GO:0003829 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0003829 describes the enzymatic activity that adds N-acetylglucosamine in a beta-1,6 linkage to the core 1 structure of O-glycans, forming core 2.
• This activity is primarily carried out by the GCNT family enzymes, especially GCNT1 (core 2 beta-1,6-N-acetylglucosaminyltransferase-1, C2GnT-1).
• Core 2 O-glycans are critical for selectin ligand formation, immune cell trafficking, and cancer cell motility.
• GCNT1-mediated core 2 branching on CD43 is a sensitive indicator of Notch signaling in activated T cells.
• Dysregulation of this activity is linked to leukemia, lymphoma, testicular germ cell tumors, pancreatic cancer, and melanoma progression.
• CRISPR knockout, point mutation, knock-in, and overexpression models enable precise dissection of GO:0003829-related gene function in disease and immunity.
Description
GO:0003829, beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity, is a molecular function that catalyzes the addition of N-acetyl-alpha-D-glucosamine to the core 1 structure of O-glycans, forming the core 2 branch. This reaction is essential for the biosynthesis of complex O-linked glycans on cell surface glycoproteins, which modulate cell-cell interactions, receptor signaling, and immune recognition. The enzyme activity is encoded by the GCNT family of glycosyltransferases, with GCNT1 being the predominant core 2 beta-1,6-N-acetylglucosaminyltransferase in humans. Researchers study GO:0003829 because core 2 O-glycans are key determinants of selectin-mediated leukocyte adhesion and are frequently dysregulated in cancer and immune disorders. For example, core 2 branching on P-selectin glycoprotein ligand-1 (PSGL-1) is required for high-affinity binding to P-selectin, a critical step in inflammation and metastasis. In T cells, GCNT1-mediated O-glycosylation of CD43 serves as a sensitive readout of Notch signaling, linking glycosylation to developmental pathways. This article provides a comprehensive overview of GO:0003829, covering its definition, biological roles, key genes, disease associations, and modern research methods including CRISPR-based models. All statements are grounded in published literature to support researchers in glycobiology, immunology, and oncology.
beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity At A Glance
| GO ID | GO:0003829 |
|---|---|
| GO term | beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity |
| Ontology | molecular_function |
| Synonym | core 2 acetylglucosaminyltransferase activity; beta6-N-acetylglucosaminyltransferase activity; uridine diphosphoacetylglucosamine-mucin beta-(1,6)-acetylglucosaminyltransferase activity |
| Major function | Adds N-acetylglucosamine in beta-1,6 linkage to core 1 O-glycans, forming core 2 structures on glycoproteins |
| Substrates | UDP-N-acetyl-D-glucosamine and beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl-R (core 1 O-glycan) |
| Products | UDP and beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-D-galactosaminyl-R (core 2 O-glycan) |
| Major enzyme | GCNT1 (core 2 beta-1,6-N-acetylglucosaminyltransferase-1) |
| Cellular location | Golgi apparatus (glycosyltransferase) |
What Is GO:0003829?
GO:0003829 is defined as the catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl-R = UDP + beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-D-galactosaminyl-R. In simpler terms, this enzyme transfers N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to the core 1 O-glycan structure (Gal beta-1,3-GalNAc-R), creating a beta-1,6 branch that forms the core 2 structure. This activity is synonymous with core 2 acetylglucosaminyltransferase activity and is essential for the synthesis of branched O-glycans on glycoproteins.
Why Is beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Important in Cell Biology?
GO:0003829 is important because core 2 O-glycan branching is a critical post-translational modification that regulates protein function, cell adhesion, and signal transduction. This activity is essential for the biosynthesis of selectin ligands such as PSGL-1, which mediate leukocyte rolling and extravasation during inflammation and immune surveillance. In cancer, core 2 O-glycans contribute to tumor cell motility, metastasis, and chemoresistance, making this enzyme activity a potential therapeutic target.
• Core 2 O-glycans are required for P-selectin glycoprotein ligand-1 (PSGL-1) binding to P-selectin, a key step in leukocyte adhesion and inflammation.
• GCNT1-mediated core 2 branching on CD43 is a sensitive indicator of Notch signaling in activated T cells, linking glycosylation to T cell development.
• Core 2 N-acetylglucosaminyltransferase-1 expression induces aggressive potential in testicular germ cell tumors.
• Haploinsufficiency of C2GnT-I renders T lymphoma cells resistant to cell death, implicating core 2 glycans in apoptosis regulation.
