Cemazar, M., Joshi, A., Daly, N. L., Mark, A. E., Craik, D. J.
We have determined the three-dimensional structure of a two-disulfide intermediate (Cys8-Cys20, Cys14-Cys26) on the oxidative folding pathway of the cyclotide MCoTI-II. Cyclotides have a range of...
The chemistry and biology of cyclotides (2007)
Craik, DJ, Cemazar, M, Daly, NL
Cyclotides are mini-proteins with a macrocyclic peptide backbone and cystine-knot arrangement of disulfide bonds that makes them exceptionally stable to chemical, thermal or enzymatic degradation....
Gruber, GW, Cemazar, M, Clark, R, Horibe, T, Renda, R, Anderson, MA, ...
Gruber, C. W, Cemazar, M., Clark, R. .J, Horibe, T, Renda, R. F., Anderson, M. A., ...
We have isolated a protein-disulfide isomerase (PDI) from Oldenlandia affinis (OaPDI), a coffee family ( Rubiaceae) plant that accumulates knotted circular proteins called cyclotides. The novel plant...
Insecticidal plant cyclotides and related cystine knot toxins (2007)
Gruber, C. W, Cemazar, M., Anderson, MA, Craik, D. J
Cyclotides are small disulphide-rich peptides found in plants from the violet (Violaceae), coffee (Rubiaceae) and cucurbit (Cucurbitaceae) families. They have the distinguishing structural features...
The chemistry and biology of cyclotides (2007)
Craik, D. J., Cemazar, M., Daly, N. L.
Cyclotides are mini-proteins with a macrocyclic peptide backbone and cystine-knot arrangement of disulfide bonds that makes them exceptionally stable to chemical, thermal or enzymatic degradation....
Heras, B., Kurz, M., Jarrott, R., Shouldice, S. R., Frei, P., Robin, G., ...
In Gram-negative bacteria, the introduction of disulfide bonds into folding proteins occurs in the periplasm and is catalyzed by donation of an energetically unstable disulfide from DsbA, which is...
Gruber, C. W, Cemazar, M., Clark, R. .J, Horibe, T, Renda, R. F., Anderson, M. A., ...
We have isolated a protein-disulfide isomerase (PDI) from Oldenlandia affinis (OaPDI), a coffee family ( Rubiaceae) plant that accumulates knotted circular proteins called cyclotides. The novel plant...
Insecticidal plant cyclotides and related cystine knot toxins (2007)
Gruber, C. W, Cemazar, M., Anderson, MA, Craik, D. J
Cyclotides are small disulphide-rich peptides found in plants from the violet (Violaceae), coffee (Rubiaceae) and cucurbit (Cucurbitaceae) families. They have the distinguishing structural features...
The chemistry and biology of cyclotides (2007)
Craik, D. J., Cemazar, M., Daly, N. L.
Cyclotides are mini-proteins with a macrocyclic peptide backbone and cystine-knot arrangement of disulfide bonds that makes them exceptionally stable to chemical, thermal or enzymatic degradation....
Heras, B., Kurz, M., Jarrott, R., Shouldice, S. R., Frei, P., Robin, G., ...
In Gram-negative bacteria, the introduction of disulfide bonds into folding proteins occurs in the periplasm and is catalyzed by donation of an energetically unstable disulfide from DsbA, which is...
Zahariev, S, Guarnaccia, C, Pongor, CI, Quaroni, L, Cemazar, M, Pongor, S
We developed an efficient, cost effective strategy for Fmoc-based solid phase synthesis of 'difficult' peptides and/or peptides containing Asp/Asn-Gly sequences, free of aspartimide and related...
Cyclotides are a large family of mini-proteins that have the distinguishing features of a head-to-tail cyclised backbone and a cystine knot formed by six conserved cysteine residues. They are present...
Cemazar, M., Daly, N. L., Haggblad, S., Lo, K. P., Yulyaningsih, E., Craik, D. J.
The aim of this work was to elucidate the oxidative folding mechanism of the macrocyclic cystine knot protein MCoTI-II. We aimed to investigate how the six-cysteine residues distributed on the...
Protein disulfide isomerase: the structure of oxidative folding (2006)
Gruber, C. W., Cemazar, M., Heras, B., Martin, J. L., Craik, D. J.
Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, a...
The cyclotide family of circular miniproteins: Nature's combinatorial peptide template (2006)
Craik, D. J., Cemazar, M., Wang, C. K. L., Daly, N. L.
The cyclotides are a recently discovered family of miniproteins that contain a head-to-tail cyclized backbone and a knotted arrangement of disulfide bonds. They are approximately 30 amino acids in...
