p-chloromercuribenzoic acid and manganese

p-chloromercuribenzoic acid has been researched along with manganese in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ishikawa, T; Mukohara, Y; Nakamura, H; Watabe, K	1
Fessner, WD; Korndörfer, IP; Matthews, BW	1

Other Studies

2 other study(ies) available for p-chloromercuribenzoic acid and manganese

Article	Year
N-carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: purification and some properties of the enzyme expressed in Escherichia coli. Bioscience, biotechnology, and biochemistry, 1996, Volume: 60, Issue:4 Topics: Adenosine Triphosphate; Amidohydrolases; Chloromercuribenzoates; Hydrogen-Ion Concentration; Manganese; Methionine; p-Chloromercuribenzoic Acid; Pseudomonas; Recombinant Proteins; Substrate Specificity; Temperature	1996
The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution. Journal of molecular biology, 2000, Jul-21, Volume: 300, Issue:4 Topics: Aldose-Ketose Isomerases; Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Evolution, Molecular; Genetic Complementation Test; Isomerism; Manganese; Mannitol; Models, Molecular; Molecular Sequence Data; p-Chloromercuribenzoic Acid; Protein Structure, Secondary; Rhamnose; Sequence Alignment; Zinc	2000

Article

Year

N-carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: purification and some properties of the enzyme expressed in Escherichia coli.

Bioscience, biotechnology, and biochemistry, 1996, Volume: 60, Issue:4

Topics: Adenosine Triphosphate; Amidohydrolases; Chloromercuribenzoates; Hydrogen-Ion Concentration; Manganese; Methionine; p-Chloromercuribenzoic Acid; Pseudomonas; Recombinant Proteins; Substrate Specificity; Temperature

1996

The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution.

Journal of molecular biology, 2000, Jul-21, Volume: 300, Issue:4

Topics: Aldose-Ketose Isomerases; Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Evolution, Molecular; Genetic Complementation Test; Isomerism; Manganese; Mannitol; Models, Molecular; Molecular Sequence Data; p-Chloromercuribenzoic Acid; Protein Structure, Secondary; Rhamnose; Sequence Alignment; Zinc

2000