Targeting collagen Prolyl 4-hydroxylase for cancer treatment.

Run Shi, Yang Liu, RuiXue Yu

Abstract readReview

In one paragraph

Review in Medical oncology (Northwood, London, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Collagen Prolyl 4-Hydroxylase: An Emerging Key Player in Cardiac Fibrosis.Journal of cardiovascular translational research · 2026
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

3 authors.

Run ShiSchool of Medicine, Pingdingshan University, Pingdingshan, 467000, Henan, China. 3503@pdsu.edu.cn.

Yang LiuSchool of Medicine, Pingdingshan University, Pingdingshan, 467000, Henan, China.

RuiXue YuSchool of Medicine, Pingdingshan University, Pingdingshan, 467000, Henan, China. 2746@pdsu.edu.cn.

Funding

Key Scientific Research Projects of Higher Education Institutions in Henan Province 25A180026Pingdingshan College PhD Startup Fund PXY-BSQD-2024007

6 · The paper itself

Abstract

Collagen prolyl 4-hydroxylase (C-P4H) is a critical enzyme involved in collagen biosynthesis, mediating the hydroxylation of proline residues to ensure the stability of collagen and its integration into the extracellular matrix (ECM). Within the tumor microenvironment (TME), aberrant ECM remodeling, characterized by excessive collagen deposition, contributes to tumor progression, metastasis, and resistance to therapy. C-P4H operates as an α2β2 tetramer, comprising three isoenzymes distinguished by their catalytic α-subunits (P4HA1, P4HA2, P4HA3) and a common β-subunit (P4HB). Both P4HAs and P4HB are frequently overexpressed in various cancers, where they facilitate ECM remodeling, cancer cell invasion, and metastasis. Inhibitors targeting P4HAs or P4HB have demonstrated promising anti-tumor effects, highlighting its potential as a therapeutic target. This review consolidates recent advancements in the comprehension of the roles and regulatory mechanisms of C-P4H in cancer progression and evaluates the development of C-P4H targeted therapies for prospective cancer treatment.

Indexed as

NeoplasmsProcollagen-Proline DioxygenaseProlyl-Hydroxylase InhibitorsProlyl HydroxylasesAnimalsHumansMolecular Targeted TherapyTumor MicroenvironmentProcollagen-Proline DioxygenaseProlyl-Hydroxylase InhibitorsProlyl HydroxylasesCollagenEnzyme inhibitorsMolecular targeted therapyNeoplasm metastasisProcollage-Proline dioxygenase

Identifiers

PMID41452560

DOI10.1007/s12032-025-03219-w

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.