• GCNT3 (beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3) increases MCAM stability and enhances S100A8/A9-mediated cancer motility.
• FUT3-B3GNT3 interaction promotes pancreatic cancer progression and chemoresistance via NF-kB signaling mediated autophagy.
• Core 2 branching is essential for sialyl-Lewis x expression in human precursor B cells, affecting immune cell trafficking.
• A multipotential beta-1,6-N-acetylglucosaminyltransferase is encoded by bovine herpesvirus type 4, highlighting viral exploitation of this activity.
• Dysregulated O-glycosylation is a hallmark of many cancers and immune disorders, making GO:0003829 a research priority.
What Happens During beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity?
Substrate Recognition and Binding
In simple terms: The enzyme grabs the core 1 O-glycan and a sugar donor molecule.
The enzyme recognizes the core 1 O-glycan structure, beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl-R, on glycoproteins and binds the donor substrate UDP-N-acetyl-D-glucosamine. This initial binding is mediated by the enzyme's catalytic domain, which is located in the Golgi lumen. The specificity for the core 1 acceptor distinguishes this activity from other glycosyltransferases.
Catalytic Transfer of N-Acetylglucosamine
In simple terms: The enzyme attaches a sugar molecule to the core 1 structure, creating a branch.
The enzyme catalyzes the transfer of N-acetyl-alpha-D-glucosamine from UDP-N-acetyl-D-glucosamine to the C6 hydroxyl group of the N-acetyl-D-galactosamine residue in the core 1 structure, forming a beta-1,6 linkage. This reaction produces UDP and the core 2 O-glycan structure, beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-D-galactosaminyl-R. The core 2 branch is a prerequisite for further elongation and sialylation, such as sialyl-Lewis x formation.
Formation of Core 2 O-Glycans
In simple terms: The new branch allows the glycan to become more complex and functional.
The addition of the beta-1,6-linked GlcNAc creates the core 2 structure, which serves as a scaffold for additional glycosylation steps, including sialylation, fucosylation, and polylactosamine extension. Core 2 O-glycans are critical for the function of selectin ligands like PSGL-1, where they present sialyl-Lewis x epitopes that bind to selectins. This branching also affects the stability and interactions of cell surface receptors such as MCAM.
Biological Consequences in Immune Cells
In simple terms: The branched sugars help immune cells stick to blood vessels and communicate.
In activated T cells, GCNT1-mediated core 2 O-glycosylation of CD43 is a sensitive indicator of Notch signaling, influencing T cell activation and differentiation. Core 2 branching on PSGL-1 is required for P-selectin binding, which mediates the initial tethering and rolling of leukocytes on activated endothelium during inflammation. In precursor B cells, core 2 branching regulates sialyl-Lewis x expression, affecting cell migration and homing.
Role in Cancer Progression
In simple terms: Abnormal sugar branching can make cancer cells more aggressive.
In testicular germ cell tumors, core 2 N-acetylglucosaminyltransferase-1 expression induces aggressive potential, promoting invasion and metastasis. GCNT3 increases MCAM stability, enhancing S100A8/A9-mediated cancer motility in melanoma and other cancers. FUT3-B3GNT3 interaction promotes pancreatic cancer progression and chemoresistance via NF-kB signaling mediated autophagy. These findings highlight GO:0003829 as a driver of malignant phenotypes.
Key Genes Involved in GO:0003829 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity
The following genes encode enzymes or related proteins that carry out or regulate beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity (GO:0003829) and its downstream functions.
