Abstract: The present invention includes novel systems, methods, and compositions for the enzymatic/chemical production of pseudouridine (?) and its variants, such as N1-methyl-pseudouridine-5?-triphosphate (m1?TP).

Abstract: The present invention includes novel systems, methods, and compositions for the enzymatic/chemical production of pseudouridine (?) and its variants, such as N1-methyl-pseudouridine-5?-triphosphate (m1?TP).

Abstract: The invention includes novel, systems, methods and compositions for the in vitro production of polynucleotides, and in particular the production of mRNA for use in therapeutic applications.

Abstract: The present invention relates to conjugates comprising a protein and multivalent cell-penetrating peptide(s), each multivalent cell-penetrating peptide comprising at least two cell-penetrating peptides, wherein the multivalent cell-penetrating peptide(s) is/are covalently attached to the protein. The present invention furthermore relates to a method of generating the conjugates and to their medical uses, in particular their use in the diagnosis, prevention and/or treatment of diseases. The present invention relates to methods of diagnosis, prevention and/or treatment of diseases, comprising administering the conjugates of the invention to a patient.

Abstract: The discovery of a non-ribosomal peptide synthetase (NRPS) gene cluster in the genome of Clostridium thermocellum that produces a secondary metabolite that is assembled outside of the host membrane is described. Also described is the identification of homologous NRPS gene clusters from several additional microorganisms. The secondary metabolites produced by the NRPS gene clusters exhibit broad spectrum antibiotic activity. Thus, antibiotic compounds produced by the NRPS gene clusters, and analogs thereof, their use for inhibiting bacterial growth, and methods of making the antibiotic compounds are described.

Abstract: The discovery of a non-ribosomal peptide synthetase (NRPS) gene cluster in the genome of Clostridium thermocellum that produces a secondary metabolite that is assembled outside of the host membrane is described. Also described is the identification of homologous NRPS gene clusters from several additional microorganisms. The secondary metabolites produced by the NRPS gene clusters exhibit broad spectrum antibiotic activity. Thus, antibiotic compounds produced by the NRPS gene clusters, and analogs thereof, their use for inhibiting bacterial growth, and methods of making the antibiotic compounds are described.

Abstract: The present invention relates to conjugates comprising a protein and multivalent cell-penetrating peptide(s), each multivalent cell-penetrating peptide comprising at least two cell-penetrating peptides, wherein the multivalent cell-penetrating peptide(s) is/are covalently attached to the protein. The present invention furthermore relates to a method of generating the conjugates and to their medical uses, in particular their use in the diagnosis, prevention and/or treatment of diseases. The present invention relates to methods of diagnosis, prevention and/or treatment of diseases, comprising administering the conjugates of the invention to a patient.

Abstract: A simple mutant of the natural asparagine oxygenase comprises at least the amino acids 13 to 318 of the natural asparagine oxygenase AsnO. In this protein according to the present invention, comprising at least the amino acids 13-318 of AsnO D241N, the amino acid residue at position 241 of the natural asparagine oxygenase AsnO is exchanged from aspartate (D) to asparagine (N). The protein according to the present invention, comprising at least the amino acids 13-318 of AsnO D241N, is produced by means of a directed mutagenesis from the AsnO wild type, cloning of this expression plasmid into a vector, transformation of the vector plasmid construction into a host organism and expression of the recombinant protein. The protein according to the present invention is suitable for the chemoenzymatic and enantioselective production of L-threo-hydroxyaspartate from L-aspartate. The protein is substrate-specific and converts quantitatively L-aspartate into L-threo-hydroxyaspartate.