Evidence map›Paper›PMID 42138128›Full record

ReviewBiochemical Society transactions2026

Structural insights into HRI kinase activity and inhibition.

Min Cao, Glenn R Masson

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Min CaoMRC Protein Phosphorylation and Ubiquitination Unit, Faculty of Life Sciences, University of Dundee, Dundee, U.K.
Glenn R MassonDivision of Cancer Research, Faculty of Heath, University of Dundee, Ninewells Hospital, Dundee, U.K.ORCID 0000-0002-1386-4719

Funding

China Scholarship Council (CSC) N/AUniversity of Dundee (Oilthigh Dhùn Dè) N/A
6 · The paper itself

Abstract

Haem-regulated inhibitor (HRI) is emerging as a potential therapeutic target in several disease areas, including cancers such as multiple myeloma and neurodegenerative disease. As one of four related mammalian kinases that phosphorylate the mRNA translation machinery substrate eIF2α, it has a central role in sensing several disparate proteotoxic stresses and preventing subsequent rounds of protein production. In this review, we will examine the latest research on the structural and molecular basis of HRI inhibition and activation, examining both regulatory biological interactions with proteins and cofactors. What emerges is that despite almost 75 years since the first identification of HRI, we still know remarkably little about how this kinase functions and is regulated.

Indexed as

eIF-2 KinaseAnimalsEukaryotic Initiation Factor-2HumansIntegrated Stress ResponsePhosphorylationProtein Kinase InhibitorseIF-2 KinaseEukaryotic Initiation Factor-2Protein Kinase InhibitorsDELE1-CTDeIF2alphahaemHRIISRkinases

Identifiers

PMID42138128
PMCPMC13181343

What OpenQuestion holds

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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.