| Gene | Major Role | Research Relevance |
|---|---|---|
| GCNT1 | Core 2 beta-1,6-N-acetylglucosaminyltransferase-1; primary enzyme for core 2 O-glycan synthesis | Regulates PSGL-1 binding, T cell development, and lymphoma apoptosis |
| GCNT3 | Core 2 beta-1,6-N-acetylglucosaminyltransferase-3; increases MCAM stability | Promotes cancer motility and metastasis via S100A8/A9 |
| GCNT2 | Core 2 beta-1,6-N-acetylglucosaminyltransferase-2; involved in O-glycan branching | Not a major regulator of sialyl-Lewis x in precursor B cells |
| B3GNT3 | Beta-1,3-N-acetylglucosaminyltransferase; interacts with FUT3 | Promotes pancreatic cancer progression and chemoresistance |
| FUT3 | Fucosyltransferase 3; interacts with B3GNT3 | Modulates NF-kB signaling and autophagy in pancreatic cancer |
| PSGL-1 (SELPLG) | P-selectin glycoprotein ligand-1; requires core 2 O-glycans for binding | Critical for leukocyte adhesion and inflammation |
| CD43 (SPN) | Sialomucin; O-glycosylated by GCNT1 | Sensitive indicator of Notch signaling in activated T cells |
| MCAM | Melanoma cell adhesion molecule; stabilized by GCNT3 | Enhances S100A8/A9-mediated cancer motility |
| S100A8/A9 | Calcium-binding proteins; mediate cancer motility | Ligands that promote MCAM-dependent migration |
| C2GnT-I (GCNT1 alias) | Core 2 beta-1,6-N-acetylglucosaminyltransferase-1 | Haploinsufficiency renders T lymphoma cells resistant to cell death |
| Notch receptors | Signaling proteins that induce GCNT1-mediated CD43 glycosylation | Link glycosylation to T cell activation |
| NF-kB | Transcription factor activated by FUT3-B3GNT3 interaction | Mediates autophagy and chemoresistance in pancreatic cancer |
| Bovine herpesvirus 4 beta-1,6-N-acetylglucosaminyltransferase | Viral enzyme with multipotential activity | Model for viral exploitation of glycosylation |
| Selectins (P-, E-, L-selectin) | Adhesion molecules that bind core 2 O-glycans | Mediate leukocyte rolling and extravasation |
| Sialyl-Lewis x | Glycan epitope synthesized downstream of core 2 branching | Regulates immune cell trafficking and cancer metastasis |
How Is beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Regulated?
The activity of beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase is regulated at multiple levels. Transcription of GCNT1 is induced by Notch signaling in activated T cells, leading to increased core 2 O-glycosylation of CD43. In cancer, GCNT3 expression is modulated by interactions with FUT3, which promotes NF-kB signaling and autophagy, contributing to chemoresistance. Additionally, the enzyme activity can be influenced by substrate availability and Golgi localization, as well as by post-translational modifications, although specific mechanisms remain to be fully elucidated.
beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| GCNT3 | Melanoma progression and metastasis | GCNT3 knockout melanoma cells; overexpression in cancer cell lines |
| GCNT1 | T lymphoma resistance to cell death | GCNT1 haploinsufficient T lymphoma cells; CRISPR knockout |
| GCNT1 | Testicular germ cell tumor aggressiveness | GCNT1 overexpression in germ cell tumor lines; knockout models |
| B3GNT3/FUT3 | Pancreatic cancer chemoresistance | B3GNT3 or FUT3 knockout pancreatic cancer cells; knock-in of mutants |
| PSGL-1 (SELPLG) | Leukocyte adhesion and inflammation | PSGL-1 point mutants lacking core 2 glycosylation; knock-in mice |
Cancer Progression and Metastasis
Dysregulation of GO:0003829 is strongly associated with cancer. GCNT3 increases MCAM stability, enhancing S100A8/A9-mediated cancer motility in melanoma and other malignancies. In testicular germ cell tumors, core 2 N-acetylglucosaminyltransferase-1 expression induces aggressive potential, correlating with poor prognosis. FUT3-B3GNT3 interaction promotes pancreatic cancer progression and chemoresistance via NF-kB signaling mediated autophagy. These findings suggest that core 2 O-glycan branching is a driver of malignant phenotypes and a potential therapeutic target.
Leukemia and Lymphoma
Haploinsufficiency of C2GnT-I (GCNT1) renders T lymphoma cells resistant to cell death, indicating that core 2 O-glycans are involved in apoptosis regulation. This suggests that loss of GO:0003829 activity may contribute to lymphoma pathogenesis by promoting survival of malignant T cells. Additionally, GCNT1-mediated core 2 branching on CD43 is a sensitive indicator of Notch signaling in activated T cells, linking glycosylation to T cell development and leukemogenesis.
Immune and Inflammatory Disorders
Core 2 beta-1,6-N-acetylglucosaminyltransferase activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin, a key step in leukocyte adhesion and inflammation. Defects in this activity could impair immune cell trafficking and contribute to inflammatory diseases. In precursor B cells, core 2 branching regulates sialyl-Lewis x expression, affecting cell migration and homing. Thus, GO:0003829 is essential for normal immune function and its dysregulation may underlie immune disorders.
