The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) as Messengers for Calcium Mobilization
Open accessAbstract
Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate were discovered >2 decades ago. That they are second messengers for mobilizing Ca(2+) stores has since been firmly established. Separate stores and distinct Ca(2+) channels are targeted, with cyclic ADP-ribose acting on the ryanodine receptors in the endoplasmic reticulum, whereas nicotinic acid adenine dinucleotide phosphate mobilizes the endolysosomes via the two-pore channels. Despite the structural and functional differences, both messengers are synthesized by a ubiquitous enzyme, CD38, whose crystal structure and catalytic mechanism have now been well elucidated. How this novel signaling enzyme is regulated remains largely unknown and is the focus of this minireview.
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Cites
Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology
Malavasi, F., Deaglio, S., Funaro, A., Ferrero, E., Horenstein, A. L., Ortolan, E., Vaisitti, T., & Aydin, S. (2008) · Physiological Reviews · doi:10.1152/physrev.00035.2007 · Cited by 862
NAADP mobilizes calcium from acidic organelles through two-pore channels
Calcraft, P. J., Ruas, M., Pan, Z., Cheng, X., Arredouani, A., Hao, X., Tang, J., Rietdorf, K., Teboul, L., Chuang, K.-T., et al. (2009) · Nature · doi:10.1038/nature08030 · Cited by 760
CD38 is critical for social behaviour by regulating oxytocin secretion
Jin, D., Liu, H.-X., Hirai, H., Torashima, T., Nagai, T., Lopatina, O., Shnayder, N. A., Yamada, K., Noda, M., Seike, T., et al. (2007) · Nature · doi:10.1038/nature05526 · Cited by 665
Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
Lee, H. C. (2001) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.317 · Cited by 433
Self-citationJackson, D. G., & Bell, J. I. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.7.2811 · Cited by 343 · cited 1×
“In lymphocytes, CD38 is expressed on the surface as a type II protein, with its catalytic C-terminal domain facing outside (66).”
Background
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The many faces of calmodulin in cell proliferation, programmed cell death, autophagy, and cancer
Berchtold, M. W., & Villalobo, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.021 · Cited by 320
Naviaux, J. C., Wang, L., Li, K., Bright, A., Alaynick, W. A., Williams, K. R., Powell, S. B., & Naviaux, R. K. (2015) · Molecular Autism · doi:10.1186/2040-2392-6-1 · Cited by 285
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Metadata
- Authors
- Lee, H. C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-09
- Volume
- 287
- Issue
- 38
- Pages
- 31633-31640
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038626940
- Cited by
- 197
- References
- 5
- FWCI
- 13.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Lee, H. C. (2012). Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) as Messengers for Calcium Mobilization. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r112.349464
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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