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2006

Journal Article

Cyclic MrIA: A stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter

Lovelace, E. S., Armishaw, C. J., Colgrave, M. L., Wahlstrom, M. E., Alewood, P. F., Daly, N. L. and Craik, D. J. (2006). Cyclic MrIA: A stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter. Journal of Medicinal Chemistry, 49 (22), 6561-6568. doi: 10.1021/jm060299h

Cyclic MrIA: A stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter

2006

Journal Article

NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids

Marx, U. C., Daly, N. L. and Craik, D. J. (2006). NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids. Magnetic Resonance In Chemistry, 44 (Sp. Iss. SI), S41-S50. doi: 10.1002/mrc.1821

NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids

2006

Journal Article

The cyclotide family of circular miniproteins: Nature's combinatorial peptide template

Craik, D. J., Cemazar, M., Wang, C. K. L. and Daly, N. L. (2006). The cyclotide family of circular miniproteins: Nature's combinatorial peptide template. Biopolymers, 84 (3), 250-266. doi: 10.1002/hip.20451

The cyclotide family of circular miniproteins: Nature's combinatorial peptide template

2006

Journal Article

Discovery of cyclotide-like protein sequences in graminaceous crop plants: Ancestral precursors of circular proteins?

Mulvenna, J. P., Mylne, J. S., Bharathi, R., Burton, R. A., Shirley, N. J., Fincher, G. B., Anderson, M. A. and Craik, D. J. (2006). Discovery of cyclotide-like protein sequences in graminaceous crop plants: Ancestral precursors of circular proteins?. Plant Cell, 18 (9), 2134-2144. doi: 10.1105/tpc.106.042812

Discovery of cyclotide-like protein sequences in graminaceous crop plants: Ancestral precursors of circular proteins?

2006

Journal Article

A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins

Imperial, J. S., Bansal, P. S., Alewood, P. F., Daly, N. L., Craik, D., Sporning, A., Terlau, H., Lopez-Vera, E., Bandyopadhyay, P. K. and Olivera, B. M. (2006). A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins. Biochemistry, 45 (27), 8331-8340. doi: 10.1021/bi060263r

A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins

2005

Journal Article

Isolation and characterization of novel cyclotides from Viola hederaceae - Solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide

Chen, Bin, Colgrave, Michelle L., Daly, Norelle L., Rosengren, K. Johan, Gustafson, Kirk R. and Craik, David J. (2005). Isolation and characterization of novel cyclotides from Viola hederaceae - Solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide. Journal of Biological Chemistry, 280 (23), 22395-22405. doi: 10.1074/jbc.M501737200

Isolation and characterization of novel cyclotides from Viola hederaceae - Solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide

2005

Journal Article

Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance

Kamimori, Hiroshi, Hall, Kristopher, Craik, David J. and Aguilar, Marie-Isabel (2005). Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance. Analytical Biochemistry, 337 (1), 149-153. doi: 10.1016/j.ab.2004.10.028

Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance

2005

Journal Article

Peptide quantification by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry: Investigations of the cyclotide kalata B1 in biological fluids

Colgrave, M. L., Jones, A. and Craik, D. J. (2005). Peptide quantification by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry: Investigations of the cyclotide kalata B1 in biological fluids. Journal of Chromatography A, 1091 (1-2), 187-193. doi: 10.1016/j.chroma.2005.07.094

Peptide quantification by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry: Investigations of the cyclotide kalata B1 in biological fluids

2005

Journal Article

The role of disulfide bonds in the structure and function of murine epidermal growth factor (mEGF)

Alewood, D., Nielsen, K., Alewood, P. F., Craik, D. J., Andrews, P., Nerrie, M., White, S., Domagala, T., Walker, F., Rothacker, J., Burgess, A. W. and Nice, E. C. (2005). The role of disulfide bonds in the structure and function of murine epidermal growth factor (mEGF). Growth Factors, 23 (2), 97-110. doi: 10.1080/08977190500096061

The role of disulfide bonds in the structure and function of murine epidermal growth factor (mEGF)

2005

Journal Article

Novel gene sequences of cyclotides

Sando, L, Bharati, R and Craik, DJ (2005). Novel gene sequences of cyclotides. Biopolymers, 80 (4), 514-514.

