The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested identity is verified: human A4GNT (HGNC:17968; UniProt Q9UNA3) encodes alpha-1,4-N-acetylglucosaminyltransferase (alpha4GnT), not the similarly related A4GALT/Gb3 synthase. A4GNT is the gastric gland/class-III mucin glycosyltransferase that generates terminal GlcNAcα1→4Gal structures on mucin O-glycans. The literature identifies alpha4GnT as the sole enzyme responsible for these characteristic alphaGlcNAc termini; comparative sequence analysis places it near alpha1,4-galactosyltransferases, consistent with the supplied GT32, nucleotide-diphosphosugar-transferase, and DxD-motif domain annotations. No conflicting use of A4GNT for another human protein was found (kawakubo2019analysisofa4gnt pages 1-2, hennet2002thegalactosyltransferasefamily pages 10-11).
Its best-supported physiological role is to elaborate the protective, predominantly MUC6-associated gland mucus of the stomach and proximal duodenum. The resulting alphaGlcNAc cap contributes to gastric host defense, including direct suppression of Helicobacter pylori. Loss of the pathway in mice removes alphaGlcNAc-bearing gastric O-glycans and causes spontaneous differentiated-type gastric adenocarcinoma. This is compelling causal evidence in animals, but it should not be interpreted as proof that isolated A4GNT deficiency is an established monogenic human gastric-cancer syndrome (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6, arai2024theroleof pages 2-4).
| Topic | Best-supported annotation | Evidence type/species | Confidence/caveat |
|---|---|---|---|
| Identity verification | A4GNT matches human alpha1,4-N-acetylglucosaminyltransferase (alpha4GnT), the enzyme responsible for biosynthesis of terminal α1,4-linked GlcNAc (αGlcNAc) on gastric gland mucin; no conflicting same-symbol protein was identified in the retrieved literature (kawakubo2019analysisofa4gnt pages 1-2, hennet2002thegalactosyltransferasefamily pages 10-11) | Review/legacy biochemical literature; human-focused, with mouse validation of the same pathway | High for identity; direct cloning paper was not retrieved here, so this synthesis relies on authoritative review wording plus later functional mouse studies |
| Enzymatic reaction and product | Best-supported function is transfer of GlcNAc in α1,4 linkage to terminal galactose on gastric gland mucin O-glycans, producing αGlcNAc-capped O-glycans; 2019 mouse glycomic analysis confirms WT stomach contains αGlcNAc-bearing neutral O-glycans that are absent in A4gnt knockout mucosa (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6) | Review statement plus mouse glycomics/histochemistry | High for product/linkage; donor (UDP-GlcNAc) and precise acceptor structural rules are standard legacy annotations but were not directly shown in the retrieved excerpts |
| Donor/acceptor specificity | Conservative annotation: donor is likely UDP-GlcNAc and acceptor is gastric gland mucin O-glycan terminal Gal in the MUC6/class III mucin context; this is consistent with the literature describing alpha4GnT as the class-III mucin-specific α4GlcNAc transferase and with review discussion of α1,4GlcNAc-capped core 2 O-glycans on MUC6 (hennet2002thegalactosyltransferasefamily pages 10-11, arai2024theroleof pages 2-4) | Human review literature with mechanistic inference from established glycosyltransferase biochemistry | Moderate; specific donor/acceptor biochemistry was not directly reproduced in retrieved primary excerpts |
| Family/domain context | A4GNT is consistent with a GT32-like, DxD-motif, nucleotide-sugar-dependent Golgi glycosyltransferase evolutionarily related to α1,4-galactosyltransferase (A4GALT/Gb3 synthase); review notes ~40% identity between α4GalT1 and α4GlcNAc transferase (hennet2002thegalactosyltransferasefamily pages 10-11) | Comparative glycosyltransferase review | Moderate-high; family relationship is well supported, but no direct structural paper for A4GNT itself was retrieved |
| Localization/topology | Best-supported annotation is a Golgi-resident type II membrane glycosyltransferase, as expected for mucin O-glycan extension enzymes and consistent with legacy/database annotation; however, this was not directly established in the retrieved excerpts (hennet2002thegalactosyltransferasefamily pages 10-11) | Indirect inference from glycosyltransferase class and legacy annotation | Moderate; likely correct, but evidence here is inferential rather than from a directly retrieved localization experiment |
