Evidence map›Paper›PMID 28479601›Full record

ArticleCellular & molecular immunology2018

B7-DC (PD-L2) costimulation of CD4

Xinxin Nie, Wenni Chen, Ying Zhu, Baozhu Huang, Weiwei Yu, Zhanshuai Wu, Sizheng Guo, Yiping Zhu, Liqun Luo, Shengdian Wang and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Cellular & molecular immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

34 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Immune dysregulation inFrontiers in immunology · 2026
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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

11 authors at 3 institutions in 2 countries.

Xinxin NieLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Wenni ChenLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Ying ZhuLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Baozhu HuangLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Weiwei YuLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Zhanshuai WuLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Sizheng GuoLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Yiping ZhuLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Liqun LuoLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China.
Shengdian WangInstitute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Lieping ChenLaboratory of Immunotherapy, Sun Yat-sen University, Guangzhou, Guangdong, China. lieping.chen@yale.edu.
Sun Yat-sen University · CNInstitute of Biophysics · CNYale University · US

Funding

Yale Pathology Tissue Services Shared ResourceP30CA016359 · NCI · YALE UNIVERSITY · PI Eric P. Winer · 1985 to 2026
$85.0M
Yale SPORE in Lung Cancer (YSILC): The Biology and Personalized Treatment of Lung CancerP50CA196530 · NCI · YALE UNIVERSITY · PI Harriet M. Kluger · 2015 to 2026
$31.1M
NCI NIH HHS P30 CA016359NCI NIH HHS P50 CA196530
6 · The paper itself

Abstract

The role of B7-DC in T-cell responses remains controversial because both coinhibitory and costimulatory functions have been reported in various experimental systems in vitro and in vivo. In addition to interacting with the coinhibitory receptor PD-1, B7-DC has also been shown to bind repulsive guidance molecule b (RGMb). The functional consequences of the B7-DC/RGMb interaction, however, remain unclear. More than a decade ago, we reported that replacement of a murine B7-DC mutant lysine with serine (K113S) at positive 113 resulted in a loss of binding capacity to PD-1. Nevertheless, K113S remained costimulatory for T cells in vitro, implicating a dual functionality for B7-DC in T-cell responses. Here we show that recombinant K113S protein interacts with RGMb with a similar affinity to wild-type B7-DC. More importantly, K113S costimulates CD4

Indexed as

Amino Acid SubstitutionAnimalsAsthmaCell Adhesion Molecules, NeuronalCHO CellsCricetulusFemaleGPI-Linked ProteinsHumansMiceMice, Inbred BALB CMutation, MissenseNerve Tissue ProteinsProgrammed Cell Death 1 Ligand 2 ProteinProgrammed Cell Death 1 ReceptorTh1 CellsCell Adhesion Molecules, NeuronalGPI-Linked ProteinsNerve Tissue ProteinsPdcd1lg2 protein, mousePdcd1 protein, mouseProgrammed Cell Death 1 Ligand 2 ProteinProgrammed Cell Death 1 ReceptorRgmb protein, mouseasthmaB7-DCK113SRGMbTh1/Th2

Identifiers

PMID28479601
PMCPMC6207567
OpenAlexW2612185660

What OpenQuestion holds

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Registered trials

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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.