P. W. Kuchel

Publication List Details

Period

2002 - 2007

Number

9

Co-Authors

Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom (2007)

Torres, A. M., Tsampazi, M., Kennett, E. C., Belov, K., Geraghty, D. P., Bansal, P. S., ...

Platypus venom contains an isomerase that reversibly interconverts the second amino-acid residue in some peptides between the L-form and the D-form. The enzyme acts on the natriuretic peptides OvCNPa...

Mammalian L-to-D-amino-acid-residue isomerase from platypus venom (2006)

Torres, A. M., Tsampazi, M., Tsampazi, C., Kennett, EC, Belov, K., Geraghty, D. P., ...

The presence Of D-amino-acid-containing polypeptides, defensin-like peptide (DLP)-2 and Ornithorhyncus venom C-type natriuretic peptide (OvCNP)b, in platypus venom suggested the existence of a...

D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties (2005)

Torres, A. M., Tsampazi, C., Geraghty, D. P., Bansal, P. S., Alewood, P. F., Kuchel, P. W.

The recent discovery that the natriuretic peptide OvCNPb (Ornithorhynchus venom C-type natriuretic peptide B) from platypus (Ornithorynchus anatinus) venom contains a D-amino acid residue suggested...

NMR studies of exchange between intra- and extracellular glutathione in human erythrocytes (2005)

Kennett, E. C., Bubb, W. A., Bansal, P., Alewood, P., Kuchel, P. W.

Glutathione is the main source of intracellular antioxidant protection in the human erythrocyte and its redox status has frequently been used as a measure of oxidative stress. Extracellular...

Diffusion coefficients of the monomer and oligomers in hydroxyethyl methacrylate (2003)

Strauch, J., McDonald, J., Chapman, B. E., Kuchel, P. W., Hawkett, B. S., Roberts, G. E., ...

The diffusion coefficients are reported of rubbery ternary systems consisting of the polymer, its monomer analogue (i.e., the saturated equivalent of the monomer), and trace quantities of oligomers...

Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin (2003)

Torres, A. M., Bansal, P., Alewood, P. F., Bursill, J. A., Kuchel, P. W., Vandenberg, J. I.

The three-dimensional structure of chemically synthesized CnErg1 (Ergtoxin), which specifically blocks HERG (human ether-a-go-go-related gene) K+ channels, was determined by nuclear magnetic...

Structure of the HERG K+ channel S5P extracellular linker - Role of an amphipathic alpha-helix in C-type inactivation (2003)

Torres, A. M., Bansal, P. S., Sunde, M., Clarke, C. E., Bursill, J. A., Smith, D. J., ...

The HERG K+ channel has very unusual kinetic behavior that includes slow activation but rapid inactivation. These features are critical for normal cardiac repolarization as well as in preventing...

D-amino acid residue in the C-type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus (2002)

Torres, A. M., Menz, I., Alewood, P. F., Bansal, P., Lahnstein, J., Gallagher, C. H., ...

The C-type natriuretic peptide from the platypus venom (OvCNP) exists in two forms, OvCNPa and OvCNPb, whose amino acid sequences are identical. Through the use of nuclear magnetic resonance, mass...

The S631A Mutation Causes a Mechanistic Switch in the Block of hERG Channels by CnErg1

Hill, Adam P., Campbell, T. J., Bansal, P. S., Kuchel, P. W., Vandenberg, J. I.

We have studied the interaction of CnErg1, a member of the γ-KTX subfamily of scorpion toxins with the inactivation-deficient S631A hERG channel. In the background of this mutation, we observed a...