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Cited by 736

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38

Howard, Maureen, Grimaldi, J. Christopher, Bazan, J. Fernando, Lund, Frances E., Santos-Argumedo, Leopoldo, Parkhouse, R. M. E., Walseth, Timothy F., Lee, Hon Cheung·1993·Science

Abstract

CD38 is a 42-kilodalton glycoprotein expressed extensively on B and T lymphocytes. CD38 exhibits a structural homology to Aplysia adenosine diphosphate (ADP)-ribosyl cyclase. This enzyme catalyzes the synthesis of cyclic ADP-ribose (cADPR), a metabolite of nicotinamide adenine dinucleotide (NAD + ) with calcium-mobilizing activity. A complementary DNA encoding the extracellular domain of murine CD38 was constructed and expressed, and the resultant recombinant soluble CD38 was purified to homogeneity. Soluble CD38 catalyzed the formation and hydrolysis of cADPR when added to NAD + . Purified cADPR augmented the proliferative response of activated murine B cells, potentially implicating the enzymatic activity of CD38 in lymphocyte function.

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Metadata

Authors
Howard, M., Grimaldi, J. C., Bazan, J. F., Lund, F. E., Santos-Argumedo, L., Parkhouse, R. M. E., Walseth, T. F., & Lee, H. C.
Venue
Science
Published
1993-11-12
Volume
262
Issue
5136
Pages
1056-1059
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2082340361
Cited by
736
References
1
FWCI
10.98
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38. https://app.cochat.ai/papers/10.1126/science.8235624
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Howard, M., Grimaldi, J. C., Bazan, J. F., Lund, F. E., Santos-Argumedo, L., Parkhouse, R. M. E., Walseth, T. F., & Lee, H. C. (1993). Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38. Science. https://doi.org/10.1126/science.8235624

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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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