Evidence map›Paper›PMID 29438695›Full record

ArticleCancer cell2018

Eradication of Triple-Negative Breast Cancer Cells by Targeting Glycosylated PD-L1.

Chia-Wei Li, Seung-Oe Lim, Ezra M Chung, Yong-Soo Kim, Andrew H Park, Jun Yao, Jong-Ho Cha, Weiya Xia, Li-Chuan Chan, Taewan Kim and 18 more

Abstract read
In one paragraph

Article in Cancer cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 366 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
366citing papers in PubMed, 2 pooled it
–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

366 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Efficacy and safety of a combination treatment of immune checkpoint inhibitors in metastatic breast cancer: a systematic review and meta-analysis.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2024
    Pooled it
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306 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

28 authors.

Chia-Wei LiDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Seung-Oe LimDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
Ezra M ChungSTCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA.
Yong-Soo KimSTCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA.
Andrew H ParkSTCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA.
Jun YaoDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Jong-Ho ChaDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 151-742, Korea.
Weiya XiaDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Li-Chuan ChanDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Taewan KimDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Shih-Shin ChangDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Heng-Huan LeeDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Chao-Kai ChouDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Yen-Liang LiuDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA.
Hsin-Chih YehDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA.
Evan P PerilloDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA.
Andrew K DunnDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712, USA.
Chu-Wei KuoCore Facilities for Protein Structural Analysis, Academia Sinica, Taipei 115, Taiwan; Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
Kay-Hooi KhooInstitute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
Jennifer L HsuDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Graduate Institute of Biomedical Sciences and Center for Molecular Medicine, China Medical University, Taichung 404, Taiwan.
Yun WuDepartment of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Jung-Mao HsuDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Hirohito YamaguchiDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Tzu-Hsuan HuangDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Aysegul A SahinDepartment of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Gabriel N HortobagyiDepartment of Breast Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Stephen S YooSTCube Pharmaceuticals, Inc., 401 Professional Drive, Suite 250, Gaithersburg, MD 20879, USA.
Mien-Chie HungDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Unit 108, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA; Graduate Institute of Biomedical Sciences and Center for Molecular Medicine, China Medical University, Taichung 404, Taiwan; Department of Biotechnology, Asia University, Taichung 413, Taiwan. Electronic address: mhung@mdanderson.org.

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
Comprehensive Training Program in Imaging Science and InformaticsT32EB007507 · NIBIB · UNIVERSITY OF TEXAS AT AUSTIN · PI MARKEY, MIA K, RYLANDER, HENRY GRADY · 2009 to 2024
$2.7M
An integrated imaging tool for probing EGFR subcellular trafficking in real timeR21CA193038 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI DUNN, ANDREW K, YEH, HSIN-CHIH · 2015 to 2017
$625k
NCI NIH HHS P30 CA016672NCI NIH HHS R21 CA193038NIBIB NIH HHS T32 EB007507NIEHS NIH HHS 27303C0140
6 · The paper itself

Abstract

Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring β-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy.

Indexed as

AnimalsAntibodies, MonoclonalCell Line, TumorFemaleHumansLymphocytes, Tumor-InfiltratingMice, Inbred BALB CN-AcetylglucosaminyltransferasesProgrammed Cell Death 1 ReceptorTriple Negative Breast NeoplasmsAntibodies, MonoclonalN-AcetylglucosaminyltransferasesProgrammed Cell Death 1 Receptorantibody-drug conjugateB3GNT3glycosylationimmune checkpoint blockadeimmunosuppressionimmunotherapyPD-1PD-L1receptor internalizationTNBC

Identifiers

PMID29438695
PMCPMC5824730

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.