Viral Pathogenesis
A multipotential beta-1,6-N-acetylglucosaminyltransferase is encoded by bovine herpesvirus type 4, demonstrating that viruses can exploit this activity to modify host glycans and evade immune responses. This highlights the broader biological significance of GO:0003829 beyond human physiology.
From beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of GCNT1 affect T cell development and Notch signaling? | GCNT1 knockout mice or CRISPR knockout in T cell lines |
| How does GCNT3 stabilize MCAM and promote cancer motility? | GCNT3 knockout melanoma cells; overexpression and tagged knock-in |
| What is the role of core 2 O-glycans in PSGL-1 binding to P-selectin? | PSGL-1 point mutations at glycosylation sites; knock-in mice |
| Does B3GNT3-FUT3 interaction drive chemoresistance in pancreatic cancer? | B3GNT3 knockout and FUT3 overexpression in pancreatic cancer cells |
| Can GCNT1 haploinsufficiency protect against T lymphoma? | GCNT1 heterozygous knockout mice; lymphoma cell lines |
| Does core 2 branching regulate sialyl-Lewis x in B cells? | GCNT1 knockout B cell lines; CRISPR point mutations |
How to Study the beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Glycosyltransferase activity assay | Enzymatic transfer of GlcNAc to core 1 acceptor | Validation of GCNT1/GCNT3 activity |
| Mass spectrometry glycomics | O-glycan structures and branching | Profiling core 2 O-glycans in cells |
| Flow cytometry with lectins | Cell surface glycan epitopes | Detection of sialyl-Lewis x and core 2 |
| Western blot | Protein expression and stability | MCAM stabilization by GCNT3 |
| CRISPR knockout screening | Gene function in glycosylation pathways | Identifying regulators of core 2 O-glycans |
| RNA-seq | Transcriptional changes in GCNT genes | Notch signaling-induced GCNT1 expression |
| Immunoprecipitation | Protein-protein interactions | FUT3-B3GNT3 interaction |
| Autophagy flux assay | Autophagic activity | Chemoresistance mediated by NF-kB |
Glycosyltransferase Activity Assays
Enzymatic activity of GO:0003829 can be measured using radioactive or fluorescent donor substrates (UDP-GlcNAc) and acceptor glycans, followed by chromatographic separation of products. These assays are essential for validating the catalytic function of GCNT enzymes and their mutants.
Glycan Profiling by Mass Spectrometry
Mass spectrometry-based glycomics allows detailed structural analysis of O-glycans, including core 2 structures, from cell lysates or secreted glycoproteins. This method can quantify changes in core 2 branching upon genetic manipulation of GCNT genes.
Flow Cytometry and Lectin Staining
Flow cytometry using lectins or antibodies specific for core 2 O-glycans (e.g., sialyl-Lewis x) can assess cell surface glycosylation changes in live cells. This is useful for studying immune cell populations and cancer cells.
CRISPR-Based Genetic Screens
Pooled CRISPR knockout screens targeting glycosyltransferase genes can identify regulators of core 2 O-glycan expression and function. These screens are powerful for discovering novel genes in the GO:0003829 pathway.
How CRISPR Can Be Used to Study GO:0003829 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity
Knockout
CRISPR knockout of GCNT1, GCNT3, or B3GNT3 eliminates beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity, allowing researchers to study loss-of-function phenotypes such as impaired PSGL-1 binding, reduced cancer cell motility, and altered T cell signaling. Knockout models are essential for validating the causal role of these genes in disease.
Point Mutation
CRISPR point mutations can be introduced into the catalytic domain of GCNT enzymes to dissect substrate binding and catalytic residues without completely abolishing protein expression. Such models help distinguish between enzymatic activity and non-catalytic functions.
Knock-in
Knock-in of tagged GCNT1 or GCNT3 (e.g., FLAG, HA) enables precise tracking of protein localization, interaction partners, and stability in live cells. Knock-in of disease-associated mutations can model human glycosylation disorders.
Overexpression
CRISPR activation or lentiviral overexpression of GCNT1, GCNT3, or B3GNT3 can mimic the upregulated state observed in cancers, promoting core 2 O-glycan synthesis and enhancing malignant phenotypes such as motility and chemoresistance. Overexpression models are useful for gain-of-function studies.
How EDITGENE Supports beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Research
Researchers studying beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in glycosylation-dependent phenotypes, immune regulation, or cancer progression. EDITGENE provides end-to-end CRISPR services to generate precisely engineered cell models that answer these questions.
