GO:0009225 nucleotide-sugar metabolic process: Glycosylation Pathway, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0009225 nucleotide-sugar metabolic process describes the cellular reactions and pathways that produce and interconvert nucleotide-sugars, the activated sugar donors used for glycosylation.
• Nucleotide-sugars such as UDP-GlcNAc, GDP-mannose, UDP-galactose and CMP-sialic acid are the substrates of glycosyltransferases in the endoplasmic reticulum and Golgi apparatus [1,4].
• Defects in nucleotide-sugar metabolism and transport cause congenital disorders of glycosylation, a growing group of inherited metabolic diseases with multisystem phenotypes.
• Nucleotide-sugar availability is a metabolic checkpoint: glycometabolic stress can alter N-glycosylation and activate Notch signaling in cancer cells.
• In bioprocessing, media components such as raffinose and suramin modulate nucleotide-sugar pools and the glycosylation profile of recombinant proteins [6,7].
• CRISPR knockout, point-mutation, knock-in and overexpression models are essential to test causality of nucleotide-sugar pathway genes in disease and bioproduction [2,8].
Description
Nucleotide-sugar metabolic process (GO:0009225) is the set of cellular chemical reactions and pathways involving nucleotide-sugars, defined as any nucleotide-carbohydrate in which the distal phosphoric residue of a nucleoside 5'-diphosphate is in glycosidic linkage with a monosaccharide or monosaccharide derivative. In practical terms, this process generates and interconverts activated sugar donors such as UDP-N-acetylglucosamine, GDP-mannose, UDP-galactose and CMP-sialic acid, which are the substrates used by glycosyltransferases during glycosylation. Because glycosyltransferases cannot use free monosaccharides, the nucleotide-sugar metabolic process is the metabolic gateway that supplies the endoplasmic reticulum and Golgi apparatus with activated sugars for N-glycan, O-glycan, glycolipid and proteoglycan biosynthesis [1,4]. For researchers, GO:0009225 is a convergence point between central carbon metabolism, nucleotide metabolism and the secretory pathway. The pathway includes enzymes that interconvert sugar-1-phosphates and nucleotide-sugars, nucleotide-sugar transporters that import donors into the endoplasmic reticulum and Golgi lumen, and accessory reactions that regenerate cofactors [2,3]. Disruption of these steps changes the glycan structures displayed on cell surfaces and secreted proteins, which affects cell signaling, protein stability and immune recognition [2,5]. Interest in nucleotide-sugar metabolism has increased because congenital disorders of glycosylation are now recognized as a broad clinical spectrum, and because glycoengineering of biotherapeutic-producing cells depends on controlling nucleotide-sugar pools [2,6,8]. This article summarizes the definition, mechanism, key genes, disease links and experimental methods for studying GO:0009225, with an emphasis on CRISPR-based functional models.
nucleotide-sugar metabolic process At A Glance
| GO ID | GO:0009225 |
|---|---|
| GO term | nucleotide-sugar metabolic process |
| Ontology | biological_process |
| Synonym | nucleotide-sugar metabolism |
| Major function | Production, interconversion and supply of activated sugar donors for glycosylation and other biosynthetic pathways [1,4] |
| Key substrates | UDP-GlcNAc, UDP-Glc, UDP-Gal, GDP-Man, GDP-Fuc, CMP-sialic acid [1,4] |
| Key enzymes | Sugar-1-phosphate nucleotidyltransferases, epimerases, N-acetyltransferases, nucleotide-sugar transporters [1,2,3] |
| Subcellular location | Cytosol, nucleus, endoplasmic reticulum and Golgi apparatus [3,4] |
| Disease relevance | Congenital disorders of glycosylation and cancer-associated glycometabolic stress [2,5] |
What Is GO:0009225?
GO:0009225 nucleotide-sugar metabolic process is a biological process ontology term covering the cellular chemical reactions and pathways involving nucleotide-sugars. A nucleotide-sugar is a nucleotide-carbohydrate in which the distal phosphoric residue of a nucleoside 5'-diphosphate is glycosidically linked to a monosaccharide or monosaccharide derivative. The term therefore includes biosynthetic reactions that form nucleotide-sugars, interconversion reactions that equilibrate sugar epimers and N-acetylated forms, and reactions that consume or regenerate these activated donors. It is distinct from glycosylation itself, which is the transfer of sugars to acceptor molecules by glycosyltransferases.
Why Is nucleotide-sugar metabolic process Important in Cell Biology?
Nucleotide-sugar metabolism is important because it determines the availability of activated sugar donors for every major glycosylation pathway, and therefore controls the structure and function of glycoproteins, glycolipids and proteoglycans on the cell surface and in secretions [1,4]. Because glycosylation influences protein folding, trafficking, receptor signaling and immune recognition, changes in nucleotide-sugar pools can have broad physiological consequences [2,5]. In biotechnology, the same pathway controls the glycan profile, efficacy and safety of recombinant therapeutic proteins produced in mammalian cells [6,7,8].
• Supplies activated sugar donors such as UDP-GlcNAc, GDP-mannose and CMP-sialic acid for glycosyltransferase reactions.
• Links central carbon and nucleotide metabolism to the secretory pathway and cell-surface glycan display.
• Mutations in nucleotide-sugar synthesis and transport genes cause congenital disorders of glycosylation with multisystem phenotypes.
• Altered nucleotide-sugar flux can change N-glycosylation and activate Notch signaling in cancer cells.
• Nucleotide-sugar transporters such as SLC35 family members control donor import into the endoplasmic reticulum and Golgi lumen.
• Media supplements such as raffinose can shift high-mannose glycan formation in cultured cells.
• Additives such as suramin can influence glycosylation of Fc-fusion proteins in CHO cells.