| Principal biological context | A4GNT acts in the MUC6-positive gastric gland mucin system: MUC6 is a major gland mucin of stomach, and α1,4GlcNAc-capped O-glycans are discussed as characteristic protective glycans in that layer (arai2024theroleof pages 2-4, arai2024theroleof pages 6-7) | 2024 review integrating human and mouse data | High for close functional association with MUC6; exact proportion of all A4GNT activity attributable to MUC6 vs other gland mucins is not quantified here |
| Tissue/cell distribution | αGlcNAc-bearing gland mucin is reported in pyloric gland cells and mucous neck cells of gastric mucosa and Brunner's gland cells of duodenum; in 2019 mouse sections, αGlcNAc immunostaining and related mucin changes were tracked in gastroduodenal mucosa, with sulfomucins abundant in pyloric gland cells and goblet-cell sulfomucins persisting independently of A4gnt/Chst4 status (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6) | Mouse histochemistry/immunohistochemistry, reflecting established gastroduodenal distribution | High for murine distribution; human distribution is likely analogous but was not directly shown in retrieved excerpts |
| Antimicrobial role against H. pylori | α1,4GlcNAc-capped O-glycans are described as a natural antibiotic that inhibits Helicobacter pylori growth, supporting the view that A4GNT contributes to host defense through glycan elaboration of gland mucin (arai2024theroleof pages 2-4) | 2024 review summarizing in vitro evidence from prior studies; human-pathogen context | Moderate-high; strong as a mechanistic model, but the retrieved excerpt is a review summary rather than the original primary assay |
| A4gnt knockout phenotype | A4gnt knockout mice spontaneously develop differentiated-type gastric adenocarcinoma, supporting a tumor-suppressive role for the αGlcNAc mucin pathway; inflammatory genes are implicated in this phenotype (kawakubo2019analysisofa4gnt pages 1-2) | Mouse genetic model | High for mouse phenotype; direct causal extrapolation to human cancer requires caution |
| 2019 sulfomucin double-knockout refinement | In A4gnt/Chst4 double-knockout mice, gastric sulfomucins are eliminated, yet differentiated-type adenocarcinoma still develops; unexpectedly these mice show early severe gastric erosion and later gastritis cystica profunda (GCP), implying sulfomucins preserve mucosal integrity but are not the primary determinant of cancer development in this model (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6) | Mouse double-knockout genetics, histology, qRT-PCR, glycomics | High for this mechanistic refinement in mice |
| 2024 mechanistic update | A 2024 review synthesizes that Muc6−/−, A4gnt−/−, and C1galt1−/− mice share a theme of impaired glycosylation, with Golgi stress/GOLPH3-MAPK signaling proposed as a tumorigenic mechanism in mucin-deficient stomach; loss of αGlcNAc is also discussed with altered MUC1/Src/β-catenin signaling and inflammatory programs (arai2024theroleof pages 6-7, arai2024theroleof pages 4-6) | 2024 authoritative review synthesizing mouse and human studies | Moderate for A4GNT-specific mechanism because the review aggregates related models and not every step is shown specifically for A4GNT in the retrieved excerpts |
| 2024 therapeutic/real-world development | 2024 literature highlights mucin/glycan-targeted strategies in gastric cancer, including MEK inhibition for MUC6-deficient/MAPK-active tumors and lectin-drug conjugates targeting aberrant glycans in mucin-deficient gastric cancers; these are conceptually relevant to A4GNT-loss states because A4GNT is part of the same gastric gland glycosylation axis (arai2024theroleof pages 6-7, arai2024theroleof pages 4-6) | 2024 review of translational and preclinical work | Moderate; promising and mechanistically linked, but not yet an A4GNT-specific approved clinical application |
| Human disease interpretation | Across the retrieved evidence, the most defensible human annotation is that A4GNT supports a protective gastric gland mucin glycan program; loss or dysregulation of this axis is associated with gastric carcinogenesis risk, but the strongest direct causal evidence still comes from mouse genetics and integrated reviews rather than retrieved human-only intervention studies (arai2024theroleof pages 1-2, arai2024theroleof pages 6-7, arai2024theroleof pages 4-6) | Human review literature plus mouse model inference | Moderate-high overall; biologically coherent, but human causality remains less direct than murine evidence |
Table: This table synthesizes the strongest retrieved evidence for human A4GNT/Q9UNA3, separating direct support from inference and highlighting where mouse genetics, review synthesis, or legacy annotation underpin the functional annotation.
