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physcomitrella patens/antimykotikum

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ArtikelKlinische VersuchePatente
13 Ergebnisse

Moss-Produced, Glycosylation-Optimized Human Factor H for Therapeutic Application in Complement Disorders.

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Genetic defects in complement regulatory proteins can lead to severe renal diseases, including atypical hemolytic uremic syndrome and C3 glomerulopathies, and age-related macular degeneration. The majority of the mutations found in patients with these diseases affect the glycoprotein complement

Physcomitrella patens: a non-vascular plant for recombinant protein production.

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The moss Physcomitrella patens is a long-standing model for studying plant development, growth and cell differentiation in particular. Interest in this non-vascular plant arose following the discovery that homologous recombination is an efficient process. P. patens is, therefore, a tool of choice
Recently, the moss Physcomitrella patens was established as a versatile tool in plant functional genomics. Mosses represent the oldest living clade of land plants, separated by approximately 450 million years of evolution from crop plants. Consequently, mosses contain metabolites and genes not known
To overcome the potential future demand for terpenoids used as drugs, a new production platform is currently being established in our laboratory. The moss Physcomitrella has been chosen as the candidate organism for production of drug candidates based on terpenoids derived from plants, with a
Production of apoplastic reactive oxygen species (ROS), or oxidative burst, is among the first responses of plants upon recognition of microorganisms. It requires peroxidase or NADPH oxidase (NOX) activity and factors maintaining cellular redox homeostasis. Here, PpTSPO1 involved in mitochondrial

In vivo assembly of DNA-fragments in the moss, Physcomitrella patens.

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Direct assembly of multiple linear DNA fragments via homologous recombination, a phenomenon known as in vivo assembly or transformation associated recombination, is used in biotechnology to assemble DNA constructs ranging in size from a few kilobases to full synthetic microbial genomes. It has also

Targeted knockouts of Physcomitrella lacking plant-specific immunogenic N-glycans.

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Using plants as production factories for therapeutic proteins requires modification of their N-glycosylation pattern because of the immunogenicity of plant-specific sugar residues. In an attempt towards such humanization, we disrupted the genes for alpha1,3-fucosyltransferase and

Moss-based production of asialo-erythropoietin devoid of Lewis A and other plant-typical carbohydrate determinants.

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Protein therapeutics represent one of the most increasing areas in the pharmaceutical industry. Plants gain acceptance as attractive alternatives for high-quality and economical protein production. However, as the majority of biopharmaceuticals are glycoproteins, plant-specific N-glycosylation has
BACKGROUND Membrane proteins represent roughly one third of the human proteome and many of them serve as targets of therapeutic drugs. An exception is the SLC solute carrier superfamily with only a handful of approved drugs targeting SLCs. Indeed, for many of the SLCs, the natural transport

In vivo glyco-engineered antibody with improved lytic potential produced by an innovative non-mammalian expression system.

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Recent studies have demonstrated that the reduction of the core fucosylation on N-glycans of human IgGs is responsible for a clearly enhanced antibody-dependent cellular cytotoxicity (ADCC). This finding might give access to improved active therapeutic antibodies. Here, the expression of the tumor

Glycoprotein production in moss bioreactors.

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Complex multimeric recombinant proteins such as therapeutic antibodies require a eukaryotic expression system. Transgenic plants may serve as promising alternatives to the currently favored mammalian cell lines or hybridomas. In contrast to prokaryotic systems, posttranslational modifications of

Glyco-engineering for biopharmaceutical production in moss bioreactors.

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The production of recombinant biopharmaceuticals (pharmaceutical proteins) is a strongly growing area in the pharmaceutical industry. While most products to date are produced in mammalian cell cultures, namely Chinese hamster ovary cells, plant-based production systems gained increasing acceptance

Recombinant Production of MFHR1, A Novel Synthetic Multitarget Complement Inhibitor, in Moss Bioreactors.

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The human complement system is an important part of the immune system responsible for lysis and elimination of invading microorganisms and apoptotic body cells. Improper activation of the system due to deficiency, mutations, or autoantibodies of complement regulators, mainly factor H (FH) and
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