Evidence map›Paper›PMID 36819105›Full record

ReviewFrontiers in cell and developmental biology2023

Mortalin: Protein partners, biological impacts, pathological roles, and therapeutic opportunities.

Niki Esfahanian, Cole D Knoblich, Gaven A Bowman, Khosrow Rezvani

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. GRP75 sustains CD8Cell death and differentiation · 2026
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  5. The role of HMGA1 in genome stability: Implications in human cancer.Cellular and molecular life sciences : CMLS · 2026
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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

4 authors at 1 institution in 1 country.

Niki EsfahanianDivision of Basic Biomedical Sciences, Sanford School of Medicine, The University of South Dakota, Vermillion, SD, United States.
Cole D KnoblichDivision of Basic Biomedical Sciences, Sanford School of Medicine, The University of South Dakota, Vermillion, SD, United States.
Gaven A BowmanDivision of Basic Biomedical Sciences, Sanford School of Medicine, The University of South Dakota, Vermillion, SD, United States.
Khosrow RezvaniDivision of Basic Biomedical Sciences, Sanford School of Medicine, The University of South Dakota, Vermillion, SD, United States.
University of South Dakota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mortalin (GRP75, HSPA9A), a heat shock protein (HSP), regulates a wide range of cellular processes, including cell survival, growth, and metabolism. The regulatory functions of mortalin are mediated through a diverse set of protein partners associated with different cellular compartments, which allows mortalin to perform critical functions under physiological conditions, including mitochondrial protein quality control. However, alteration of mortalin's activities, its abnormal subcellular compartmentalization, and its protein partners turn mortalin into a disease-driving protein in different pathological conditions, including cancers. Here, mortalin's contributions to tumorigenic pathways are explained. Pathology information based on mortalin's RNA expression extracted from The Cancer Genome Atlas (TCGA) transcriptomic database indicates that mortalin has an independent prognostic value in common tumors, including lung, breast, and colorectal cancer (CRC). Subsequently, the binding partners of mortalin reported in different cellular models, from yeast to mammalian cells, and its regulation by post-translational modifications are discussed. Finally, we focus on colorectal cancer and discuss how mortalin and its tumorigenic downstream protein targets are regulated by a ubiquitin-like protein through the 26S proteasomal degradation machinery. A broader understanding of the function of mortalin and its positive and negative regulation in the formation and progression of human diseases, particularly cancer, is essential for developing new strategies to treat a diverse set of human diseases critically associated with dysregulated mortalin.

Indexed as

cancercellular localizationmortalin (HSPA9)post-translational modification (PTM)protein partners

Identifiers

PMID36819105
PMCPMC9932541
OpenAlexW4319014135

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.