The target is A4GNT/alpha4GnT, the alpha1,4-GlcNAc transferase acting on gastric gland mucins. A glycosyltransferase review explicitly identifies alpha4GnT as the human class-III mucin-specific alpha4GlcNAc transferase and reports substantial sequence relationship to alpha4GalT1/A4GALT. The latter transfers galactose to glycolipids and must not be confused with A4GNT, which transfers N-acetylglucosamine in the gland-mucin pathway (hennet2002thegalactosyltransferasefamily pages 10-11).
This literature assignment agrees with the supplied UniProt annotation: Homo sapiens, accession Q9UNA3, glycosyltransferase family 32, with A1-4-glycosyltransferase, nucleotide-diphosphosugar-transferase, and DxD sugar-binding signatures. The domain architecture is therefore coherent with a nucleotide-sugar-dependent glycosyltransferase. However, a solved experimental structure of human A4GNT was not identified in the retrieved evidence; fold-level claims remain family-based inference rather than A4GNT-specific crystallographic proof.
The functional reaction can be summarized as:
UDP-GlcNAc + terminal Gal–R → UDP + GlcNAcα1→4Gal–R
Here, UDP-N-acetylglucosamine is the activated sugar donor and terminal galactose on an O-linked gastric gland-mucin glycan is the acceptor. A4GNT therefore creates a nonreducing terminal alpha1,4-linked GlcNAc cap, rather than polymerizing a repeated carbohydrate chain. The physiologically prominent products are alphaGlcNAc-capped O-glycans associated with MUC6/class-III gastric gland mucin; the 2024 review specifically discusses alpha1,4-GlcNAc-capped core-2 O-glycans in this protective system (hennet2002thegalactosyltransferasefamily pages 10-11, arai2024theroleof pages 2-4).
The strongest genetic validation comes from glycomic analysis of mouse gastric mucin. Seven mass-spectrometric peaks corresponding to alphaGlcNAc-containing neutral O-glycans were detected in wild-type stomach but were completely absent from A4gnt-null stomach. Histochemical alphaGlcNAc reactivity was likewise absent after A4gnt deletion. These results strongly establish that A4gnt is required—and apparently nonredundant—for this gastric glycan terminus in vivo (kawakubo2019analysisofa4gnt pages 3-6).
A4GNT is best described as a gastric gland-mucin O-glycan transferase, not a general cytosolic GlcNAc-transferase. Its physiological acceptors terminate in galactose and occur especially on MUC6-rich gland mucus. “MUC6-specific” should nevertheless be interpreted as dominant biological context rather than absolute proof that no other suitably glycosylated protein can be modified. The retrieved literature establishes close association with class-III/MUC6 mucin but does not provide a complete modern kinetic matrix comparing every candidate glycan and protein acceptor (hennet2002thegalactosyltransferasefamily pages 10-11, arai2024theroleof pages 2-4).