Novel gene sequences of cyclotides

2005

Journal Article

Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A

Mulvenna, J. R., Sando, L. and Craik, D. J. (2005). Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A. Structure, 13 (5), 691-701. doi: 10.1016/j.str.2005.02.013

Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A

2005

Journal Article

Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1

Mulvenna, J. P., Foley, F. M. and Craik, D. J. (2005). Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1. Journal of Biological Chemistry, 280 (37), 32245-32253. doi: 10.1074/jbc.M506060200

Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1

2005

Journal Article

A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae)

Simonsen, S. M., Sando, L., Ireland, D. C., Colgrave, M. L., Bharathi, R., Goransson, U. and Craik, D. J. (2005). A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae). Plant Cell, 17 (11), 3176-3189. doi: 10.1105/tpc.105.034678

A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae)

2005

Journal Article

Isolation, solution structure, and insecticidal activity of Kalata B2, a circular protein with a twist: Do Mobius strips exist in nature?

Jennings, Cameron V., Rosengren, K. Johan, Daly, Norelle L., Plan, Manuel, Stevens, Jackie, Scanlon, Martin J., Waine, Clement, Norman, David G., Anderson, Marilyn A. and Craik, David J. (2005). Isolation, solution structure, and insecticidal activity of Kalata B2, a circular protein with a twist: Do Mobius strips exist in nature?. Biochemistry, 44 (3), 851-860. doi: 10.1021/bi047837h

Isolation, solution structure, and insecticidal activity of Kalata B2, a circular protein with a twist: Do Mobius strips exist in nature?

2005

Journal Article

Structure and folding of potato type II proteinase inhibitors: Circular permutation and intramolecular domain swapping

Schirra, H. J. and Craik, D. J. (2005). Structure and folding of potato type II proteinase inhibitors: Circular permutation and intramolecular domain swapping. Protein And Peptide Letters, 12 (5), 421-431. doi: 10.2174/0929866054395266

Structure and folding of potato type II proteinase inhibitors: Circular permutation and intramolecular domain swapping

2005

Journal Article

Structure and neurofunction of relaxin-3, the ancestral relaxin

Wade, JD, Lin, F, Rosengren, J, Craik, D, Otvos, L, Bathgate, R and Tregear, GW (2005). Structure and neurofunction of relaxin-3, the ancestral relaxin. Biopolymers, 80 (4), 538-538.

Structure and neurofunction of relaxin-3, the ancestral relaxin

2005

Journal Article

Oxidative folding of the cystine knot motif in cyclotide proteins

Craik, DJ and Daly, NL (2005). Oxidative folding of the cystine knot motif in cyclotide proteins. Protein And Peptide Letters, 12 (2), 147-152. doi: 10.2174/0929866053005863

Oxidative folding of the cystine knot motif in cyclotide proteins

2005

Journal Article

Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1

Korsinczky, M. L. J., Clark, R. J. and Craik, D. J. (2005). Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1. Biochemistry, 44 (4), 1145-1153. doi: 10.1021/bi048297r

Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1

2005

Journal Article

Engineering stable peptide toxins by means of backbone cyclization: Stabilization of the alpha-conotoxin MII

Clark, R. J., Fischer, H., Dempster, L., Daly, N. L., Rosengren, K. J., Nevin, S. T., Meunier, F. A., Adams, D. J. and Craik, D. J. (2005). Engineering stable peptide toxins by means of backbone cyclization: Stabilization of the alpha-conotoxin MII. Proceedings of The National Academy of Sciences of The United States of America, 102 (39), 13767-13772. doi: 10.1073/pnas.0504613102

Engineering stable peptide toxins by means of backbone cyclization: Stabilization of the alpha-conotoxin MII

2005

Journal Article

Threaded rings and complex topologies in novel antimicrobial peptides: Nature's bio-engineering templates

Craik, DJ, Rosengren, KJ, Sando, L and Simonsen, SM (2005). Threaded rings and complex topologies in novel antimicrobial peptides: Nature's bio-engineering templates. Biopolymers, 80 (4), 489-489.

Threaded rings and complex topologies in novel antimicrobial peptides: Nature's bio-engineering templates