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dithiobis(succinimidylpropionate) and cysteine

dithiobis(succinimidylpropionate) has been researched along with cysteine in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (66.67)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Arselin, G; Bathany, K; Brèthes, D; Chaignepain, S; Dautant, A; Fronzes, R; Giraud, MF; Schmitter, JM; Velours, J1
Alexander, ET; Bhat, S; Samuel, MP; Sorci-Thomas, MG; Thomas, MJ1
Bowie, JH; Calabrese, AN; Pukala, TL; Wang, T1

Other Studies

3 other study(ies) available for dithiobis(succinimidylpropionate) and cysteine

ArticleYear
Topological and functional study of subunit h of the F1Fo ATP synthase complex in yeast Saccharomyces cerevisiae.
    Biochemistry, 2003, Oct-21, Volume: 42, Issue:41

    Topics: Amino Acid Sequence; Amino Acid Substitution; Cross-Linking Reagents; Cysteine; Enzyme Activation; Intracellular Membranes; Lysine; Maleimides; Mitochondria; Mitochondrial Proton-Translocating ATPases; Molecular Sequence Data; Peptide Fragments; Protein Processing, Post-Translational; Protein Subunits; Saccharomyces cerevisiae Proteins; Sodium-Potassium-Exchanging ATPase; Succinimides; Vacuolar Proton-Translocating ATPases

2003
Intermolecular contact between globular N-terminal fold and C-terminal domain of ApoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry.
    The Journal of biological chemistry, 2005, Sep-23, Volume: 280, Issue:38

    Topics: Amino Acid Sequence; Apolipoprotein A-I; Chromatography, Liquid; Cross-Linking Reagents; Cysteine; Dimerization; Electrophoresis, Polyacrylamide Gel; Glycerylphosphorylcholine; Lipids; Lysine; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Mutation; Oligonucleotides; Peptides; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Spectrometry, Mass, Electrospray Ionization; Succinimides; Trypsin; Urea

2005
Negative ion fragmentations of disulfide-containing cross-linking reagents are competitive with aspartic acid side-chain-induced cleavages.
    Rapid communications in mass spectrometry : RCM, 2013, Jan-15, Volume: 27, Issue:1

    Topics: Acetates; Anions; Aspartic Acid; Cross-Linking Reagents; Cysteine; Disulfides; Peptides; Succinimides; Tandem Mass Spectrometry; Thermodynamics

2013