A4GNT is annotated as a Golgi-resident type-II membrane glycosyltransferase: a short cytosolic amino terminus, one transmembrane anchor, and a luminal catalytic domain positioned to encounter secretory-pathway mucins and UDP-sugar substrates. This topology is mechanistically consistent with its role in O-glycan maturation before mucin secretion.
The functional site should therefore be distinguished at two levels:
The retrieved excerpts strongly support the secretory-pathway context but did not reproduce the original A4GNT localization experiment. Thus, Golgi/type-II topology is a high-confidence database and family annotation, whereas the in-vivo glycan product and its tissue distribution have more direct experimental support.
AlphaGlcNAc-bearing gland mucin is concentrated in pyloric gland cells, gastric mucous-neck cells, and duodenal Brunner-gland cells. This is a much narrower functional distribution than that of ubiquitous intracellular O-GlcNAc modification. In mouse tissue, alphaGlcNAc immunohistochemistry and O-glycomics directly confirmed its presence in normal gastroduodenal gland mucus and complete loss after A4gnt deletion (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6).
Within the stomach, MUC5AC and MUC6 form a spatially organized mucus system. MUC5AC predominates in surface/foveolar mucus, whereas MUC6 characterizes deeper gland-type mucus. This organization protects the epithelium from acid, digestive factors, drugs, and microorganisms. A4GNT operates specifically in the MUC6/gland-mucin arm of this system (arai2024theroleof pages 1-2, arai2024theroleof pages 2-4).
A4GNT acts late in secretory mucin O-glycan elaboration, after construction and galactosylation of the underlying O-glycan. Its terminal alphaGlcNAc product changes the biological behavior of the mature mucin and marks the gastric-gland glycan phenotype. This is a biochemical biosynthetic pathway rather than a canonical receptor-mediated signaling cascade.
The MUC6-rich layer is relatively resistant to colonization by H. pylori. In-vitro work summarized in the 2024 review identifies alpha1,4-GlcNAc-capped O-glycans as a natural antibiotic that inhibits H. pylori growth. The same review reports that added GlcNAc can suppress Fusobacterium-mediated gastric epithelial activation, indicating broader relevance of gastric mucin glycans to host–microbiome interactions, although this latter observation does not demonstrate that intact A4GNT products are the sole active species (arai2024theroleof pages 2-4).
Thus, the most precise interpretation is that A4GNT creates a chemical feature of gland mucus that both reinforces ecological separation between bacteria and epithelium and directly restricts at least H. pylori. It does not itself function as an immune receptor or signaling ligand.
A4gnt-null mice spontaneously develop differentiated-type gastric adenocarcinoma, accompanied by increased expression of inflammatory mediators including Ccl2, Il11, and Fgf7. This establishes a tumor-suppressive function for the alphaGlcNAc mucin-glycan program in the mouse stomach (kawakubo2019analysisofa4gnt pages 1-2).
The likely mechanism is multifactorial rather than a single linear pathway:
A 2024 synthesis proposes that impaired glycosylation in A4gnt−/−, Muc6−/−, and C1galt1−/− stomachs converges on stress and tumorigenic programs. Loss of alphaGlcNAc has also been linked to MUC1 carboxy-terminal phosphorylation and galectin-3-dependent recruitment of Src and beta-catenin. Because some elements were established in related mucin-deficiency models, they should be viewed as a pathway-level model, not as proof that every step has been demonstrated directly downstream of A4GNT in human tissue (arai2024theroleof pages 6-7, arai2024theroleof pages 4-6).
The 2019 double-knockout study separated the role of alphaGlcNAc loss from secondary sulfomucin production. A4gnt-null pyloric mucosa overproduced sulfated O-glycans, whereas deletion of both A4gnt and Chst4 eliminated these gastric sulfomucins. Despite sulfomucin loss, double-knockout mice still developed differentiated gastric adenocarcinoma. Sulfomucins therefore are not necessary for tumor formation in this model (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6).