Contact EDITGENE today to design your custom CRISPR model for beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity research.
Frequently Asked Questions About beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity
What is beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity?
It is the enzymatic activity (GO:0003829) that adds N-acetylglucosamine in a beta-1,6 linkage to core 1 O-glycans, forming core 2 structures on glycoproteins.
What genes are involved in GO:0003829?
The main genes are GCNT1, GCNT3, and GCNT2, which encode core 2 beta-1,6-N-acetylglucosaminyltransferases. Other related genes include B3GNT3 and FUT3.
What is the function of core 2 O-glycans?
Core 2 O-glycans are essential for selectin ligand formation, immune cell trafficking, and cancer cell motility.
How is GCNT1 related to T cell development?
GCNT1-mediated core 2 O-glycosylation of CD43 is a sensitive indicator of Notch signaling in activated T cells.
What diseases are associated with core 2 beta-1,6-N-acetylglucosaminyltransferase activity?
Dysregulation is linked to leukemia, lymphoma, testicular germ cell tumors, pancreatic cancer, and melanoma.
How can I study GO:0003829 in the lab?
Common methods include glycosyltransferase activity assays, mass spectrometry glycomics, flow cytometry, and CRISPR knockout models.
What is the role of GCNT3 in cancer?
GCNT3 increases MCAM stability and enhances S100A8/A9-mediated cancer motility, promoting metastasis.
Does GCNT1 affect lymphoma cell death?
Haploinsufficiency of C2GnT-I (GCNT1) renders T lymphoma cells resistant to cell death.
How does FUT3-B3GNT3 interaction affect pancreatic cancer?
It promotes pancreatic cancer progression and chemoresistance via NF-kB signaling mediated autophagy.
What CRISPR models are available for studying this activity?
Knockout, point mutation, knock-in, and overexpression models can be generated for GCNT1, GCNT3, B3GNT3, and FUT3 to dissect their roles.
Conclusion
GO:0003829, beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity, is a fundamental enzymatic function that drives core 2 O-glycan biosynthesis, impacting immune cell adhesion, T cell signaling, and cancer progression. The GCNT family enzymes, particularly GCNT1 and GCNT3, are key players whose dysregulation contributes to leukemia, lymphoma, testicular germ cell tumors, pancreatic cancer, and melanoma. Advances in CRISPR-based models and glycomic technologies are enabling precise dissection of this activity in health and disease. EDITGENE offers comprehensive services to support researchers in generating knockout, point mutation, knock-in, and overexpression models, as well as CRISPR library screening and bioinformatics, to accelerate discoveries in glycobiology and oncology.
References
- 1. Sumardika IW et al.. 2018. β-1,3-Galactosyl-O-Glycosyl-Glycoprotein β-1,6-N-Acetylglucosaminyltransferase 3 Increases MCAM Stability, Which Enhances S100A8/A9-Mediated Cancer Motility.. Oncol Res 26(3):431-444 PMID: 28923134
- 2. Kumar R et al.. 1996. Core2 beta-1,6-N-acetylglucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin.. Blood 88(10):3872-9 PMID: 8916952
- 3. Jin L et al.. 2025. FUT3-B3GNT3 interaction promotes pancreatic cancer progression and chemoresistance via NF-κB signaling mediated autophagy.. Eur J Med Res 30(1):1223 PMID: 41366466
- 4. Kikuchi J et al.. 2005. Not core 2 beta 1,6-N-acetylglucosaminyltransferase-2 or -3 but -1 regulates sialyl-Lewis x expression in human precursor B cells.. Glycobiology 15(3):271-80 PMID: 15483269
- 5. Vanderplasschen A et al.. 2000. A multipotential beta -1,6-N-acetylglucosaminyl-transferase is encoded by bovine herpesvirus type 4.. Proc Natl Acad Sci U S A 97(11):5756-61 PMID: 10811884
- 6. Perkey E et al.. 2020. GCNT1-Mediated O-Glycosylation of the Sialomucin CD43 Is a Sensitive Indicator of Notch Signaling in Activated T Cells.. J Immunol 204(6):1674-1688 PMID: 32060138
- 7. Cabrera PV et al.. 2006. Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death.. Blood 108(7):2399-406 PMID: 16778138
- 8. Hatakeyama S et al.. 2010. Core 2 N-acetylglucosaminyltransferase-1 expression induces aggressive potential of testicular germ cell tumor.. Int J Cancer 127(5):1052-9 PMID: 20017138
