cysteine sulfinic acid and asparagine

cysteine sulfinic acid has been researched along with asparagine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Boehlein, SK; Hiratake, J; Nakatsu, T; Richards, NG; Schuster, SM; Stewart, JD; Thirumoorthy, R	1
Gruschus, JM; Jeong, W; Lee, DY; Oho, T; Park, SJ; Rhee, SG; Sung, HJ; Wu, X	1

Other Studies

2 other study(ies) available for cysteine sulfinic acid and asparagine

Article	Year
Characterization of inhibitors acting at the synthetase site of Escherichia coli asparagine synthetase B. Biochemistry, 2001, Sep-18, Volume: 40, Issue:37 Topics: Adenosine Monophosphate; Adenosine Triphosphate; Asparagine; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; Cysteine; Enzyme Inhibitors; Escherichia coli; Hydrolysis; Methionine Sulfoximine; Models, Chemical; Neurotransmitter Agents; Nuclear Magnetic Resonance, Biomolecular; Phosphorus Isotopes; Spectrometry, Mass, Electrospray Ionization	2001
Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis. Biochemistry, 2006, Dec-26, Volume: 45, Issue:51 Topics: Adenosine Triphosphate; Asparagine; Aspartic Acid; Catalysis; Crystallography, X-Ray; Cysteine; Humans; Hydrolysis; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Peroxiredoxins; Protein Structure, Tertiary	2006

Article

Year

Characterization of inhibitors acting at the synthetase site of Escherichia coli asparagine synthetase B.

Biochemistry, 2001, Sep-18, Volume: 40, Issue:37

Topics: Adenosine Monophosphate; Adenosine Triphosphate; Asparagine; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; Cysteine; Enzyme Inhibitors; Escherichia coli; Hydrolysis; Methionine Sulfoximine; Models, Chemical; Neurotransmitter Agents; Nuclear Magnetic Resonance, Biomolecular; Phosphorus Isotopes; Spectrometry, Mass, Electrospray Ionization

2001

Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis.

Biochemistry, 2006, Dec-26, Volume: 45, Issue:51

Topics: Adenosine Triphosphate; Asparagine; Aspartic Acid; Catalysis; Crystallography, X-Ray; Cysteine; Humans; Hydrolysis; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Peroxiredoxins; Protein Structure, Tertiary

2006