Compounds > dodecyl-beta-d-maltoside
Page last updated: 2024-09-02

dodecyl-beta-d-maltoside and guanidine

dodecyl-beta-d-maltoside has been researched along with guanidine in 8 studies

Compound Research Comparison

Studies
(dodecyl-beta-d-maltoside)		Trials
(dodecyl-beta-d-maltoside)		Recent Studies (post-2010)
(dodecyl-beta-d-maltoside)		Studies
(guanidine)		Trials
(guanidine)		Recent Studies (post-2010) (guanidine)
31901045,55541,308

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19904 (50.00)18.7374
1990's0 (0.00)18.2507
2000's2 (25.00)29.6817
2010's2 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Horowitz, P; Tandon, S2
Criscimagna, NL; Horowitz, P1
Horowitz, PM; Tandon, S1
Lonzer, WL; Nagy, JK; Sanders, CR1
Alkorta, I; Arrondo, JL; de la Cruz, F; Goñi, FM; Hormaeche, I; Iloro, I1
Bishop, RE; Khan, MA; Moktar, J; Mott, PJ1
Hansted, JG; Nielsen, SB; Otzen, DE; Pedersen, LR; Petersen, TE; Sørensen, ES1

Other Studies

8 other study(ies) available for dodecyl-beta-d-maltoside and guanidine

ArticleYear
The effects of lauryl maltoside on the reactivation of several enzymes after treatment with guanidinium chloride.
    Biochimica et biophysica acta, 1988, Jun-29, Volume: 955, Issue:1

    Topics: Enzyme Inhibitors; Enzymes; Glucosides; Glycosides; Guanidine; Guanidines; Kinetics; Protein Denaturation

1988
Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.
    The Journal of biological chemistry, 1986, Nov-25, Volume: 261, Issue:33

    Topics: Dose-Response Relationship, Drug; Enzyme Activation; Enzyme Reactivators; Glucosides; Glycosides; Guanidine; Guanidines; Kinetics; Protein Conformation; Protein Denaturation; Sulfurtransferases; Thiosulfate Sulfurtransferase

1986
Low concentrations of guanidinium chloride expose apolar surfaces and cause differential perturbation in catalytic intermediates of rhodanese.
    The Journal of biological chemistry, 1986, Nov-25, Volume: 261, Issue:33

    Topics: Anilino Naphthalenesulfonates; Animals; Binding Sites; Cattle; Circular Dichroism; Fluorescent Dyes; Glucosides; Guanidine; Guanidines; Macromolecular Substances; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Sulfur; Sulfurtransferases; Thiosulfate Sulfurtransferase

1986
Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent.
    The Journal of biological chemistry, 1987, Apr-05, Volume: 262, Issue:10

    Topics: Detergents; Enzyme Reactivators; Glucosides; Guanidine; Guanidines; In Vitro Techniques; Micelles; Protein Denaturation; Sulfurtransferases; Surface-Active Agents; Thiosulfate Sulfurtransferase

1987
Kinetic study of folding and misfolding of diacylglycerol kinase in model membranes.
    Biochemistry, 2001, Jul-31, Volume: 40, Issue:30

    Topics: Amino Acid Sequence; Detergents; Diacylglycerol Kinase; Escherichia coli; Glucosides; Guanidine; Kinetics; Lipid Bilayers; Micelles; Models, Chemical; Molecular Sequence Data; Phosphatidylcholines; Protein Denaturation; Protein Folding; Reproducibility of Results; Solutions; Ultracentrifugation; Urea

2001
Role of the transmembrane domain in the stability of TrwB, an integral protein involved in bacterial conjugation.
    The Journal of biological chemistry, 2004, Mar-19, Volume: 279, Issue:12

    Topics: Base Sequence; Conjugation, Genetic; DNA Primers; DNA-Binding Proteins; Escherichia coli Proteins; Glucosides; Guanidine; Protein Denaturation; Protein Structure, Secondary; Spectrometry, Fluorescence

2004
A thiolate anion buried within the hydrocarbon ruler perturbs PagP lipid acyl chain selection.
    Biochemistry, 2010, Mar-23, Volume: 49, Issue:11

    Topics: Acyltransferases; Detergents; Enzyme Stability; Escherichia coli; Escherichia coli Proteins; Glucosides; Guanidine; Hydrocarbons; Hydrogen-Ion Concentration; Lipid Metabolism; Lipids; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Denaturation; Protein Engineering; Protein Folding; Protons; Solvents; Static Electricity; Substrate Specificity; Sulfhydryl Compounds; Temperature

2010
PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation.
    The FEBS journal, 2012, Volume: 279, Issue:2

    Topics: Animals; Anisotropy; Caseins; Cattle; Circular Dichroism; Dimerization; Fluorescence Polarization; Fractionation, Field Flow; Glucosides; Glycoproteins; Guanidine; Hot Temperature; Hydrogen-Ion Concentration; Milk Proteins; Molecular Weight; Oleic Acid; Peptide Fragments; Protein Denaturation; Protein Interaction Domains and Motifs; Protein Refolding; Surface-Active Agents

2012