Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities - Wikidata - wikimedia - TriplyDB

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

http://www.wikidata.org/entity/Q28278612

about

Curculin exhibits sweet-tasting and taste-modifying activities through its distinct molecular surfaces Structural Role of the Terminal Disulfide Bond in the Sweetness of Brazzein The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana Identification and modulation of the key amino acid residue responsible for the pH sensitivity of neoculin, a taste-modifying protein Genetically stable expression of functional miraculin, a new type of alternative sweetener, in transgenic tomato plants.Functional expression of miraculin, a taste-modifying protein in Escherichia coli.Identification of key neoculin residues responsible for the binding and activation of the sweet taste receptor Extracellular production of neoculin, a sweet-tasting heterodimeric protein with taste-modifying activity, by Aspergillus oryzae.pH-Dependent structural change in neoculin with special reference to its taste-modifying activity.Natural product modulators of human sensations and mood: molecular mechanisms and therapeutic potential.Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.An efficient in vitro plantlet regeneration from shoot tip cultures of Curculigo latifolia, a medicinal plant.

P2860

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P2860

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

http://www.wikidata.org/entity/Q28278612

description

2004 nî lūn-bûn

@nan

2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@ast

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@en

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@nl

type

label

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@ast

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@en

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@nl

prefLabel

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@ast

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@en

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@nl

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P2860

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P356

J.FEBSLET.2004.07.073

P1433

P1476

Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities

@en

P2093

Ei-Ichiro Suzuki

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

Eiji Kurimoto

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

Maiko Suzuki

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

Misako Kawai

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

Nobuhisa Shimba

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

Satoru Nirasawa

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

Yoshie Kurihara

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

Yutaka Masuda

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

P2860

Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin

Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. structural origin of sweetness

The mechanism of interaction of sweet proteins with the T1R2-T1R3 receptor: evidence from the solution structure of G16A-MNEI

Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution

Solution structure of the thermostable sweet-tasting protein brazzein

Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein

Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin

Activity and stability of a new sweet protein with taste-modifying action, curculin

Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe

Critical regions for the sweetness of brazzein.

P304

135-138

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P31

scholarly article

P356

10.1016/J.FEBSLET.2004.07.073

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P407

P433

1-3

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P478

573

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P50

P577

2004-08-01T00:00:00Z

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P5875

8384152

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P698

15327988

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