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Increased awareness about environmental adverse effects of human activities has prompted the use of insecticides with low impact on systems associated to agriculture. Currently, the most successful biological products are based on protein toxins from the bacterial species Bacillus thuringiensis. Because of the remarkable properties of these proteins, their encoding genes were introduced into farming species (the so called Bt-crops), in such a way, that these plants are self-protected against some key insect pests. Despite the fact that a relatively large number of these toxins, with different toxicity ranges, have been described, it is still important to find new resources with novel capabilities to complement, or to replace in the future, the currently used ones. On another hand, it is important to continue studying their mode action in susceptible insects, and the changes occurred in resistant ones, to determine the most effective strategy for long lasting pest control. The focus of this Special Issue of Toxins is to provide updated information on the use of B. thuringiensis and their toxins on different field crops, the interactions of these toxins with other molecules, analyze the biochemical and molecular basis of emerging cases of resistance and, in general, to provide information which can contribute to an effective pest management with these toxins.
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Annotation Bridging cellular membranes is a key step in the pathogenic action of both binary and pore-forming bacterial toxins. The former use their translocation domains, containing various structural motifs, to ensure efficient delivery of the toxic component into the host cell, while the latter act on the cellular membrane itself. In either case, the integrity of the membrane is compromised via targeted protein-lipid and protein-protein interactions triggered by specific signals, such as proteolytic cleavage or endosomal acidification. This Special Issue presents recent advances in characterizing functional, structural and thermodynamic aspects of the conformational switching and membrane interactions involved in the cellular entry of bacterial protein toxins. Deciphering the physicochemical principles underlying these processes is also a prerequisite for the use of protein engineering to develop toxin-based molecular vehicles capable of targeted delivery of therapeutic agents to tumors and other diseased tissues.
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Increased awareness about environmental adverse effects of human activities has prompted the use of insecticides with low impact on systems associated to agriculture. Currently, the most successful biological products are based on protein toxins from the bacterial species Bacillus thuringiensis. Because of the remarkable properties of these proteins, their encoding genes were introduced into farming species (the so called Bt-crops), in such a way, that these plants are self-protected against some key insect pests. Despite the fact that a relatively large number of these toxins, with different toxicity ranges, have been described, it is still important to find new resources with novel capabilities to complement, or to replace in the future, the currently used ones. On another hand, it is important to continue studying their mode action in susceptible insects, and the changes occurred in resistant ones, to determine the most effective strategy for long lasting pest control. The focus of this Special Issue of Toxins is to provide updated information on the use of B. thuringiensis and their toxins on different field crops, the interactions of these toxins with other molecules, analyze the biochemical and molecular basis of emerging cases of resistance and, in general, to provide information which can contribute to an effective pest management with these toxins.
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Annotation Bridging cellular membranes is a key step in the pathogenic action of both binary and pore-forming bacterial toxins. The former use their translocation domains, containing various structural motifs, to ensure efficient delivery of the toxic component into the host cell, while the latter act on the cellular membrane itself. In either case, the integrity of the membrane is compromised via targeted protein-lipid and protein-protein interactions triggered by specific signals, such as proteolytic cleavage or endosomal acidification. This Special Issue presents recent advances in characterizing functional, structural and thermodynamic aspects of the conformational switching and membrane interactions involved in the cellular entry of bacterial protein toxins. Deciphering the physicochemical principles underlying these processes is also a prerequisite for the use of protein engineering to develop toxin-based molecular vehicles capable of targeted delivery of therapeutic agents to tumors and other diseased tissues.
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Venoms from marine and terrestrial animals (cone snails, scorpions, spiders, snakes, centipedes, cnidarian, etc.) can be seen as an untapped cocktail of biologically-active compounds, being increasingly recognized as new emerging source of peptide-based therapeutics. Venomous animals are considered to be specialized predators that have evolved the most sophisticated peptide chemistry and neuropharmacology for their own biological purposes by producing venoms that contains a structural and functional diversity of neurotoxins. These neurotoxins have shown to be highly selective ligands for a wide range of ion channels and receptors. Therefore, they represent interesting lead compounds for the development of, for example, analgesics, anti-cancer drugs, drugs for neurological disorders such as multiple sclerosis, Parkinson's disease, Alzheimer's disease, etc. This Special Issue of Toxins aims to provide a comprehensive look at toxins and toxin inspired leads and will focus on the mechanism of action, structure-function and evolution of pharmacological interesting venom components, including but not limited to, recent developments relating to the emergence of venoms as an underutilized source of highly evolved bioactive peptides with clinical potential.
