Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state.
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Design Rationale and Development Approach for Pegfilgrastim as a Long-Acting Granulocyte Colony-Stimulating FactorNon-native aggregation of recombinant human granulocyte-colony stimulating factor under simulated process stress conditions.Improved drug-like properties of therapeutic proteins by directed evolution.Fully Synthetic Granulocyte Colony-Stimulating Factor Enabled by Isonitrile-Mediated Coupling of Large, Side-Chain-Unprotected PeptidesEGCG induces G-CSF expression and neutrophilia in experimental sepsisDetection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches.Effects of glycosylation on the stability of protein pharmaceuticals.Oxidation of therapeutic proteins and peptides: structural and biological consequences.Biochemical and biophysical characterization of cytokine-like protein 1 (CYTL1).Nonspecific shielding of unfavorable electrostatic intramolecular interactions in the erythropoietin native-state increase conformational stability and limit non-native aggregation.Engineering a therapeutic IgG molecule to address cysteinylation, aggregation and enhance thermal stability and expression.The feeding tube of cyst nematodes: characterisation of protein exclusion.Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study.Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.Chromatography process development in the quality by design paradigm I: Establishing a high-throughput process development platform as a tool for estimating "characterization space" for an ion exchange chromatography step.Freeze drying formulation using microscale and design of experiment approaches: a case study using granulocyte colony-stimulating factor.Characterization of disulfide linkages in recombinant human granulocyte-colony stimulating factor.Transient co-expression with three -glycosylation enzymes allows production of GalNAc--glycosylated Granulocyte-Colony Stimulating Factor in
P2860
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P2860
Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state.
description
2005 nî lūn-bûn
@nan
2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
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2005年學術文章
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2005年學術文章
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name
Aggregation of granulocyte-col ...... nally altered monomeric state.
@ast
Aggregation of granulocyte-col ...... nally altered monomeric state.
@en
type
label
Aggregation of granulocyte-col ...... nally altered monomeric state.
@ast
Aggregation of granulocyte-col ...... nally altered monomeric state.
@en
prefLabel
Aggregation of granulocyte-col ...... nally altered monomeric state.
@ast
Aggregation of granulocyte-col ...... nally altered monomeric state.
@en
P2093
P2860
P356
P1433
P1476
Aggregation of granulocyte-col ...... nally altered monomeric state.
@en
P2093
David N Brems
Gary Pipes
Jesse M Barnes
Jonathan King
Kevin M Maloney
Michael J Treuheit
Stephen W Raso
P2860
P304
P356
10.1110/PS.051489405
P577
2005-09-01T00:00:00Z