scholarly journals Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues

ChemBioChem ◽  
2017 ◽  
Vol 18 (4) ◽  
pp. 378-381 ◽  
Author(s):  
Susanne Ermert ◽  
Stephan M. Hacker ◽  
Alexander Buntru ◽  
Martin Scheffner ◽  
Christof R. Hauck ◽  
...  
Keyword(s):  
Atp Analogues

scholarly journals Inhibition of vascular smooth muscle cell calcification by ATP analogues

2019 ◽  
Vol 15 (3) ◽  
pp. 315-326 ◽  
Author(s):  
Jessal J. Patel ◽  
Lucie E. Bourne ◽  
José Luis Millán ◽  
Timothy R. Arnett ◽  
Vicky E. MacRae ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Vascular Smooth Muscle Cell ◽  
Atp Analogues

scholarly journals Two ATP-activated conductances in bullfrog atrial cells.

1988 ◽  
Vol 91 (1) ◽  
pp. 1-27 ◽  
Author(s):  
D D Friel ◽  
B P Bean
Keyword(s):  
Ionic Channels ◽  
Extracellular Atp ◽  
Fluctuation Analysis ◽  
Current Fluctuation ◽  
Atrial Cells ◽  
Atp Analogues ◽  
Alpha Beta ◽  
Gamma S ◽  
Inwardly Rectifying ◽  
Current Fluctuation Analysis

Currents activated by extracellular ATP were studied in single voltage-clamped bullfrog atrial cells. Rapid application of ATP elicited currents carried through two different conductance pathways: a rapidly desensitizing conductance reversing near -10 mV, and a maintained, inwardly rectifying conductance reversing near -85 mV. ATP activated the desensitizing component of current with a K 1/2 of approximately 50 microM and the maintained component with a K 1/2 of approximately 10 microM. Both types of current were activated by ATP but not by adenosine, AMP, or ADP. The desensitizing current was selectively inhibited by alpha, beta-methylene ATP, and the maintained, inwardly rectifying current was selectively suppressed by extracellular Cs. The desensitizing component of current was greatly reduced when extracellular Na was replaced by N-methylglucamine, but was slightly augmented when Na was replaced by Cs. GTP, ITP, and UTP were all ineffective in activating the desensitizing current, and of a variety of ATP analogues, only ATP-gamma-S was effective. Addition of EGTA or BAPTA to the intracellular solution did not obviously affect the desensitizing current. Fluctuation analysis of currents through the desensitizing conductance suggested that current is carried through ionic channels with a small (less than pS) unitary conductance.

scholarly journals Enzymic ribonucleoside reduction at the non-phosphorylated level in Acetabularia

1985 ◽  
Vol 73 (1) ◽  
pp. 7-18
Author(s):  
E.J. de Groot ◽  
H.G. Schweiger
Keyword(s):  
Inhibitory Effect ◽  
Atp Analogues

The occurrence of an enzyme that catalyses the conversion of cytidine into deoxycytidine was demonstrated in homogenates of Acetabularia. Cytidine was identified as the substrate by comparing cytidine, cytidine 5′-monophosphate, cytidine 5′-diphosphate and cytidine 5′-triphosphate as potential substrates. Experiments with ATP analogues whose inhibitory effect on kinase reactions is well established, supplied evidence that the nucleoside is reduced without a phosphorylation step before the reduction. Further evidence in this line came from incubations with cytidine in the presence of phosphatase and from trap-type experiments in which the effects of excess non-labelled cytidine 5′-phosphate and deoxycytidine, respectively, on the formation of deoxycytidine phosphates from cytidine were studied.

scholarly journals Volume-sensitive K influx in human red cell ghosts.

1988 ◽  
Vol 92 (5) ◽  
pp. 685-711 ◽  
Author(s):  
J R Sachs
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Cell ◽  
Influx Rate ◽  
Phosphatidylinositol Kinase ◽  
Kinase C ◽  
Low Concentrations ◽  
Atp Analogues ◽  
High Concentrations ◽  
Activate Protein Kinase

K influx into resealed human red cell ghosts increases when the ghosts are swollen. The influx demonstrates properties similar to volume-sensitive K fluxes present in other cells. The influx is, for the most part, insensitive to the nature of the major intracellular cation and therefore is not a K-K exchange. The influx is much greater when the major anion is Cl than when the major anion is NO3; Cl stimulates the flux and, at constant Cl, NO3 inhibits it. Increase in the influx rate is rapid when shrunken ghosts are swollen or when NO3 is replaced by Cl. The volume-sensitive K influx requires intracellular MgATP at low concentrations, and ATP cannot be replaced by nonhydrolyzable ATP analogues. The volume-sensitive influx is inhibited by Mg2+ and by high concentrations of vanadate, but is stimulated by low concentrations of vanadate. It is not modified by cAMP, the removal of Ca2+ by EGTA, substances that activate protein kinase C, or by inhibition of phosphatidylinositol kinase. The influx is inhibited by neomycin and by trifluoperazine.

Interaction between Synthetic ATP Analogues and Actomyosin Systems. IV*

1967 ◽  
Vol 61 (4) ◽  
pp. 460-472 ◽  
Author(s):  
YUJI TONOMURA ◽  
KIICHI IMAMURA ◽  
MORIO IKEHARA ◽  
HITOSHI UNO ◽  
FUMIO HARADA
Keyword(s):  
Atp Analogues
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