Pichia pastoris: protein production host and model organism for biomedical research. - Test2 - elhamkhani - TriplyDB

Pichia pastoris: protein production host and model organism for biomedical research.

Pichia pastoris: protein production host and model organism for biomedical research.

http://www.wikidata.org/entity/Q38078461

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Recombinant production of plant lectins in microbial systems for biomedical application - the frutalin case study The bud tip is the cellular hot spot of protein secretion in yeasts.Improved production of a recombinant Rhizomucor miehei lipase expressed in Pichia pastoris and its application for conversion of microalgae oil to biodiesel.Scaling-up Fermentation of Pichia pastoris to demonstration-scale using new methanol-feeding strategy and increased air pressure instead of pure oxygen supplement Autolysis of Pichia pastoris induced by cold.The effect of hypoxia on the lipidome of recombinant Pichia pastoris.Model based engineering of Pichia pastoris central metabolism enhances recombinant protein production Secretion of a foreign protein from budding yeasts is enhanced by cotranslational translocation and by suppression of vacuolar targeting.Design of optimally constructed metabolic networks of minimal functionality.Pichia pastoris regulates its gene-specific response to different carbon sources at the transcriptional, rather than the translational, level.Integration and Validation of the Genome-Scale Metabolic Models of Pichia pastoris: A Comprehensive Update of Protein Glycosylation Pathways, Lipid and Energy Metabolism Enhanced secretion of a methyl parathion hydrolase in Pichia pastoris using a combinational strategy.Chlamydomonas carries out fatty acid β-oxidation in ancestral peroxisomes using a bona fide acyl-CoA oxidase.Dynamic genome-scale metabolic modeling of the yeast Pichia pastoris Increasing pentose phosphate pathway flux enhances recombinant protein production in Pichia pastoris.Pichia pastoris Exhibits High Viability and a Low Maintenance Energy Requirement at Near-Zero Specific Growth Rates.Functional inclusion bodies produced in the yeast Pichia pastoris.Methanol-Independent Protein Expression by AOX1 Promoter with trans-Acting Elements Engineering and Glucose-Glycerol-Shift Induction in Pichia pastoris.Gene and protein sequence optimization for high-level production of fully active and aglycosylated lysostaphin in Pichia pastoris.New opportunities by synthetic biology for biopharmaceutical production in Pichia pastoris.Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production.Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a/GNA in Pichia pastoris: sequence modifications and a simple method for the generation of multi-copy strains.Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris.ATP regulation in bioproduction.Recent advances in the production of recombinant subunit vaccines in Pichia pastoris.Non-conventional expression systems for the production of vaccine proteins and immunotherapeutic molecules.Comprehensive clone screening and evaluation of fed-batch strategies in a microbioreactor and lab scale stirred tank bioreactor system: application on Pichia pastoris producing Rhizopus oryzae lipase Overexpressing target helper genes enhances secretion and glycosylation of recombinant proteins in Pichia pastoris under simulated microgravity.Integration event induced changes in recombinant protein productivity in Pichia pastoris discovered by whole genome sequencing and derived vector optimization.Molecular optimization of rabies virus glycoprotein expression in Pichia pastoris.Investigating the effect of carbon source on rabies virus glycoprotein production in Pichia pastoris by a transcriptomic approach.Methanol regulated yeast promoters: production vehicles and toolbox for synthetic biology.Restriction site free cloning (RSFC) plasmid family for seamless, sequence independent cloning in Pichia pastoris Non-canonical integration events in Pichia pastoris encountered during standard transformation analysed with genome sequencing.Multicopy plasmid integration in Komagataella phaffii mediated by a defective auxotrophic marker.Pichia pastoris Aft1--a novel transcription factor, enhancing recombinant protein secretion.Metabolic profiling of amino acids in cellular samples via zwitterionic sub-2 μm particle size HILIC-MS/MS and a uniformly 13C labeled internal standard.Creation of stable heterothallic strains of Komagataella phaffii enables dissection of mating gene regulation.Enhanced cell-surface display and secretory production of cellulolytic enzymes with Saccharomyces cerevisiae Sed1 signal peptide.Fine-tuning the P. pastoris iMT1026 genome-scale metabolic model for improved prediction of growth on methanol or glycerol as sole carbon sources.

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P2860

Pichia pastoris: protein production host and model organism for biomedical research.

http://www.wikidata.org/entity/Q38078461

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Pichia pastoris: protein production host and model organism for biomedical research.

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Pichia pastoris: protein production host and model organism for biomedical research.

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Pichia pastoris: protein production host and model organism for biomedical research.

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Future Microbiology

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Pichia pastoris: protein production host and model organism for biomedical research.

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Brigitte Gasser

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Diethard Mattanovich

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Hans Marx

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Justyna Nocon

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Matthias Steiger

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Michael Maurer

http://www.w3.org/2001/XMLSchema#string

Michael Sauer

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Roland Prielhofer

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Verena Puxbaum

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P2860

The HAC1 gene from Pichia pastoris: characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins

One step at a time: endoplasmic reticulum-associated degradation

Differential gene expression in recombinant Pichia pastoris analysed by heterologous DNA microarray hybridisation

Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae.

Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion

Ku70-deficient embryonic stem cells have increased ionizing radiosensitivity, defective DNA end-binding activity, and inability to support V(D)J recombination

Sec12 binds to Sec16 at transitional ER sites

Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology

Systematic single-cell analysis of Pichia pastoris reveals secretory capacity limits productivity

High-throughput protein expression using a combination of ligation-independent cloning (LIC) and infrared fluorescent protein (IFP) detection

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191-208

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scholarly article

P356

10.2217/FMB.12.133

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2

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P478

8

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P577

2013-02-01T00:00:00Z

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P698

23374125

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