ArticleNature communications2026
p38β-mediated BiP phosphorylation drives stemness and chemoresistance by suppressing UPR activation in hepatocellular carcinoma.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
Abstract
Tumor-initiating cells (TICs) promote tumor initiation and therapy resistance, yet the kinase regulators that sustain TICs remain incompletely defined. Here, we identify the stress kinase p38β (MAPK11) supports TIC maintenance and drug resistance in hepatocellular carcinoma (HCC). Integrated analysis of chemotherapy-enriched HCC spheroids, and DepMap data prioritized p38β as a kinase linked to stemness and chemoresistance. High p38β expression correlates with poor prognosis and aggressive clinicopathological features in HCC patients. Mechanistically, p38β phosphorylates the endoplasmic reticulum (ER) chaperone BiP at threonine 648, enhancing its association with the unfolded protein response (UPR) sensors PERK and IRE1-α. This modification suppresses UPR activation and reduces unfolded protein accumulation, thereby preserving ER proteostasis under chemotherapeutic stress. Functionally, p38β-driven BiP phosphorylation sustains TIC phenotypes and cisplatin resistance in vitro and in vivo. BiP inhibition with HA15 restores UPR signaling and sensitizes patient-derived xenograft and organoid models to cisplatin, revealing a targetable p38β-BiP axis in HCC.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.