Skip to search formSkip to main contentSkip to account menu

Cypridina

National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Enzymatic Conversion of Cypridina Luciferyl Sulfate to Cypridina Luciferin with Coenzyme A as a Sulfate Acceptor in Cypridina (Vargula) hilgendorfii
In the luminous ostracod Cypridina (presently Vargula) hilgendorfii, Cypridina luciferyl sulfate (3‐enol sulfate of Cypridina… 
1998
1998
Changes in Purine Metabolism and Production of Oxygen Free Radicals by Intermittent Partial Umbilical Cord Occlusion in Chronically Instrumented Fetal Lambs
Objective: Undetected umbilical‐cord compression has been suggested to be implicated in unexplained fetal brain damage. We tested… 
1989
1989
Generation of O2- and tyrosine cation-mediated chemiluminescence during the fertilization of sea urchin eggs.
Sea urchin eggs emit light in the visible region during their fertilization. Judging from the chemiluminescence spectra, one of… 
1975
1975
Influence of buffer system and pH on the amount of oxygen exchanged between solvent H2O and the CO2 produced in the aerobic oxidation of Cypridina luciferin catalyzed by Cypridina luciferase.
Highly Cited
1971
Highly Cited
1971
Mechanism of the luminescent oxidation of cypridina luciferin.
1970
1970
[Synthesis of cypridina luciferin and related compounds. IV. Synthesis of 3,7-dihydroimidazo [1,2-a]pyrazin-3-ones].
1970
1970
[Synthesis of cypridina luciferin and related compounds. V. On the structure of imidazo[1,2-a]pyrazine derivatives].
1968
1968
Cypridina bioluminescence V. structure of emitting species in the luminescence of cypridina luciferin and its related compounds.
1960
1960
The sedimentation constant and molecular weight of Cypridina luciferase.
1946
1946
Reversible heat inactivation of Cypridina luciferase.
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)