They did, however, protect tissue integrity. Double-knockout mice developed severe gastric erosion by three weeks, followed with aging by gastritis cystica profunda; all examined double-knockout mice had this lesion by 60 weeks. At five weeks, Cxcl1, Cxcl5, Ccl2, and Cxcr2 were significantly elevated relative to A4gnt-only knockouts. The study used approximately six mice per genotype/time point for histopathology and four to six for expression analysis. These data imply that compensatory sulfomucins mitigate erosion and early inflammation but do not correct the primary tumor-promoting consequence of alphaGlcNAc loss (kawakubo2019analysisofa4gnt pages 2-3, kawakubo2019analysisofa4gnt pages 1-2).
Human data support the importance of the broader MUC6/A4GNT glycosylation axis, but direct causality is less complete than in mice. Recent genomic synthesis estimates that approximately 15% of gastric cancers contain MUC6 mutations, with reported frequencies of 9.6% in microsatellite-stable tumors and 18.2% in microsatellite-instability tumors. These statistics concern MUC6, not A4GNT, and should not be misreported as A4GNT mutation prevalence (arai2024theroleof pages 4-6).
Reduced gastric gland-mucin glycans have also been investigated as histopathological risk or progression markers. Nevertheless, current evidence does not establish A4GNT testing as a standard standalone clinical diagnostic, predictive biomarker, or hereditary-cancer test.
The most important recent advance is the mechanistic integration of mucin-core loss and glycosyltransferase loss. The 2024 Cancer Science review highlights a model in which MUC6 deficiency induces Golgi stress, increases GOLPH3, and activates MAPK signaling; A4gnt- and C1galt1-deficient mice show related gastric phenotypes. This shifts interpretation of A4GNT from a simple glycan marker toward a component of a broader mucin-quality-control and epithelial-stress axis (arai2024theroleof pages 6-7, arai2024theroleof pages 4-6).
A 2024 primary study summarized by that review reported that impaired gastric-mucin glycosylation generates therapeutically recognizable glycan states. Banana lectin bound aberrant high-mannose glycans in Muc6-deficient tumors, and a banana-lectin–Pseudomonas aeruginosa exotoxin-A conjugate induced apoptosis in deficient tumor cells. MAPK-active, MUC6-deficient tumors were also proposed as candidates for MEK inhibition (arai2024theroleof pages 6-7).
These advances are relevant to A4GNT loss because A4GNT modifies the same gland-mucin system, but neither strategy is presently an approved A4GNT-specific therapy. The most accurate status is preclinical proof of concept for stratifying mucin/glycan-deficient gastric tumors.
Histopathology and biomarker research. AlphaGlcNAc can be detected with glycan-reactive antibodies such as HIK1083. Its loss can identify disruption of the gastric-gland mucin phenotype and is being studied in gastric and Barrett-associated neoplasia. This remains primarily a pathology/research application rather than a universally standardized clinical assay (kawakubo2019analysisofa4gnt pages 3-6).
Gastric-cancer stratification. Combined analysis of MUC6, alphaGlcNAc/A4GNT products, and broader glycan profiles may define tumors with gland-mucin deficiency, Golgi stress, or MAPK activation. The 2024 literature proposes lectin microarrays as one route toward patient-specific glycan profiling (arai2024theroleof pages 6-7).
Antimicrobial glycan mimetics. Alpha1,4-GlcNAc-capped O-glycans or stable mimetics could in principle exploit the natural anti-H. pylori mechanism. No clinical implementation or efficacy trial was identified in the retrieved evidence (arai2024theroleof pages 2-4).
Targeted therapeutics. MEK inhibitors and lectin–drug conjugates are experimental approaches for selected mucin-deficient tumors. Their relevance to A4GNT must be established prospectively with A4GNT/product-level biomarkers rather than assumed from MUC6 deficiency alone (arai2024theroleof pages 6-7, arai2024theroleof pages 4-6).
