Page last updated: 2024-09-05

4-nitrocatechol sulfate and glycine

4-nitrocatechol sulfate has been researched along with glycine in 2 studies

Compound Research Comparison

Studies
(4-nitrocatechol sulfate)
Trials
(4-nitrocatechol sulfate)
Recent Studies (post-2010)
(4-nitrocatechol sulfate)
Studies
(glycine)
Trials
(glycine)
Recent Studies (post-2010) (glycine)
260435,1637568,415

Protein Interaction Comparison

ProteinTaxonomy4-nitrocatechol sulfate (IC50)glycine (IC50)
Glutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)1.4852
Sodium- and chloride-dependent glycine transporter 1Homo sapiens (human)106
Glutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)0.3253
Glutamate receptor ionotropic, NMDA 2BRattus norvegicus (Norway rat)0.3253
Glutamate receptor ionotropic, NMDA 2CRattus norvegicus (Norway rat)0.3253
Glutamate receptor ionotropic, NMDA 2DRattus norvegicus (Norway rat)0.3253
Glutamate receptor ionotropic, NMDA 3BRattus norvegicus (Norway rat)0.3253
Glutamate receptor ionotropic, NMDA 3ARattus norvegicus (Norway rat)0.3253
Sodium- and chloride-dependent glycine transporter 2Homo sapiens (human)128

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (50.00)18.2507
2000's1 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dierks, T; Recksiek, M; Schmidt, B; Selmer, T; von Figura, K1
Dierks, T; Schmidt, B; Usón, I; von Bülow, R; von Figura, K1

Other Studies

2 other study(ies) available for 4-nitrocatechol sulfate and glycine

ArticleYear
Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine.
    The Journal of biological chemistry, 1998, Mar-13, Volume: 273, Issue:11

    Topics: Alanine; Alkaline Phosphatase; Binding Sites; Catechols; Cerebroside-Sulfatase; Chondro-4-Sulfatase; Galactose; Glycine; Humans; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Serine; Sulfuric Acid Esters

1998
Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis.
    Journal of molecular biology, 2001, Jan-12, Volume: 305, Issue:2

    Topics: Alanine; Binding Sites; Catalysis; Catechols; Cations, Divalent; Cerebroside-Sulfatase; Crystallography, X-Ray; Glycine; Humans; Hydrogen Bonding; Models, Molecular; Mutation; Protein Conformation

2001