Crystal structure of a sweet tasting protein thaumatin I, at 1·65 Å resolution

Ogata, Craig M.; Gordon, P. F.; Vos, Abraham M. de; Kim, Sung‐Hou

doi:10.1016/0022-2836(92)90873-i

Cited by 113 publications

(56 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The predicted mass of the mature protein is 21,286.45 D, whereas that obtained by MS is 21,272.90 ± 1.88 D. The discrepancy of 16 D is accounted for by the formation of eight disulfide bonds, as seen in crystallized thaumatin (Ogata et al, 1992). Thus, we conclude not only that the cDNA sequence (Fig.…”

Section: Polypeptide Pattern Of Developing Grape Berriesmentioning

confidence: 70%

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

1997

View full text Add to dashboard Cite

Section: Polypeptide Pattern Of Developing Grape Berriesmentioning

confidence: 70%

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

1997

View full text Add to dashboard Cite

“…This highly stabilized structure allows PR-5 proteins to be very resistant to protease degradation (148). The X-ray structures have been determined for two PR-5 proteins and thaumatin (82,134).…”

Section: Fungal Cell Wall Structurementioning

confidence: 99%

Antifungal Proteins

Selitrennikoff

2001

Appl Environ Microbiol

529

362

View full text Add to dashboard Cite

“…No glycosylation has been reported from any TLP so far. The structure of thaumatin I has been determined by X-ray crystallography [52]. The locations of the cysteines are highly conserved between other high molecular weight members of the PR-5 family.…”

Section: Pr-5 – Thaumatin-like Proteins (Tlps)mentioning

confidence: 99%

Plant Allergens and Pathogenesis-Related Proteins

Hoffmann‐Sommergruber

2000

Int Arch Allergy Immunol

173

114

View full text Add to dashboard Cite

In the recent past a great number of proteins causing type 1 allergic reactions in humans have been isolated and characterised. The main sources containing allergens are plants, mites, fungal spores and insects. Plant-derived allergens may either be taken in from the upper respiratory tract or they are present in a vast range of plant food causing food allergic reactions. Compared to the enormous amount of different plant proteins only a small number out of them are identified as a an allergen at present. Looking at the allergen encoding sequences, relationships by sequence similarity can be found quite frequently to a restricted number of plant protein families. Predominantly, these protein families are seed storage proteins, structural proteins and proteins involved in the defence-related system – pathogenesis-related proteins. In the following, a short overview of a number of pathogenesis-related protein families is presented in relation to the already known homologous plant allergens.

show abstract

Crystal structure of a sweet tasting protein thaumatin I, at 1·65 Å resolution

Cited by 113 publications

References 51 publications

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

Antifungal Proteins

Plant Allergens and Pathogenesis-Related Proteins

Contact Info

Product

Resources

About