Page last updated: 2024-08-26

thallium and asparagine

thallium 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	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
Jorgensen, PL; Nielsen, JM; Pedersen, PA; Rasmussen, JH	1
Eisenberg, D; Gill, HS	1

Other Studies

2 other study(ies) available for thallium and asparagine

Article	Year
Contribution to Tl+, K+, and Na+ binding of Asn776, Ser775, Thr774, Thr772, and Tyr771 in cytoplasmic part of fifth transmembrane segment in alpha-subunit of renal Na,K-ATPase. Biochemistry, 1998, Dec-22, Volume: 37, Issue:51 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Asparagine; Binding Sites; Cytoplasm; Hydroxides; Kidney; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Potassium; Protein Structure, Tertiary; Recombinant Proteins; Serine; Sodium; Sodium-Potassium-Exchanging ATPase; Swine; Thallium; Threonine; Tyrosine	1998
The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Biochemistry, 2001, Feb-20, Volume: 40, Issue:7 Topics: Aminobutyrates; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Computer Simulation; Crystallography, X-Ray; Electrons; Enzyme Inhibitors; Glutamate-Ammonia Ligase; Glutamic Acid; Models, Molecular; Salmonella typhimurium; Spectroscopy, Fourier Transform Infrared; Static Electricity; Substrate Specificity; Thallium; Tyrosine	2001

Article

Year

Contribution to Tl+, K+, and Na+ binding of Asn776, Ser775, Thr774, Thr772, and Tyr771 in cytoplasmic part of fifth transmembrane segment in alpha-subunit of renal Na,K-ATPase.

Biochemistry, 1998, Dec-22, Volume: 37, Issue:51

Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Asparagine; Binding Sites; Cytoplasm; Hydroxides; Kidney; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Potassium; Protein Structure, Tertiary; Recombinant Proteins; Serine; Sodium; Sodium-Potassium-Exchanging ATPase; Swine; Thallium; Threonine; Tyrosine

1998

The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.

Biochemistry, 2001, Feb-20, Volume: 40, Issue:7

Topics: Aminobutyrates; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Computer Simulation; Crystallography, X-Ray; Electrons; Enzyme Inhibitors; Glutamate-Ammonia Ligase; Glutamic Acid; Models, Molecular; Salmonella typhimurium; Spectroscopy, Fourier Transform Infrared; Static Electricity; Substrate Specificity; Thallium; Tyrosine

2001