Evidence map›Paper›PMID 39194692›Full record

ReviewCurrent issues in molecular biology2024

Neuraminidase-1 (NEU1): Biological Roles and Therapeutic Relevance in Human Disease.

Jingxia Du, Hanqi Shui, Rongjun Chen, Yibo Dong, Chengyao Xiao, Yue Hu, Nai-Kei Wong

Abstract readReview
In one paragraph

Review in Current issues in molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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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

7 authors.

Jingxia DuCollege of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China.
Hanqi ShuiCollege of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China.
Rongjun ChenClinical Pharmacology Section, Department of Pharmacology, Shantou University Medical College, Shantou 515041, China.
Yibo DongCollege of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China.
Chengyao XiaoCollege of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China.
Yue HuCollege of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China.
Nai-Kei WongClinical Pharmacology Section, Department of Pharmacology, Shantou University Medical College, Shantou 515041, China.ORCID 0000-0003-1303-3170

Funding

Li Ka-Shing Foundation at Shantou University Medical College 510858044Luoyang City Social Development Public Welfare Project 2302001ANational Natural Science Foundation of China 32073002
6 · The paper itself

Abstract

Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both physiological and pathophysiological contexts, neuraminidases mediate diverse biological activities via the catalytic hydrolysis of terminal neuraminic, or sialic acid residues in glycolipid and glycoprotein substrates. The selective modulation of neuraminidase activity constitutes a promising strategy for treating a broad spectrum of human pathologies, including sialidosis and galactosialidosis, neurodegenerative disorders, cancer, cardiovascular diseases, diabetes, and pulmonary disorders. Structurally distinct as a large family of mammalian proteins, neuraminidases (NEU1 through NEU4) possess dissimilar yet overlapping profiles of tissue expression, cellular/subcellular localization, and substrate specificity. NEU1 is well characterized for its lysosomal catabolic functions, with ubiquitous and abundant expression across such tissues as the kidney, pancreas, skeletal muscle, liver, lungs, placenta, and brain. NEU1 also exhibits a broad substrate range on the cell surface, where it plays hitherto underappreciated roles in modulating the structure and function of cellular receptors, providing a basis for it to be a potential drug target in various human diseases. This review seeks to summarize the recent progress in the research on NEU1-associated diseases and highlight the mechanistic implications of NEU1 in disease pathogenesis. An improved understanding of NEU1-associated diseases should help accelerate translational initiatives to develop novel or better therapeutics.

Indexed as

disease mechanismsdrug developmentlysosomal sialidaseneuraminidase-1sialic acids (SAs)

Identifiers

PMID39194692
PMCPMC11353077

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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.