Evidence map›Paper›PMID 39849460›Full record

ReviewCell communication and signaling : CCS2025

New insights into the structure domain and function of NLR family CARD domain containing 5.

Haiqing Zhu, Chengwei Xiao, Jiahua Chen, Bao Guo, Wenyan Wang, Zhenhai Tang, Yunxia Cao, Lei Zhan, Jun-Hui Zhang

Abstract readReview
In one paragraph

Review in Cell communication and signaling : CCS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Review
  2. Role of PANoptosis in intestinal diseases and its therapeutic implications.Journal of molecular medicine (Berlin, Germany) · 2026
    Review
  3. Mechanistic insights into natural product-driven modulation of NLRP3-inflammasome signalling in metabolic syndrome.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
  4. Review
  5. Review
  6. Review
  7. Integrative Analysis of Intestinal Transcriptomes UnderscoresBioinformatics and biology insights · 2026
    Article
  8. Review
  9. Review
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

9 authors.

Haiqing Zhu *The Second Affiliated Hospital of Anhui Medical University, No. 678 Furong Road, Hefei, Anhui, 230601, China.
Chengwei Xiao *The Second Affiliated Hospital of Bengbu Medical University, No. 663 Longhua Road, Bengbu, Anhui, 233040, China.
Jiahua Chen *The Second Affiliated Hospital of Anhui Medical University, No. 678 Furong Road, Hefei, Anhui, 230601, China.
Bao Guo *The Second Affiliated Hospital of Anhui Medical University, No. 678 Furong Road, Hefei, Anhui, 230601, China.
Wenyan WangThe Second Affiliated Hospital of Anhui Medical University, No. 678 Furong Road, Hefei, Anhui, 230601, China.
Zhenhai TangCenter for Scientific Research of Anhui Medical University, No. 81 Meishan Road, Hefei, Anhui, 230022, China.
Yunxia CaoThe First Affiliated Hospital of Anhui Medical University, No. 218 Jixi Road, Hefei, Anhui, 230022, China. caoyunxia5972@ahmu.edu.cn.
Lei ZhanThe First Affiliated Hospital of Anhui Medical University, No. 218 Jixi Road, Hefei, Anhui, 230022, China. 499329901@qq.com.
Jun-Hui ZhangThe Second Affiliated Hospital of Anhui Medical University, No. 678 Furong Road, Hefei, Anhui, 230601, China. huiui_zhang@foxmail.com.

Funding

National Natural Science Foundation of China No: 81802586Natural Science Foundation of Anhui Province No:2308085MH244Research Fund of the Anhui Institute of Translational Medicine No: 2022zhyx-C41, ZHYX2020A001University Research Fund of Anhui Medical University No: 2022xkj017
6 · The paper itself

Abstract

NOD-like receptor family CARD domain-containing 5 (NLRC5) is a major transcriptional coactivator of MHC class I genes. NLRC5 is the largest member of the NLR family and contains three domains: an untypical caspase recruitment domain (uCARD), a central nucleotide-binding and oligomerization domain (NOD or NACHT), and a leucine-rich repeat (LRR) domain. The functional variability of NLRC5 has been attributed to its different domain interactions with specific ligands in different cell types. In this review, we address the molecular mechanisms and their implications in multiple microenvironments based on the different functional domains of NLRC5.

Indexed as

Intracellular Signaling Peptides and ProteinsAnimalsHumansProtein DomainsIntracellular Signaling Peptides and ProteinsNLRC5 protein, humanImmunityMHC INLRC5PRRStructural domainTumour

Identifiers

PMID39849460
PMCPMC11755879

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.