Pharmacology. --- Toxins.
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Increased awareness about environmental adverse effects of human activities has prompted the use of insecticides with low impact on systems associated to agriculture. Currently, the most successful biological products are based on protein toxins from the bacterial species Bacillus thuringiensis. Because of the remarkable properties of these proteins, their encoding genes were introduced into farming species (the so called Bt-crops), in such a way, that these plants are self-protected against some key insect pests. Despite the fact that a relatively large number of these toxins, with different toxicity ranges, have been described, it is still important to find new resources with novel capabilities to complement, or to replace in the future, the currently used ones. On another hand, it is important to continue studying their mode action in susceptible insects, and the changes occurred in resistant ones, to determine the most effective strategy for long lasting pest control. The focus of this Special Issue of Toxins is to provide updated information on the use of B. thuringiensis and their toxins on different field crops, the interactions of these toxins with other molecules, analyze the biochemical and molecular basis of emerging cases of resistance and, in general, to provide information which can contribute to an effective pest management with these toxins.
Choose an application
Annotation Bridging cellular membranes is a key step in the pathogenic action of both binary and pore-forming bacterial toxins. The former use their translocation domains, containing various structural motifs, to ensure efficient delivery of the toxic component into the host cell, while the latter act on the cellular membrane itself. In either case, the integrity of the membrane is compromised via targeted protein-lipid and protein-protein interactions triggered by specific signals, such as proteolytic cleavage or endosomal acidification. This Special Issue presents recent advances in characterizing functional, structural and thermodynamic aspects of the conformational switching and membrane interactions involved in the cellular entry of bacterial protein toxins. Deciphering the physicochemical principles underlying these processes is also a prerequisite for the use of protein engineering to develop toxin-based molecular vehicles capable of targeted delivery of therapeutic agents to tumors and other diseased tissues.
Choose an application
Venoms from marine and terrestrial animals (cone snails, scorpions, spiders, snakes, centipedes, cnidarian, etc.) can be seen as an untapped cocktail of biologically-active compounds, being increasingly recognized as new emerging source of peptide-based therapeutics. Venomous animals are considered to be specialized predators that have evolved the most sophisticated peptide chemistry and neuropharmacology for their own biological purposes by producing venoms that contains a structural and functional diversity of neurotoxins. These neurotoxins have shown to be highly selective ligands for a wide range of ion channels and receptors. Therefore, they represent interesting lead compounds for the development of, for example, analgesics, anti-cancer drugs, drugs for neurological disorders such as multiple sclerosis, Parkinson's disease, Alzheimer's disease, etc. This Special Issue of Toxins aims to provide a comprehensive look at toxins and toxin inspired leads and will focus on the mechanism of action, structure-function and evolution of pharmacological interesting venom components, including but not limited to, recent developments relating to the emergence of venoms as an underutilized source of highly evolved bioactive peptides with clinical potential.
Pharmacology. --- Toxins.
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Bridging cellular membranes is a key step in the pathogenic action of both binary and pore-forming bacterial toxins. The former use their translocation domains, containing various structural motifs, to ensure efficient delivery of the toxic component into the host cell, while the latter act on the cellular membrane itself. In either case, the integrity of the membrane is compromised via targeted protein-lipid and protein-protein interactions triggered by specific signals, such as proteolytic cleavage or endosomal acidification. This Special Issue presents recent advances in characterizing functional, structural and thermodynamic aspects of the conformational switching and membrane interactions involved in the cellular entry of bacterial protein toxins. Deciphering the physicochemical principles underlying these processes is also a prerequisite for the use of protein engineering to develop toxin-based molecular vehicles capable of targeted delivery of therapeutic agents to tumors and other diseased tissues.
Bacterial toxins. --- Bacterial antigens --- Microbial toxins
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The very first marine-derived anticancer drug, Cytarabine (aka Ara-C, Cytosar-U(R)), was approved by the FDA in 1969 for the treatment of leukemia. At the beginning of 2021, the list of approved marine-derived anticancer drugs consists of nine substances, five of which received approval within the last two years, demonstrating the rapid evolution of the field. The current book is a collection of scientific articles related to the exponentially growing field of anticancer marine compounds. These articles cover the whole field, from agents with cancer-preventive activity, to novel and previously characterized compounds with anticancer activity, both in vitro and in vivo, as well as the latest status of compounds under clinical development.
Cancer --- Marine toxins. --- Radiotherapy.
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