(Q46447820)

English

Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride

scientific article published in March 2005

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride (English)

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

0 references

alpha,alpha-trehalose

1 reference

based on heuristic

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author name string

Elena Ganea

1

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

John J Harding

2

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

publication date

1 March 2005

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

386

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

3

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

269-278

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

Stabilization of protein structure by sugars

1 reference

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Inhibition of insulin amyloid formation by small stress molecules

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Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis

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A ligand-induced conformational change in apolipoprotein(a) enhances covalent Lp(a) formation.

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Prevention of the fructation-induced inactivation of glutathione reductase by bovine alpha-crystallin acting as a molecular chaperone

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Bovine and human alpha-crystallins as molecular chaperones: prevention of the inactivation of glutathione reductase by fructation.

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The osmophobic effect: natural selection of a thermodynamic force in protein folding

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Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency

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Osmolyte effects on helix formation in peptides and the stability of coiled-coils

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Therapeutic approaches to protein-misfolding diseases

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An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme

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The molecular chaperone alpha-crystallin incorporated into red cell ghosts protects membrane Na/K-ATPase against glycation and oxidative stress

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Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses

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Dicarboxylic amino acids and glycine-betaine regulate chaperone-mediated protein-disaggregation under stress.

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High osmolarity glycerol (HOG) pathway-induced phosphorylation and activation of 6-phosphofructo-2-kinase are essential for glycerol accumulation and yeast cell proliferation under hyperosmotic stress

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Molecular chaperones: inside and outside the Anfinsen cage

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Macromolecular crowding: obvious but underappreciated

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Early events in protein folding

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Role of epsilon amino caproic acid in the management of haemophilic patients with inhibitors

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Molecular chaperones in the cytosol: from nascent chain to folded protein

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Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose

1 reference

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Chemical chaperones--a new concept in drug research

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Regulation of the cellular content of the organic osmolyte taurine in mammalian cells

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Trehalose-protein interaction in aqueous solution

1 reference

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Trehalose favors a cutinase compact intermediate off-folding pathway

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Role of proline, glycerol, and heparin as protein folding aids during refolding of rabbit muscle creatine kinase

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Organic osmolytes betaine, sorbitol and inositol are potent inhibitors of erythrocyte membrane ATPases

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Molecular mechanism for osmolyte protection of creatine kinase against guanidine denaturation

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Effect of osmolytes as folding aids on creatine kinase refolding pathway

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Correct protein folding in glycerol

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Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation.

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Chemical chaperones increase the cellular activity of N370S beta -glucosidase: a therapeutic strategy for Gaucher disease

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Inhibition of yeast glutathione reductase by trehalose: possible implications in yeast survival and recovery from stress.

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Structural control of endoplasmic reticulum-associated degradation: effect of chemical chaperones on 3-hydroxy-3-methylglutaryl-CoA reductase

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Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: why is trehalose more effective than other sugars?

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Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease

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Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components

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Protein folding by the effects of macromolecular crowding

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Therapeutic potential of breakers of advanced glycation end product–protein crosslinks

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The thermodynamic mechanism of protein stabilization by trehalose

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Evidence of CFTR function in cystic fibrosis after systemic administration of 4-phenylbutyrate

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Identifiers

10.1515/BC.2005.032

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 December 2017

http://europepmc.org/abstract/MED/15843172

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