Page last updated: 2024-08-22

cupric chloride and arginine

cupric chloride has been researched along with arginine 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
Allison, WS; Bandyopadhyay, S	1
Allison, WS; Bandyopadhyay, S; Muneyuki, E	1

Other Studies

2 other study(ies) available for cupric chloride and arginine

Article	Year
The ionic track in the F1-ATPase from the thermophilic Bacillus PS3. Biochemistry, 2004, Mar-09, Volume: 43, Issue:9 Topics: Adenosine Diphosphate; Amino Acid Substitution; Arginine; Bacillus; Bacterial Proton-Translocating ATPases; Catalytic Domain; Copper; Cysteine; Enzyme Activation; Enzyme Inhibitors; Glutamic Acid; Lysine; Methylation; Mutagenesis, Site-Directed; Protein Subunits; Sodium-Potassium-Exchanging ATPase; Temperature	2004
The characteristics of the (alpha V371C)3(beta R337C)3 gamma double mutant subcomplex of the TF1-ATPase indicate that the catalytic site at the alpha TP-beta TP interface with bound MgADP in crystal structures of MF1 represents a catalytic site containing Biochemistry, 2005, Feb-22, Volume: 44, Issue:7 Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aluminum; Animals; Arginine; Bacillus; Catalytic Domain; Cattle; Copper; Cross-Linking Reagents; Crystallization; Cysteine; Enzyme Inhibitors; Fluorine; Hydrolysis; Mitochondria, Heart; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Subunits; Proton-Translocating ATPases; Surface Properties; Valine	2005

Article

Year

The ionic track in the F1-ATPase from the thermophilic Bacillus PS3.

Biochemistry, 2004, Mar-09, Volume: 43, Issue:9

Topics: Adenosine Diphosphate; Amino Acid Substitution; Arginine; Bacillus; Bacterial Proton-Translocating ATPases; Catalytic Domain; Copper; Cysteine; Enzyme Activation; Enzyme Inhibitors; Glutamic Acid; Lysine; Methylation; Mutagenesis, Site-Directed; Protein Subunits; Sodium-Potassium-Exchanging ATPase; Temperature

2004

The characteristics of the (alpha V371C)3(beta R337C)3 gamma double mutant subcomplex of the TF1-ATPase indicate that the catalytic site at the alpha TP-beta TP interface with bound MgADP in crystal structures of MF1 represents a catalytic site containing

Biochemistry, 2005, Feb-22, Volume: 44, Issue:7

Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aluminum; Animals; Arginine; Bacillus; Catalytic Domain; Cattle; Copper; Cross-Linking Reagents; Crystallization; Cysteine; Enzyme Inhibitors; Fluorine; Hydrolysis; Mitochondria, Heart; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Subunits; Proton-Translocating ATPases; Surface Properties; Valine

2005