High-confidence annotation: A4GNT/Q9UNA3 is the human gastric gland-mucin alpha1,4-N-acetylglucosaminyltransferase. It transfers GlcNAc from UDP-GlcNAc to terminal galactose on mucin O-glycans, generating the characteristic alphaGlcNAc cap. Its principal biological setting is the Golgi of MUC6-producing gastric and duodenal gland cells; its secreted products function in the mucus layer. Mouse knockout and gastric glycomic evidence demonstrate nonredundancy for alphaGlcNAc formation and a protective role against gastric inflammation and tumorigenesis (kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6, hennet2002thegalactosyltransferasefamily pages 10-11).
Moderate-confidence mechanistic extensions: A4GNT loss likely promotes cancer through a combination of microbial dysregulation, chronic injury, underglycosylated mucin signaling, and Golgi-stress/MAPK programs. Several components are supported by related MUC6 and O-glycosylation models rather than direct experiments on human A4GNT-deficient tissue (arai2024theroleof pages 6-7, arai2024theroleof pages 4-6).
Major knowledge gaps: no A4GNT-specific atomic structure was identified; comprehensive modern donor/acceptor kinetics remain limited; human germline or somatic A4GNT effect sizes are not established here; and no approved drug or clinical trial specifically targeting A4GNT deficiency was found.
Arai J, et al. “The role of gastric mucins and mucin-related glycans in gastric cancers.” Cancer Science 115:2853–2861. Received April 23, revised June 22, accepted July 2, 2024; published online in 2024. DOI/URL: https://doi.org/10.1111/cas.16282. This is the principal recent authoritative synthesis for gastric mucin biology, cancer mechanisms, statistics, and emerging therapy (arai2024theroleof pages 1-2, arai2024theroleof pages 6-7, arai2024theroleof pages 2-4, arai2024theroleof pages 4-6).
Kawakubo M, et al. “Analysis of A4gnt Knockout Mice Reveals an Essential Role for Gastric Sulfomucins in Preventing Gastritis Cystica Profunda.” Journal of Histochemistry & Cytochemistry 67:759–770. Accepted June 6, 2019. DOI/URL: https://doi.org/10.1369/0022155419860134. Primary genetic, histological, expression, and glycomic evidence refining the A4gnt-null phenotype (kawakubo2019analysisofa4gnt pages 2-3, kawakubo2019analysisofa4gnt pages 1-2, kawakubo2019analysisofa4gnt pages 3-6).
Hennet T. “The galactosyltransferase family.” Cellular and Molecular Life Sciences 59:1081–1095. July 2002. DOI/URL: https://doi.org/10.1007/s00018-002-8489-4. Provides comparative family context and identifies alpha4GnT as the human class-III mucin-specific alpha4GlcNAc transferase (hennet2002thegalactosyltransferasefamily pages 10-11).
References
(kawakubo2019analysisofa4gnt pages 1-2): Masatomo Kawakubo, Hitomi Komura, Yukinobu Goso, Motohiro Okumura, Yoshiko Sato, Chifumi Fujii, Masaki Miyashita, Nobuhiko Arisaka, Satoru Harumiya, Kazuhiro Yamanoi, Shigenori Yamada, Shigeru Kakuta, Hiroto Kawashima, Michiko N. Fukuda, Minoru Fukuda, and Jun Nakayama. Analysis of a4gnt knockout mice reveals an essential role for gastric sulfomucins in preventing gastritis cystica profunda. Journal of Histochemistry & Cytochemistry, 67:759-770, Jun 2019. URL: https://doi.org/10.1369/0022155419860134, doi:10.1369/0022155419860134. This article has 7 citations and is from a peer-reviewed journal.
