin in organic solvents. , 1999, Journal of bioscience and bioengineering.

[25]  A. Klibanov,et al.  Analysis of processes causing thermal inactivation of enzymes. , 1988, Methods of biochemical analysis.