• Machine learning-guided bioprocess optimization increasingly targets glycosylation and nucleotide-sugar metabolism.
• Nucleotide-sugar pathways are attractive targets for glycoengineering of therapeutic antibodies and enzymes [4,8].
• CRISPR screens can identify nucleotide-sugar metabolic genes that modify glycan-dependent phenotypes [2,8].
What Happens During nucleotide-sugar metabolic process?
Sugar activation and nucleotide-sugar biosynthesis
In simple terms: Cells attach a sugar phosphate to a nucleotide to make an activated sugar that enzymes can transfer.
The first stage of nucleotide-sugar metabolism converts monosaccharides and sugar-1-phosphates into nucleotide-sugars. Sugar-1-phosphate nucleotidyltransferases catalyze reactions in which a nucleoside triphosphate reacts with a sugar-1-phosphate to form a nucleotide-sugar and pyrophosphate. These reactions produce donors such as UDP-glucose, UDP-N-acetylglucosamine, GDP-mannose and CMP-sialic acid, which are the substrates recognized by glycosyltransferases. Because glycosyltransferases use nucleotide-sugars rather than free sugars, this activation step is the committed entry into glycosylation pathways [1,4].
Interconversion and epimerization of nucleotide-sugars
In simple terms: Cells can remodel one activated sugar into another by flipping or modifying chemical groups.
After biosynthesis, nucleotide-sugars are interconverted by epimerases, N-acetyltransferases and related enzymes. For example, UDP-glucose and UDP-galactose are interconverted by UDP-galactose 4-epimerase, and UDP-N-acetylglucosamine can be converted to UDP-N-acetylgalactosamine and CMP-sialic acid through multi-step pathways. These interconversion reactions allow a limited set of sugar precursors to supply the diverse donor pool required for different glycan structures [1,4]. The balance of these reactions determines which glycans can be assembled in a given cell type or metabolic state.
Transport of nucleotide-sugars into the ER and Golgi lumen
In simple terms: Activated sugars are carried from the cytosol into the compartments where glycosylation happens.
Most nucleotide-sugars are synthesized in the cytosol, but glycosyltransferases act in the lumen of the endoplasmic reticulum and Golgi apparatus. Nucleotide-sugar transporters of the SLC35 family mediate the exchange of nucleotide-sugars across these membranes. Recent work has shown that human SLC35B1 mediates stepwise ATP translocation into the endoplasmic reticulum, highlighting the importance of nucleotide transport in the secretory pathway. Defects in nucleotide-sugar transport can cause glycosylation disorders even when cytosolic synthesis is intact.
Donor utilization and feedback in glycosylation
In simple terms: Once inside the ER or Golgi, activated sugars are used to build glycans, and the cell adjusts production to match demand.
In the final stage, nucleotide-sugars are consumed by glycosyltransferases that transfer the sugar moiety to proteins, lipids or growing glycans, releasing the nucleotide diphosphate or monophosphate [1,4]. The released nucleotides are recycled, and the resulting nucleotide-sugar pools are subject to feedback regulation and metabolic crosstalk. When donor supply is limiting or excessive, glycan structures change, which can alter protein folding, receptor signaling and cell behavior. This coupling between nucleotide-sugar metabolism and glycosylation output is a key reason the pathway is studied in disease and bioprocessing contexts [2,8].
Key Genes Involved in GO:0009225 nucleotide-sugar metabolic process
The following genes and gene families encode enzymes, transporters and regulators that carry out or control nucleotide-sugar metabolic process (GO:0009225).
| Gene | Major Role | Research Relevance |
|---|---|---|
| UAP1 | UDP-N-acetylglucosamine pyrophosphorylase; synthesizes UDP-GlcNAc | Target for altering O-GlcNAc and N-glycan precursor supply [1,4] |
| GFPT1 | Glutamine--fructose-6-phosphate transaminase; rate-limiting step in hexosamine pathway | Links glucose metabolism to UDP-GlcNAc production [1,5] |
| GFPT2 | Glutamine--fructose-6-phosphate transaminase 2; hexosamine pathway isoform | Cancer and metabolic studies of glycometabolic stress |
| PGM1 | Phosphoglucomutase 1; interconverts glucose-6-phosphate and glucose-1-phosphate | Congenital disorder of glycosylation and glycogen metabolism |
| PGM3 | Phosphoglucomutase 3; required for UDP-GlcNAc synthesis | Congenital disorder of glycosylation with immune phenotypes |
| GALE | UDP-galactose 4-epimerase; interconverts UDP-Gal and UDP-Glc | Galactosemia and glycosylation studies |
| GALK1 | Galactokinase 1; phosphorylates galactose | Galactose metabolism and nucleotide-sugar precursor supply |
| UGP2 | UDP-glucose pyrophosphorylase 2; synthesizes UDP-glucose | Glycogen and glycosylation precursor studies [1,2] |
| GMPPA | GDP-mannose pyrophosphorylase A; GDP-mannose synthesis | Congenital disorders of glycosylation |
| GMPPB | GDP-mannose pyrophosphorylase B; GDP-mannose synthesis | Muscle and neuronal glycosylation disorders |
| SLC35A1 | CMP-sialic acid transporter | Sialylation defects and congenital disorders of glycosylation [2,3] |
| SLC35A2 | UDP-galactose transporter | Congenital disorder of glycosylation and epilepsy [2,3] |
| SLC35B1 | ER ATP translocator linked to nucleotide metabolism | ER nucleotide transport and secretory pathway studies |
| SLC35C1 | GDP-fucose transporter | Leukocyte adhesion deficiency type II [2,3] |
| FUT8 | Fucosyltransferase 8; uses GDP-fucose for core fucosylation | