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- Publications
- Influence
Alignment/phylogeny of the papain superfamily of cysteine proteases.
- P. Berti, A. C. Storer
- Biology, Medicine
- Journal of molecular biology
- 17 February 1995
An alignment/phylogeny of the papain superfamily of cysteine proteases was created using an initial structure-based alignment followed by successive iterations of sequence alignment and phylogenetic… Expand
Concentration of MgATP2- and other ions in solution. Calculation of the true concentrations of species present in mixtures of associating ions.
- A. C. Storer, A. Cornish-Bowden
- Chemistry, Medicine
- The Biochemical journal
- 1 October 1976
1. A simple method is described for calculating the free concentrations of all species in a mixture of several ionic components that associate at equilibrium to any extent and with any… Expand
Catalytic mechanism in papain family of cysteine peptidases.
- A. C. Storer, R. Ménard
- Chemistry, Medicine
- Methods in enzymology
- 1994
Publisher Summary This chapter summarizes catalytic mechanism for cysteine peptidases of the papain family. Cysteine peptidases of the papain family catalyze the hydrolysis of peptide, amide, ester,… Expand
Functional expression of human cathepsin S in Saccharomyces cerevisiae. Purification and characterization of the recombinant enzyme.
- D. Brömme, P. Bonneau, +6 authors T. Vernet
- Biology, Medicine
- The Journal of biological chemistry
- 5 March 1993
A cDNA encoding the human lysosomal cysteine proteinase cathepsin S precursor has been expressed in yeast using the pVT100-U expression vector containing the alpha-factor promoter. The procathepsin S… Expand
A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain.
- R. Ménard, H. Khouri, +7 authors A. C. Storer
- Chemistry, Medicine
- Biochemistry
- 17 July 1990
The controversy concerning the various suggested roles for the side chain of Asp158 in the active site of papain has been clarified by using site-directed mutagenesis. Both wild-type papain and an… Expand
NMR structural studies of human cystatin C dimers and monomers.
- I. Ekiel, M. Abrahamson, +9 authors K. Gehring
- Chemistry, Medicine
- Journal of molecular biology
- 15 August 1997
Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity as a cysteine proteinase inhibitor. A similar process of dimerization has been observed… Expand
Mechanistic and structural studies on Rhodococcus ATCC 39484 nitrilase.“
- D. Stevenson, R. Feng, F. Dumas, D. Groleau, A. Mihoc, A. C. Storer
- Chemistry, Medicine
- Biotechnology and applied biochemistry
- 1 June 1992
Rhodococcus ATCC 39484 produced a nitrilase when induced with isovaleronitrile. The enzyme was obtainable pure in milligram amounts, had a subunit Mr of 40 kDa, and demonstrated a substrate‐induced… Expand
Processing of the Papain Precursor
- T. Vernet, P. Berti, +6 authors D. Thomas
- Biology, Medicine
- The Journal of Biological Chemistry
- 5 May 1995
The cysteine protease papain is synthesized as a 40-kDa inactive precursor with a 107-amino-acid N-terminal pro region. Although sequence conservation in the pro region is lower than in the mature… Expand
A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses.
- H. Khouri, C. Plouffe, S. Hasnain, T. Hirama, A. C. Storer, R. Ménard
- Chemistry, Medicine
- The Biochemical journal
- 1 May 1991
1. Three synthetic substrates of cathepsin B (EC 3.4.22.1) with various amino acid residues at the P2 position (Cbz-Phe-Arg-NH-Mec, Cbz-Arg-Arg-NH-Mec and Cbz-Cit-Arg-NH-Mec, where Cbz represents… Expand
Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase.
- A. C. Storer, A. Cornish-Bowden
- Chemistry, Medicine
- The Biochemical journal
- 1 July 1977
Inhibition studies of glucokinase were carried out with the products of the reaction, glucose 6-phosphate and MgADP-, as well as with ADP3-, Mg2+ and ATP4-. The results of these, together with those… Expand