Page last updated: 2024-09-04

phosphorus and bis(3',5')-cyclic diguanylic acid

phosphorus has been researched along with bis(3',5')-cyclic diguanylic acid in 2 studies

Compound Research Comparison

Studies (phosphorus)	Trials (phosphorus)	Recent Studies (post-2010) (phosphorus)	Studies (bis(3',5')-cyclic diguanylic acid)	Trials (bis(3',5')-cyclic diguanylic acid)	Recent Studies (post-2010) (bis(3',5')-cyclic diguanylic acid)
48,074	1,126	17,139	1,112	1	912

Protein Interaction Comparison

Protein	Taxonomy	phosphorus (IC50)	bis(3',5')-cyclic diguanylic acid (IC50)
RocR	Pseudomonas aeruginosa PAO1		0.02

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	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Barends, TR; Beitlich, T; Gomelsky, M; Griese, JJ; Hartmann, E; Kirienko, NV; Reinstein, J; Ryjenkov, DA; Schlichting, I; Shoeman, RL	1
Grigorenko, BL; Knyazeva, MA; Nemukhin, AV	1

Other Studies

2 other study(ies) available for phosphorus and bis(3',5')-cyclic diguanylic acid

Article	Year
Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase. Nature, 2009, Jun-18, Volume: 459, Issue:7249 Topics: 3',5'-Cyclic-GMP Phosphodiesterases; Allosteric Regulation; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Cyclic GMP; Klebsiella pneumoniae; Light; Metals; Models, Molecular; Phosphorus; Photons; Photoreceptors, Microbial; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary	2009
Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases. Proteins, 2016, Volume: 84, Issue:11 Topics: Amino Acid Substitution; Aspartic Acid; Catalytic Domain; Cyclic GMP; Escherichia coli; Escherichia coli Proteins; Gene Expression; Glutamic Acid; Hydrogen Bonding; Hydrolysis; Kinetics; Molecular Dynamics Simulation; Phosphoric Diester Hydrolases; Phosphorus; Protein Structure, Secondary; Protons; Quantum Theory; Structure-Activity Relationship; Thermodynamics; Water	2016

Article

Year

Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase.

Nature, 2009, Jun-18, Volume: 459, Issue:7249

Topics: 3',5'-Cyclic-GMP Phosphodiesterases; Allosteric Regulation; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Cyclic GMP; Klebsiella pneumoniae; Light; Metals; Models, Molecular; Phosphorus; Photons; Photoreceptors, Microbial; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary

2009

Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases.

Proteins, 2016, Volume: 84, Issue:11

Topics: Amino Acid Substitution; Aspartic Acid; Catalytic Domain; Cyclic GMP; Escherichia coli; Escherichia coli Proteins; Gene Expression; Glutamic Acid; Hydrogen Bonding; Hydrolysis; Kinetics; Molecular Dynamics Simulation; Phosphoric Diester Hydrolases; Phosphorus; Protein Structure, Secondary; Protons; Quantum Theory; Structure-Activity Relationship; Thermodynamics; Water

2016