Results 161 to 170 of about 10,542 (222)

Biological Functions and Therapeutic Potential of NAD⁺ Metabolism in Gynecological Cancers. [PDF]

Cancers (Basel)
Myong S, Nguyen AQ, Challa S.
europepmc   +1 more source

HELIOS NAD-Seq: A Next-Generation Capture and Sequencing Protocol for NAD-Capped RNAs with Superior Targeting and Processing

Möhler M, Seong TW, Weber F, Filloy HGM, Wölke M, Tosun E, Mendonca E, Crenner A, Zhang Y, Preugschat F, Jäschke A.   +10 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

ADP-ribosyl cyclase couples to cyclic AMP signaling in the cardiomyocytes

Biochemical and Biophysical Research Communications, 2005
ADP-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.
Guang-Hua, Xie, So-Young, Rah, Sang-Jin, Kim, Tae-Sik, Nam, Ki-Chan, Ha, Soo-Wan, Chae, Mie-Jae, Im, Uh-Hyun, Kim   +7 more
openaire   +4 more sources

Mono(ADP-ribosyl)ation of Gi by eukaryotic cysteine-specific mono(ADP-ribosyl)transferase attenuates inhibition of adenylate cyclase by epinephrine

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1989
Eukaryotic cysteine-specific mono(ADP-ribosyl)transferase, named ADP-ribosyltransferase C (Tanuma, S., Kawashima, K. and Endo, H. (1988) J. Biol. Chem. 263, 5485-5489), attenuates inhibition of adenylate cyclase in human platelet membranes by epinephrine. This attenuation appeared to result from mono(ADP-ribosyl)ation by ADP-ribosyltransferase C of the
S, Tanuma, H, Endo
openaire   +4 more sources

Cloning and characterization of cDNA encoding rat ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (homologue to human CD38) from islets of Langerhans.

Biochimica Et Biophysica Acta - Molecular Cell Research, 1994
Tetsuhiko Koguma, S. Takasawa, A. Tohgo, T. Karasawa, Y. Furuya, H. Yonekura, H. Okamoto   +6 more
semanticscholar   +3 more sources

A single protein immunologically identified as CD38 displays NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes.

Biochemical and Biophysical Research Communications, 1993
E. Zocchi, L. Franco, L. Guida, Umberto Benatti, Antonio Bargellesi, F. Malavasi, Hon-cheung Lee, A. Flora   +7 more
semanticscholar   +3 more sources

Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38

Nature Structural Biology, 1996
G. Prasad, Duncan E. McRee, Enrico A. Stura, David G. Levitt, Hon-cheung Lee, C. D. Stout   +5 more
semanticscholar   +3 more sources

Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.

Journal of Molecular Biology, 2002
S. Yamamoto-Katayama, M. Ariyoshi, K. Ishihara, T. Hirano, H. Jingami, K. Morikawa   +5 more
semanticscholar   +3 more sources

ADP-Ribosyl Cyclase and CD38

Advances in experimental medicine and biology, 1997
Mobilization of internal Ca+2 is an important signaling mechanism in cells. In addition to the inositol trisphosphate pathway, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide (NAADP) have been shown to mobilize Ca+2 via independent mechanisms.
Hon Cheung Lee, Richard M. Graeff, Timothy F. Walseth   +2 more
openaire   +3 more sources