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Volumn 15, Issue 3, 2002, Pages 243-249
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A recombinant bacterial cell surface (S-layer)-major birch pollen allergen-fusion protein (rSbsC/Bet v1) maintains the ability to self-assemble into regularly structured monomolecular lattices and the functionality of the allergen
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Author keywords
Bacillus stearothermophilus; Major birch pollen allergen; Recombinant fusion protein; S layer protein
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Indexed keywords
ALLERGEN;
AMINO ACID;
BACTERIAL PROTEIN;
HYBRID PROTEIN;
IMMUNOGLOBULIN E;
MONOCLONAL ANTIBODY;
PROTEIN SBSC;
UNCLASSIFIED DRUG;
BET V 1 PROTEINS, BETULA PENDULA;
MEMBRANE PROTEIN;
SURFACE ARRAY PROTEIN, BACTERIA;
VEGETABLE PROTEIN;
AMINO ACID SEQUENCE;
ARTICLE;
BACTERIAL CELL;
BACTERIAL GROWTH;
CELL SURFACE;
CRYSTALLIZATION;
GENE EXPRESSION;
GEOBACILLUS STEAROTHERMOPHILUS;
MOLECULAR CLONING;
NONHUMAN;
POLLEN;
PRIORITY JOURNAL;
PROTEIN ASSEMBLY;
PROTEIN FUNCTION;
PROTEIN STRUCTURE;
SEQUENCE ANALYSIS;
CHEMISTRY;
GENETICS;
IMMUNOBLOTTING;
IMMUNOLOGY;
PROTEIN ENGINEERING;
BACTERIA (MICROORGANISMS);
GEOBACILLUS STEAROTHERMOPHILUS;
ALLERGENS;
BACILLUS STEAROTHERMOPHILUS;
BACTERIAL PROTEINS;
CRYSTALLIZATION;
IMMUNOBLOTTING;
IMMUNOGLOBULIN E;
MEMBRANE GLYCOPROTEINS;
PLANT PROTEINS;
PROTEIN ENGINEERING;
RECOMBINANT FUSION PROTEINS;
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EID: 0036224750
PISSN: 02692139
EISSN: None
Source Type: Journal
DOI: 10.1093/protein/15.3.243 Document Type: Article |
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Times cited : (50)
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References (36)
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