Evidence map›Paper›PMID 35901491›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2022

Succinylation Inhibits the Enzymatic Hydrolysis of the Extracellular Matrix Protein Fibrillin 1 and Promotes Gastric Cancer Progression.

Xingyun Wang, Xiao Shi, Hongcheng Lu, Chen Zhang, Xiang Li, Tiancheng Zhang, Jiajia Shen, Jianfei Wen

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

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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

8 authors at 5 institutions in 1 country.

Xingyun WangDepartment of General Surgery, First Affiliated Hospital of Nanjing Medical University, Nanjing, 210029, China.
Xiao ShiDepartment of Gastroenterology, Zhongda Hospital, School of Medicine, Southeast University, Nanjing, 210009, China.
Hongcheng LuDepartment of Urology, Zhongda Hospital Affiliated to Southeastern China University, Nanjing, 210029, China.
Chen ZhangDepartment of Biotherapy, Medical Center for Digestive Diseases, Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210011, China.
Xiang LiDepartment of Surgical Oncology, Jiangsu Province Hospital of Chinese Medicine, Affiliated Hospital of Nanjing University of Chinese Medicine, Nanjing, 210029, China.
Tiancheng ZhangDepartment of Surgical Oncology, Jiangsu Province Hospital of Chinese Medicine, Affiliated Hospital of Nanjing University of Chinese Medicine, Nanjing, 210029, China.
Jiajia ShenDepartment of General Surgery, First Affiliated Hospital of Nanjing Medical University, Nanjing, 210029, China.
Jianfei WenDepartment of General Surgery, First Affiliated Hospital of Nanjing Medical University, Nanjing, 210029, China.ORCID 0000-0002-0363-1196
Jiangsu Province Hospital · CNNanjing University of Chinese Medicine · CNZhongda Hospital Southeast University · CNSecond Affiliated Hospital of Nanjing Medical University · CNShanghai Jiao Tong University · CN

Funding

National Natural Science Foundation of China 81802464
6 · The paper itself

Abstract

Extracellular matrix (ECM) remodeling is crucial in the regulation of gastric cancer (GC) progression. This work aims to reveal novel posttranslational modifications and their relevant mechanisms in GC. In 3D matrix culture and animal models, it is found that fibrillin 1 (FBN1) expression is increased in advanced GC and has succinylation modification. The succinylation modification of FBN1 blocks its degradation by matrix metalloproteinases (MMPs). The long-term accumulation and deposition of FBN1 enhance tumor progression by activating TGF-β1 and intracellular PI3K/Akt pathway. The FBN1 succinylation site monoclonal antibody can effectively intervene the effect of succinylation modification and inhibit GC progression. FBN1 is specifically upregulated in the progression of GC compared with other tumors. In conclusion, FBN1 is widely present in the form of K672-succinylated modifications in GC. Besides, the succinyl group of FBN1 blocks its binding to MMP2, inhibits its degradation by MMP2, and leads to the accumulation of FBN1, which poses a long-term risk to the poor prognosis of GC.

Indexed as

Stomach NeoplasmsAnimalsAntibodies, MonoclonalFibrillin-1FibrillinsHydrolysisMatrilin ProteinsMatrix Metalloproteinase 2Phosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktTransforming Growth Factor beta1Antibodies, MonoclonalFibrillin-1FibrillinsMatrilin ProteinsMatrix Metalloproteinase 2Phosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktTransforming Growth Factor beta1fibrillin 1gastric cancerMMP2succinylationTGF-β1

Identifiers

PMID35901491
PMCPMC9507347
OpenAlexW4288385187

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.