cysteine and sodium arsenite

cysteine has been researched along with sodium arsenite in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's1 (14.29)29.6817
2010's4 (57.14)24.3611
2020's1 (14.29)2.80

Authors

AuthorsStudies
Bhattacharjee, H; Ksenzenko, MY; Li, J; Rosen, BP1
Bhattacharjee, H; Rosen, BP; Ruan, X1
Goto, Y; Hossain, K; Iida, M; Kato, M; Kumasaka, MY; Ohgami, N; Takeda, K; Yajima, I1
Chang, YY; Hou, DR; Hsu, CH; Huang, RN; Kao, YH; Kuo, TC1
Kurooka, H; Mori, K; Sugai, M; Yokota, Y1
Burchiel, SW; Cooper, KL; Hudson, LG; Huestis, J; Liu, KJ; Xu, H; Zhou, X1
Himeno, S; Ogawa, M; Okamoto, Y; Sumi, D; Suzukawa, K1

Other Studies

7 other study(ies) available for cysteine and sodium arsenite

ArticleYear
Role of cysteinyl residues in metalloactivation of the oxyanion-translocating ArsA ATPase.
    The Journal of biological chemistry, 1995, May-12, Volume: 270, Issue:19

    Topics: Adenosine Triphosphatases; Amino Acid Sequence; Antimony; Arsenite Transporting ATPases; Arsenites; Base Sequence; Cysteine; Enzyme Activation; Escherichia coli; Ion Pumps; Kinetics; Macromolecular Substances; Membrane Proteins; Models, Structural; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Point Mutation; Protein Conformation; Recombinant Proteins; Sodium Compounds

1995
Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase.
    The Journal of biological chemistry, 2006, Apr-14, Volume: 281, Issue:15

    Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Antimony Potassium Tartrate; Arsenites; Binding Sites; Catalysis; Catalytic Domain; Codon; Cysteine; Dose-Response Relationship, Drug; Escherichia coli; Escherichia coli Proteins; Hydrolysis; Ion Pumps; Magnesium; Models, Chemical; Models, Molecular; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Nucleotides; Oligonucleotides; Plasmids; Protein Binding; Protein Conformation; Sodium Compounds; Time Factors; Trypsin

2006
L-cysteine as a regulator for arsenic-mediated cancer-promoting and anti-cancer effects.
    Toxicology in vitro : an international journal published in association with BIBRA, 2011, Volume: 25, Issue:3

    Topics: Animals; Anticarcinogenic Agents; Arsenites; Carcinogens, Environmental; Cell Survival; Cysteine; Drug Interactions; Enzyme Inhibitors; Matrix Metalloproteinase 2; Mice; Multiple Endocrine Neoplasia Type 2a; NIH 3T3 Cells; Poly(ADP-ribose) Polymerases; Sodium Compounds; Transfection

2011
Characterization of the role of protein-cysteine residues in the binding with sodium arsenite.
    Archives of toxicology, 2012, Volume: 86, Issue:6

    Topics: Animals; Arsenic; Arsenites; Calcium-Binding Proteins; Carrier Proteins; Cell Line; Cricetinae; Cricetulus; Cysteine; Female; Heat-Shock Proteins; Ovary; Protein Binding; Sodium Compounds

2012
The metalloid arsenite induces nuclear export of Id3 possibly via binding to the N-terminal cysteine residues.
    Biochemical and biophysical research communications, 2013, Apr-19, Volume: 433, Issue:4

    Topics: Active Transport, Cell Nucleus; Amino Acid Sequence; Animals; Arsenites; Cell Nucleus; Cysteine; Cytoplasm; Exportin 1 Protein; Green Fluorescent Proteins; HEK293 Cells; Humans; Inhibitor of Differentiation Proteins; Karyopherins; MAP Kinase Signaling System; Mice; NIH 3T3 Cells; Nuclear Export Signals; Protein Binding; Receptors, Cytoplasmic and Nuclear; Recombinant Fusion Proteins; Repressor Proteins; Sodium Compounds; Transcription, Genetic; Transfection

2013
S-nitrosation on zinc finger motif of PARP-1 as a mechanism of DNA repair inhibition by arsenite.
    Oncotarget, 2016, Dec-06, Volume: 7, Issue:49

    Topics: Arsenites; Cell Line; Cell Transformation, Neoplastic; Cysteine; DNA Damage; DNA Repair; Free Radical Scavengers; Humans; Keratinocytes; Nitric Oxide; Nitric Oxide Synthase Type II; Nitrosation; Poly (ADP-Ribose) Polymerase-1; Poly(ADP-ribose) Polymerase Inhibitors; Protein Processing, Post-Translational; Sodium Compounds; Time Factors; Ultraviolet Rays; Zinc; Zinc Fingers

2016
Arsenite suppresses the transcriptional activity of EVI1 through the binding to CCHC-type Zn finger domain.
    Biochemical and biophysical research communications, 2020, 09-03, Volume: 529, Issue:4

    Topics: Alanine; Amino Acid Substitution; Arsenites; Binding Sites; Cell Nucleus; Complex Mixtures; Cysteine; Dithiothreitol; Electrophoretic Mobility Shift Assay; GATA2 Transcription Factor; Gene Expression Regulation; Humans; K562 Cells; MDS1 and EVI1 Complex Locus Protein; Peptides; Protein Binding; Recombinant Proteins; Signal Transduction; Sodium Compounds; Zinc Fingers

2020