1,6-bismaleimidohexane has been researched along with cysteine in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 8 (72.73) | 18.2507 |
| 2000's | 3 (27.27) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Neer, EJ; Schmidt, CJ; Thomas, TC | 1 |
| Neer, EJ; Sladek, T; Smith, T; Thomas, TC; Yi, F | 1 |
| Jarrett, HW; Kosk-Kosicka, D; Krinks, MH; Lee, HG; Persechini, A | 1 |
| Kaback, HR; Kemp, CR; Sun, J | 1 |
| Brunner-Neuenschwander, B; Levings, CS; Rhoads, DM; Siedow, JN | 1 |
| Hardy, D; Kaback, HR; Wu, J | 1 |
| Goto, S; Hashimoto, M; Majima, E; Shinohara, Y; Terada, H | 1 |
| Kaback, HR; Wang, Q | 1 |
| Bernier, M; Garant, MJ; Kole, S; Lee-Kwon, W; Maksimova, E; Montrose-Rafizadeh, C | 1 |
| Emi, Y; Ikushiro, S; Iyanagi, T | 1 |
| Arselin, G; Bathany, K; Brèthes, D; Chaignepain, S; Dautant, A; Fronzes, R; Giraud, MF; Schmitter, JM; Velours, J | 1 |
11 other study(ies) available for 1,6-bismaleimidohexane and cysteine
| Article | Year |
|---|---|
G-protein alpha o subunit: mutation of conserved cysteines identifies a subunit contact surface and alters GDP affinity.
Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Conserved Sequence; Cross-Linking Reagents; Cysteine; DNA Primers; Drosophila; GTP-Binding Proteins; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Macromolecular Substances; Maleimides; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Protein Structure, Secondary | 1993 |
G protein beta gamma subunit: physical and chemical characterization.
Topics: Carbon Radioisotopes; Cross-Linking Reagents; Cysteine; GTP-Binding Proteins; Hot Temperature; Iodoacetamide; Kinetics; Macromolecular Substances; Maleimides; Molecular Weight; NAD; Peptide Fragments; Phosphorus Radioisotopes; Protein Denaturation; Thermodynamics; Trypsin; Virulence Factors, Bordetella | 1993 |
Activation of enzymes by calmodulins containing intramolecular cross-links.
Topics: Brain; Calcineurin; Calcium-Transporting ATPases; Calmodulin; Calmodulin-Binding Proteins; Cross-Linking Reagents; Cysteine; Enzyme Activation; Maleimides; Phosphoprotein Phosphatases; Phosphotransferases; Phosphotransferases (Alcohol Group Acceptor); Plants | 1993 |
Ligand-induced changes in periplasmic loops in the lactose permease of Escherichia coli.
Topics: Amino Acid Substitution; Biological Transport; Cross-Linking Reagents; Cysteine; Escherichia coli; Escherichia coli Proteins; Genetic Complementation Test; Ligands; Maleimides; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Secondary; Symporters; Thiogalactosides | 1998 |
Cross-linking and disulfide bond formation of introduced cysteine residues suggest a modified model for the tertiary structure of URF13 in the pore-forming oligomers.
Topics: Amino Acid Sequence; Cross-Linking Reagents; Cysteine; Diamide; Dicyclohexylcarbodiimide; Disulfides; Maleimides; Mitochondrial Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Plant Proteins; Protein Structure, Tertiary; Sulfhydryl Compounds; Threonine; Zea mays | 1998 |
Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situ.
Topics: Cross-Linking Reagents; Cysteine; Escherichia coli Proteins; Ligands; Maleimides; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Sulfhydryl Compounds; Symporters; Thiogalactosides | 1998 |
Fluctuation of the first loop facing the matrix of the mitochondrial ADP/ATP carrier deduced from intermolecular cross-linking of Cys56 residues by bifunctional dimaleimides.
Topics: Adenosine Diphosphate; Animals; Biological Transport; Cattle; Cross-Linking Reagents; Cysteine; Ethylmaleimide; Glutathione; Maleimides; Mitochondria, Heart; Mitochondrial ADP, ATP Translocases; Protein Conformation; Solutions; Submitochondrial Particles | 1999 |
Proximity relationships between helices I and XI or XII in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking.
Topics: Biological Transport, Active; Cross-Linking Reagents; Cysteine; Escherichia coli; Escherichia coli Proteins; Lactose; Maleimides; Membrane Transport Proteins; Models, Molecular; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Sulfhydryl Compounds; Symporters | 1999 |
Cysteine 981 of the human insulin receptor is required for covalent cross-linking between beta-subunit and a thiol-reactive membrane-associated protein.
Topics: 3T3 Cells; Animals; CHO Cells; Cricetinae; Cysteine; Humans; Intracellular Signaling Peptides and Proteins; Maleimides; Membrane Proteins; Mice; Mutation; Phosphorylation; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Protein Tyrosine Phosphatase, Non-Receptor Type 6; Protein Tyrosine Phosphatases; Receptor-Like Protein Tyrosine Phosphatases, Class 4; Receptor, Insulin; Receptors, Cell Surface; Sulfhydryl Compounds; Transfection | 2000 |
Activation of glucuronidation through reduction of a disulfide bond in rat UDP-glucuronosyltransferase 1A6.
Topics: Animals; Biotransformation; COS Cells; Cysteine; Disulfides; Dithiothreitol; Enzyme Inhibitors; Ethylmaleimide; Glucuronides; Glucuronosyltransferase; Isoenzymes; Male; Maleimides; Microsomes, Liver; Nitrophenols; Oxidation-Reduction; Rats; Rats, Gunn; Rats, Wistar; Reducing Agents | 2002 |
Topological and functional study of subunit h of the F1Fo ATP synthase complex in yeast Saccharomyces cerevisiae.
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 |