Evidence map›Paper›PMID 34871367›Full record

ReviewThe Biochemical journal2021

NAD+-consuming enzymes in immune defense against viral infection.

Jialin Shang, Michael R Smith, Ananya Anmangandla, Hening Lin

Erratum issuedOpen access · hybridAbstract readReview
In one paragraph

Review in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. NADThe Journal of general virology · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Biomolecules & biomedicine · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. NADNature communications · 2023
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Jialin Shang *Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, U.S.A.
Michael R Smith *Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, U.S.A.
Ananya Anmangandla *Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, U.S.A.
Hening LinDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, U.S.A.ORCID 0000-0002-0255-2701
Cornell University · USHoward Hughes Medical Institute · US

Funding

Training future leaders at the chemistry-biology interfaceT32GM138826 · NIGMS · CORNELL UNIVERSITY · PI Jeremy Baskin · 2021 to 2026
$2.6M
Mechanisms of AHR Metabolic ToxicityR01ES027488 · NIEHS · WEILL MEDICAL COLL OF CORNELL UNIV · PI YANG, YUE · 2017 to 2021
$2.3M
Metabolite Sensing and Regulation of Protein FunctionR35GM131808 · NIGMS · CORNELL UNIVERSITY · PI LIN, HENING · 2019 to 2023
$1.9M
NIEHS NIH HHS R01 ES027488NIGMS NIH HHS R35 GM131808NIGMS NIH HHS T32 GM138826
6 · The paper itself

Abstract

The COVID-19 pandemic reminds us that in spite of the scientific progress in the past century, there is a lack of general antiviral strategies. In analogy to broad-spectrum antibiotics as antibacterial agents, developing broad spectrum antiviral agents would buy us time for the development of vaccines and treatments for future viral infections. In addition to targeting viral factors, a possible strategy is to understand host immune defense mechanisms and develop methods to boost the antiviral immune response. Here we summarize the role of NAD+-consuming enzymes in the immune defense against viral infections, with the hope that a better understanding of this process could help to develop better antiviral therapeutics targeting these enzymes. These NAD+-consuming enzymes include PARPs, sirtuins, CD38, and SARM1. Among these, the antiviral function of PARPs is particularly important and will be a focus of this review. Interestingly, NAD+ biosynthetic enzymes are also implicated in immune responses. In addition, many viruses, including SARS-CoV-2 contain a macrodomain-containing protein (NSP3 in SARS-CoV-2), which serves to counteract the antiviral function of host PARPs. Therefore, NAD+ and NAD+-consuming enzymes play crucial roles in immune responses against viral infections and detailed mechanistic understandings in the future will likely facilitate the development of general antiviral strategies.

Indexed as

Immunity, InnateADP-ribosyl Cyclase 1Antiviral AgentsArmadillo Domain ProteinsCOVID-19COVID-19 Drug TreatmentCytoskeletal ProteinsHumansNADPoly (ADP-Ribose) Polymerase-1Protein DomainsSARS-CoV-2SirtuinsViral Nonstructural ProteinsVirus DiseasesADP-ribosyl Cyclase 1Antiviral AgentsArmadillo Domain ProteinsCytoskeletal ProteinsNADPoly (ADP-Ribose) Polymerase-1SARM1 protein, humanSirtuinsViral Nonstructural Proteinsimmune responsemacrodomainNAD+-consuming enzymesPARPsirtuinsvirus

Identifiers

PMID34871367
PMCPMC8718269
OpenAlexW4200379711

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.