The cyclotides and related macrocyclic peptides as scaffolds in drug design (2006)
Craik, D. J., Cemazar, M., Daly, N. L.
The applicability of linear peptides as drugs is potentially limited by their susceptibility to proteolytic cleavage and poor bioavailability. Cyclotides are macrocyclic cystine-knotted mini-proteins...
Cyclotides are a large family of mini-proteins that have the distinguishing features of a head-to-tail cyclised backbone and a cystine knot formed by six conserved cysteine residues. They are present...
Cemazar, M., Daly, N. L., Haggblad, S., Lo, K. P., Yulyaningsih, E., Craik, D. J.
The aim of this work was to elucidate the oxidative folding mechanism of the macrocyclic cystine knot protein MCoTI-II. We aimed to investigate how the six-cysteine residues distributed on the...
Protein disulfide isomerase: the structure of oxidative folding (2006)
Gruber, C. W., Cemazar, M., Heras, B., Martin, J. L., Craik, D. J.
Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, a...
The cyclotide family of circular miniproteins: Nature's combinatorial peptide template (2006)
Craik, D. J., Cemazar, M., Wang, C. K. L., Daly, N. L.
The cyclotides are a recently discovered family of miniproteins that contain a head-to-tail cyclized backbone and a knotted arrangement of disulfide bonds. They are approximately 30 amino acids in...
The cyclotides and related macrocyclic peptides as scaffolds in drug design (2006)
Craik, D. J., Cemazar, M., Daly, N. L.
The applicability of linear peptides as drugs is potentially limited by their susceptibility to proteolytic cleavage and poor bioavailability. Cyclotides are macrocyclic cystine-knotted mini-proteins...
Graph-representation of oxidative folding pathways (2005)
Agoston, V, Cemazar, M, Kajan, L, Pongor, S
Background: The process of oxidative folding combines the formation of native disulfide bond with conformational folding resulting in the native three-dimensional fold. Oxidative folding pathways can...
Graph-representation of oxidative folding pathways (2005)
Agoston, V., Cemazar, M., Kajan, L., Pongor, S.
Background: The process of oxidative folding combines the formation of native disulfide bond with conformational folding resulting in the native three-dimensional fold. Oxidative folding pathways can...
Cemazar, M., Wilson, I., Dachs, G.U., Tozer, G.M., Sersa, G.
Background Electroporation is currently receiving much attention as a way to increase drug and DNA delivery. Recent studies demonstrated the feasibility of electrogene therapy using a range of...
Cemazar, M., Wilson, I., Dachs, G.U., Tozer, G.M., Sersa, G.
Background Electroporation is currently receiving much attention as a way to increase drug and DNA delivery. Recent studies demonstrated the feasibility of electrogene therapy using a range of...
Cemazar, M., Wilson, I., Dachs, G.U., Tozer, G.M., Sersa, G.
Background Electroporation is currently receiving much attention as a way to increase drug and DNA delivery. Recent studies demonstrated the feasibility of electrogene therapy using a range of...
Cemazar, M, Zahariev, S, Pongor, S, Hore, PJ
Oxidative folding is the fusion of native disulfide bond formation with conformational folding. This complex process is guided by two types of interactions: first, covalent interactions between...
Hudaky, I, Gaspari, Z, Carugo, O, Cemazar, M, Pongor, S, Perezel, A
A systematic comparison is made between experimental and computational data gained on vicinal disulfide bridges in proteins and peptides. Structural and stability data of ab initio and density...
Solvent-free synthesis of azole carboximidamides (2004)
Zahariev, S, Guarnaccia, C, Lamba, D, Cemazar, M, Pongor, S
A one-pot procedure is described for the preparation of 1H-pyrazole-carboximidamides 2, 1 H-benzotriazole-carboximidamides 3 and guanidinylation of amines with 3. The X-ray crystal structure of...
Cemazar, M., Zahariev, S., Pongor, S., Hore, P. J.
Oxidative folding is the fusion of native disulfide bond formation with conformational folding. This complex process is guided by two types of interactions: first, covalent interactions between...
Hudaky, I., Gaspari, Z., Carugo, O., Cemazar, M., Pongor, S., Perezel, A.
A systematic comparison is made between experimental and computational data gained on vicinal disulfide bridges in proteins and peptides. Structural and stability data of ab initio and density...
Solvent-free synthesis of azole carboximidamides (2004)
Zahariev, S., Guarnaccia, C., Lamba, D., Cemazar, M., Pongor, S.
