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Anthrax Toxin: A Pioneer of Targeted Protein Toxins. [PDF]
Richter S, Schmidt G.
europepmc +1 more source
Causal effect of tea consumption on the increased risk of puerperal sepsis and the mediation effect of CD25 on IgD- CD38-B cell: A Mendelian randomization analysis. [PDF]
Tong W +7 more
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A commentary on 'Exosomes miRNA-499a-5p targeted CD38 to alleviate anthraquinone induced cardiotoxicity: experimental research'. [PDF]
Liu YW, Hsieh CH.
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Dissemination of pathogenic bacteria is reinforced by a MARTX toxin effector duet. [PDF]
Choi S +17 more
europepmc +1 more source
The homo-dimeric form of ADP-ribosyl cyclase in solution
ADP-ribosyl cyclase is a multi-functional enzyme that catalyzes the formation of two Ca2+ signaling molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP). X-ray crystallography of three different crystal forms shows that it is a non-covalent dimer. Chemical cross-linking and dynamic light scattering were used in
Cyrus Munshi +2 more
exaly +6 more sources
Crystallization of ADP‐ribosyl cyclase from Aplysia californica
ADP-ribosyl cyclase synthesizes the secondary messenger cyclic ADP-ribose from NAD+. Diffraction quality crystals of the enzyme from ovotestes of Aplysia californica have been obtained. Crystallographic analysis of this enzyme will yield insight into the mode of binding of the novel cyclic nucleotide and the mechanism by which NAD+ is cyclized.
Lee, HC +3 more
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ADP-ribosyl cyclase couples to cyclic AMP signaling in the cardiomyocytes
Biochemical and Biophysical Research Communications, 2005ADP-ribosyl cyclase (ADPR-cyclase) produces a Ca(2+)-mobilizing second messenger cyclic ADP-ribose (cADPR) from beta-NAD(+). In this study, we examined the molecular basis of which beta-adrenergic receptor (betaAR) stimulation induces cADPR formation and characterized cardiac ADPR-cyclase.
So-Young Rah, Tae-Sik Nam, Ki-Chan Ha
exaly +3 more sources
International audienceCyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate are ubiquitous calcium-mobilizing messengers produced by the same family of multifunctional enzymes, the ADP-ribosyl cyclases.
Hélène Muller-Steffner +2 more
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