n,n'-4-phenylenedimaleimide has been researched along with cysteine in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 8 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Highsmith, S; Kirshenbaum, K; Papp, S | 1 |
| Highsmith, S; Polosukhina, K | 1 |
| Hardy, D; Kaback, HR; Wu, J | 3 |
| Nitao, LK; Reisler, E | 1 |
| Goto, S; Hashimoto, M; Majima, E; Shinohara, Y; Terada, H | 1 |
| Kaback, HR; Wang, Q | 1 |
8 other study(ies) available for n,n'-4-phenylenedimaleimide and cysteine
| Article | Year |
|---|---|
Cross-linking myosin subfragment 1 Cys-697 and Cys-707 modifies ATP and actin binding site interactions.
Topics: Actins; Adenosine Triphosphate; Allosteric Site; Animals; Biophysical Phenomena; Biophysics; Cross-Linking Reagents; Cysteine; Fluorescence Polarization; In Vitro Techniques; Kinetics; Maleimides; Molecular Structure; Myosin Subfragments; Rabbits; Thermodynamics | 1993 |
Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivities.
Topics: Actins; Adenosine Diphosphate; Animals; Cross-Linking Reagents; Cysteine; Kinetics; Ligands; Maleimides; Muscle, Skeletal; Myosin Subfragments; Protein Conformation; Rabbits | 1997 |
Transmembrane helix tilting and ligand-induced conformational changes in the lactose permease determined by site-directed chemical crosslinking in situ.
Topics: Cross-Linking Reagents; Cysteine; Escherichia coli Proteins; Maleimides; Membrane Transport Proteins; Models, Molecular; Monosaccharide Transport Proteins; Protein Conformation; Recombinant Proteins; Symporters | 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 |
Probing the conformational states of the SH1-SH2 helix in myosin: a cross-linking approach.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Cross-Linking Reagents; Cysteine; Kinetics; Maleimides; Myosin Subfragments; Protein Conformation; Protein Structure, Secondary; Psoas Muscles; Rabbits; Sulfhydryl Compounds | 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 |
Site-directed chemical cross-linking demonstrates that helix IV is close to helices VII and XI in the lactose permease.
Topics: Amino Acid Sequence; Cross-Linking Reagents; Cysteine; Escherichia coli; Escherichia coli Proteins; Ligands; Maleimides; Membrane Transport Proteins; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Symporters | 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 |