(hennet2002thegalactosyltransferasefamily pages 10-11): T. Hennet. The galactosyltransferase family. Cellular and Molecular Life Sciences CMLS, 59:1081-1095, Jul 2002. URL: https://doi.org/10.1007/s00018-002-8489-4, doi:10.1007/s00018-002-8489-4. This article has 267 citations.
(kawakubo2019analysisofa4gnt pages 3-6): Masatomo Kawakubo, Hitomi Komura, Yukinobu Goso, Motohiro Okumura, Yoshiko Sato, Chifumi Fujii, Masaki Miyashita, Nobuhiko Arisaka, Satoru Harumiya, Kazuhiro Yamanoi, Shigenori Yamada, Shigeru Kakuta, Hiroto Kawashima, Michiko N. Fukuda, Minoru Fukuda, and Jun Nakayama. Analysis of a4gnt knockout mice reveals an essential role for gastric sulfomucins in preventing gastritis cystica profunda. Journal of Histochemistry & Cytochemistry, 67:759-770, Jun 2019. URL: https://doi.org/10.1369/0022155419860134, doi:10.1369/0022155419860134. This article has 7 citations and is from a peer-reviewed journal.
(arai2024theroleof pages 2-4): Junya Arai, Yoku Hayakawa, Hiroaki Tateno, Hiroaki Fujiwara, Masato Kasuga, and Mitsuhiro Fujishiro. The role of gastric mucins and mucin‐related glycans in gastric cancers. Cancer Science, 115:2853-2861, Jul 2024. URL: https://doi.org/10.1111/cas.16282, doi:10.1111/cas.16282. This article has 27 citations and is from a peer-reviewed journal.
(arai2024theroleof pages 6-7): Junya Arai, Yoku Hayakawa, Hiroaki Tateno, Hiroaki Fujiwara, Masato Kasuga, and Mitsuhiro Fujishiro. The role of gastric mucins and mucin‐related glycans in gastric cancers. Cancer Science, 115:2853-2861, Jul 2024. URL: https://doi.org/10.1111/cas.16282, doi:10.1111/cas.16282. This article has 27 citations and is from a peer-reviewed journal.
(arai2024theroleof pages 4-6): Junya Arai, Yoku Hayakawa, Hiroaki Tateno, Hiroaki Fujiwara, Masato Kasuga, and Mitsuhiro Fujishiro. The role of gastric mucins and mucin‐related glycans in gastric cancers. Cancer Science, 115:2853-2861, Jul 2024. URL: https://doi.org/10.1111/cas.16282, doi:10.1111/cas.16282. This article has 27 citations and is from a peer-reviewed journal.
(arai2024theroleof pages 1-2): Junya Arai, Yoku Hayakawa, Hiroaki Tateno, Hiroaki Fujiwara, Masato Kasuga, and Mitsuhiro Fujishiro. The role of gastric mucins and mucin‐related glycans in gastric cancers. Cancer Science, 115:2853-2861, Jul 2024. URL: https://doi.org/10.1111/cas.16282, doi:10.1111/cas.16282. This article has 27 citations and is from a peer-reviewed journal.
(kawakubo2019analysisofa4gnt pages 2-3): Masatomo Kawakubo, Hitomi Komura, Yukinobu Goso, Motohiro Okumura, Yoshiko Sato, Chifumi Fujii, Masaki Miyashita, Nobuhiko Arisaka, Satoru Harumiya, Kazuhiro Yamanoi, Shigenori Yamada, Shigeru Kakuta, Hiroto Kawashima, Michiko N. Fukuda, Minoru Fukuda, and Jun Nakayama. Analysis of a4gnt knockout mice reveals an essential role for gastric sulfomucins in preventing gastritis cystica profunda. Journal of Histochemistry & Cytochemistry, 67:759-770, Jun 2019. URL: https://doi.org/10.1369/0022155419860134, doi:10.1369/0022155419860134. This article has 7 citations and is from a peer-reviewed journal.