Evidence map›Paper›PMID 41339784›Full record

ArticleMolecular medicine (Cambridge, Mass.)2025

Hydroxyethylamine & phthalimide analogs restoring defects due to GNE dysfunction: rare disease therapeutic significance.

Shagun Singh, Meenakshi Bansal, Neha Sharma, Vikas Yadav, Fluencephila Mashangva, Jyoti Oswalia, Vaishali Gautam, Gagan Deep Jhingan, Naidu Subbarao, Brijesh Rathi and 1 more

Abstract read
In one paragraph

Article in Molecular medicine (Cambridge, Mass.), 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.

  1. 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

11 authors.

Shagun SinghSchool of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India.ORCID 0009-0005-0843-385X
Meenakshi BansalDepartment of Chemistry, HG Khorana Centre for Chemical Biology, Hansraj College, University of Delhi, Delhi, 110007, India.
Neha SharmaDepartment of Chemistry, HG Khorana Centre for Chemical Biology, Hansraj College, University of Delhi, Delhi, 110007, India.
Vikas YadavSchool of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India.ORCID 0009-0000-9158-6702
Fluencephila MashangvaSchool of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India.ORCID 0000-0002-3154-3484
Jyoti OswaliaSchool of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India.ORCID 0000-0001-7760-760X
Vaishali GautamSchool of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India.
Gagan Deep JhinganVProteomics, Green Park, New Delhi, 110016, India.
Naidu SubbaraoSchool of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India.ORCID 0000-0002-1720-2165
Brijesh RathiDepartment of Chemistry, HG Khorana Centre for Chemical Biology, Hansraj College, University of Delhi, Delhi, 110007, India. brijeshrathi@hrc.du.ac.in.ORCID 0000-0003-2133-8847
Ranjana AryaSchool of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India. ranjanaa@mail.jnu.ac.in.ORCID 0000-0001-5924-9351

Funding

Department of Science and Technology, Ministry of Science and Technology, India DST/TDT/TC/Rare/2022/21(G)/1
6 · The paper itself

Abstract

Rare diseases refer to a group of neglected diseases with low prevalence that face challenges in diagnostics as well as therapeutics due to phenotypic heterogeneity and ineffective clinical trials. In this study, we evaluated two novel analogs of hydroxyethylamine & phthalimide (LTC-181 and LTC-1717) for their potential effect on the epimerase activity of mutant GNE proteins associated with GNE myopathy. GNE gene encodes a key bifunctional sialic acid biosynthetic enzyme, UDP-N-acetyl Glucosamine 2-epimerase/N-acetyl Mannosamine Kinase; GNE). The compounds have significantly increased the epimerase activity of r-F307C-GNE and r-A555V-GNE mutant proteins in vitro. Reduced GNE epimerase activity and sialic acid content in muscle cell-based model for GNE function (SKM-GNEHz) was increased by 2-fold after addition of these compounds. The proteomic study showed that the compounds affected cytoskeletal organization, autophagy and muscle atrophy. Also, treatment with analogs enhanced the cell viability of SKM-GNEHz cells with increased F-actin polymerization and cell migration, thereby, restoring GNE deficient function. Additionally, effect of these compounds was observed with enhanced autophagy and reduced muscle atrophy function in GNE deficient muscle cell. Docking and interaction studies showed that LTC-1717 stabilize GNE better than LTC-181, indicating better therapeutic potential. Overall, this study indicates that HEA-phthalimide analog could be promising leads for treating GNE myopathy.

Indexed as

Distal MyopathiesMultienzyme ComplexesPhthalimidesRare DiseasesAnimalsHumansMutationMultienzyme ComplexesphthalimidePhthalimidesUDP-N-acetylglucosamine 2-epimerase - N-acetylmannosamine kinaseGNE myopathyRare genetic diseaseSmall moleculesTherapeutics

Identifiers

PMID41339784
PMCPMC12673733

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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.