A one-pot procedure is described for the preparation of 1H-pyrazole-carboximidamides 2, 1 H-benzotriazole-carboximidamides 3 and guanidinylation of amines with 3. The X-ray crystal structure of...
Cemazar, M, Zahariev, S, Lopez, JJ, Carugo, O, Jones, JA, Hore, PJ, ...
The oxidative folding of the Amaranthus alpha-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the...
Vicinal disulfide turns (2003)
Carugo, O, Cemazar, M, Zahariev, S, Hudaky, I, Gaspari, Z, Perczel, A, ...
The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn...
Cemazar, M., Zahariev, S., Lopez, J. J., Carugo, O., Jones, J. A., Hore, P. J., ...
The oxidative folding of the Amaranthus alpha-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the...
Vicinal disulfide turns (2003)
Carugo, O., Cemazar, M., Zahariev, S., Hudaky, I., Gaspari, Z., Perczel, A., ...
The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn...
The importance of electric field distribution for effective in vivo electroporation of tissues.
Miklavcic, D, Beravs, K, Semrov, D, Cemazar, M, Demsar, F, Sersa, G
Cells exposed to short and intense electric pulses become permeable to a number of various ionic molecules. This phenomenon was termed electroporation or electropermeabilization and is widely used...
The importance of electric field distribution for effective in vivo electroporation of tissues.
Miklavcic, D, Beravs, K, Semrov, D, Cemazar, M, Demsar, F, Sersa, G
Cells exposed to short and intense electric pulses become permeable to a number of various ionic molecules. This phenomenon was termed electroporation or electropermeabilization and is widely used...
The cyclotides and related macrocyclic peptides as scaffolds in drug design
Craik, DJ, Cemazar, M, Daly, NL
The applicability of linear peptides as drugs is potentially limited by their susceptibility to proteolytic cleavage and poor bioavailability. Cyclotides are macrocyclic cystine-knotted mini-proteins...
Cemazar, M, Daly, NL, Haggblad, S, Lo, KP, Yulyaningsih, E, Craik, DJ
The aim of this work was to elucidate the oxidative folding mechanism of the macrocyclic cystine knot protein MCoTI-II. We aimed to investigate how the six-cysteine residues distributed on the...
The cyclotide family of circular miniproteins: Nature's combinatorial peptide template
Craik, DJ, Cemazar, M, Wang, CKL, Daly, NL
The cyclotides are a recently discovered family of miniproteins that contain a head-to-tail cyclized backbone and a knotted arrangement of disulfide bonds. They are approximately 30 amino acids in...
Cyclotides are a large family of mini-proteins that have the distinguishing features of a head-to-tail cyclised backbone and a cystine knot formed by six conserved cysteine residues. They are present...
Protein disulfide isomerase: the structure of oxidative folding
Gruber, CW, Cemazar, M, Heras, B, Martin, JL, Craik, DJ
Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, a...
Effective treatment of cutaneous and subcutaneous malignant tumours by electrochemotherapy.
Mir, L. M., Glass, L. F., Sersa, G., Teissié, J., Domenge, C., Miklavcic, D., ...
Electrochemotherapy (ECT) enhances the effectiveness of chemotherapeutic agents by administering the drug in combination with short intense electric pulses. ECT is effective because electric pulses...
Sersa, G, Jarm, T, Kotnik, T, Coer, A, Podkrajsek, M, Sentjurc, M, ...
Electrochemotherapy has a direct cytotoxic effect on tumour cells, and presumably, a vascular disrupting effect. In this study, on the basis of the prediction of the mathematical model, histological...
Cemazar, M, Wilson, I, Prise, V E, Bell, K M, Hill, S A, Tozer, G M
The vascular effects of the endothelin B (ETB) receptor agonist IRL 1620 were investigated in the rat P22 carcinosarcoma and a range of normal tissues in BDIX rats. Tissue blood flow rate was...
Cemazar, M, Parkins, C S, Holder, A L, Chaplin, D J, Tozer, G M, Sersa, G
Recent studies have indicated that the antitumour effectiveness of electrochemotherapy, a combination of chemotherapeutic drugs with application of high voltage electric pulses applied to the tumour...
Reduced blood flow and oxygenation in SA-1 tumours after electrochemotherapy with cisplatin
Sersa, G, Krzic, M, Sentjurc, M, Ivanusa, T, Beravs, K, Kotnik, V, ...
Electrochemotherapy is an antitumour treatment that utilises locally delivered electric pulses to increase cytotoxicity of chemotherapeutic drugs. Besides increased drug delivery, application of...