Evidence map›Paper›PMID 18940667›Full record

ArticleChemistry & biology2008

Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38.

Qun Liu, Irina A Kriksunov, Hong Jiang, Richard Graeff, Hening Lin, Hon Cheung Lee, Quan Hao

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The role of NADnpj metabolic health and disease · 2025
    Review
  5. Article
  6. Article
  7. The chemical biology of NADCurrent opinion in chemical biology · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Porcine CD38 exhibits prominent secondary NAD(+) cyclase activity.Protein science : a publication of the Protein Society · 2016
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Sirtuin chemical mechanisms.Biochimica et biophysica acta · 2010
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Qun LiuMacCHESS, Cornell High Energy Synchrotron Source, Department of Chemistry and Chemical Biology, School of Applied & Engineering Physics, Cornell University, Ithaca, NY 14853, USA.
Irina A Kriksunov
Hong Jiang
Richard Graeff
Hening Lin
Hon Cheung Lee
Quan Hao
Cornell University · USUniversity of Minnesota · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
Structure and Functions of CD38R01GM061568 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI GRAEFF, RICHARD M · 2000 to 2009
$2.7M
NCRR NIH HHS P41 RR001646NCRR NIH HHS RR01646NIGMS NIH HHS DMR-0225180NIGMS NIH HHS GM061568NIGMS NIH HHS R01 GM061568
6 · The paper itself

Abstract

Enzymatic utilization of nicotinamide adenine dinucleotide (NAD) has increasingly been shown to have fundamental roles in gene regulation, signal transduction, and protein modification. Many of the processes require the cleavage of the nicotinamide moiety from the substrate and the formation of a reactive intermediate. Using X-ray crystallography, we show that human CD38, an NAD-utilizing enzyme, is capable of catalyzing the cleavage reactions through both covalent and noncovalent intermediates, depending on the substrate used. The covalent intermediate is resistant to further attack by nucleophiles, resulting in mechanism-based enzyme inactivation. The noncovalent intermediate is stabilized mainly through H-bond interactions, but appears to remain reactive. Our structural results favor the proposal of a noncovalent intermediate during normal enzymatic utilization of NAD by human CD38 and provide structural insights into the design of covalent and noncovalent inhibitors targeting NAD-utilization pathways.

Indexed as

ADP-ribosyl Cyclase 1CatalysisCrystallography, X-RayGlycosidesHumansModels, MolecularMolecular StructureNADNicotinamide MononucleotideProtein BindingADP-ribosyl Cyclase 1GlycosidesNADNicotinamide Mononucleotide

Identifiers

PMID18940667
PMCPMC2607045
OpenAlexW2006458211

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.