ReviewGlycoconjugate journal2015
Exploring the role and diversity of mucins in health and disease with special insight into non-communicable diseases.
Review in Glycoconjugate journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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
19 citing papers in PubMed, 48 citations in OpenAlex.
- Chitosan as a Vaccine Adjuvant: From Material Determinants to Innate Immune Activation and Formulation Optimization.International journal of nanomedicine · 2026Review
- Article
- Targeted therapy and immunotherapy for gastric cancer: rational strategies, novel advancements, challenges, and future perspectives.Molecular medicine (Cambridge, Mass.) · 2025Review
- Review
- UnravelingAnalytical chemistry · 2024Article
- ThePolymers · 2024Review
- Review
- Mucin Glycans: A Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023Review
- Mirror Image Mucins and Thio Mucins with Tunable Biodegradation.Journal of the American Chemical Society · 2023Article
- Novel heavily fucosylated glycans as a promising therapeutic target in colorectal cancer.Journal of translational medicine · 2023Article
- Highly sialylated mucin-type glycopeptide from porcine intestinal mucosa after heparin extraction: O-glycan profiling and immunological activity evaluation.Glycoconjugate journal · 2021Article
- Pleiotropic Effects of FunctionalInternational journal of molecular sciences · 2021Article
- MUC1 is an oncoprotein with a significant role in apoptosis (Review).International journal of oncology · 2021Review
- An Evolutionary Perspective on the Impact of Genomic Copy Number Variation on Human Health.Journal of molecular evolution · 2020Review
- Highly Sensitive O-Glycan Profiling for Human Serum Proteins Reveals Gender-Dependent Changes in Colorectal Cancer Patients.Analytical chemistry · 2019Article
- Mucins and Pathogenic Mucin-Like Molecules Are Immunomodulators During Infection and Targets for Diagnostics and Vaccines.Frontiers in chemistry · 2019Review
- Calcium-activated Chloride Channel Regulator 1 (CLCA1) Controls Mucus Expansion in Colon by Proteolytic Activity.EBioMedicine · 2018Article
- Evolutionary conservation of the antimicrobial function of mucus: a first defence against infection.NPJ biofilms and microbiomes · 2018Review
- Targeting the gut barrier for the treatment of alcoholic liver disease.Liver research (Beijing, China) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mucins are major glycoprotein components of the mucus that coats the surfaces of cells lining the respiratory, digestive, gastrointestinal and urogenital tracts. They function to protect epithelial cells from infection, dehydration and physical or chemical injury, as well as to aid the passage of materials through a tract i.e., lubrication. They are also implicated in the pathogenesis of benign and malignant diseases of secretory epithelial cells. In Human there are two types of mucins, membrane-bound and secreted that are originated from mucous producing goblet cells localized in the epithelial cell layer or in mucous producing glands and encoded by MUC gene. Mucins belong to a heterogeneous family of high molecular weight proteins composed of a long peptidic chain with a large number of tandem repeats that form the so-called mucin domain. The molecular weight is generally high, ranging between 0.2 and 10 million Dalton and all mucins contain one or more domains which are highly glycosylated. The size and number of repeats vary between mucins and the genetic polymorphism represents number of repeats (VNTR polymorphisms), which means the size of individual mucins can differ substantially between individuals which can be used as markers. In human it is only MUC1 and MUC7 that have mucin domains with less than 40% serine and threonine which in turn could reduce number of PTS domains. Mucins can be considered as powerful two-edged sword, as its normal function protects from unwanted substances and organisms at an arm's length while, malfunction of mucus may be an important factor in human diseases. In this review we have unearthed the current status of different mucin proteins in understanding its role and function in various non-communicable diseases in human with special reference to its organ specific locations. The findings described in this review may be of direct relevance to the major research area in biomedicine with reference to mucin and mucin associated diseases.
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.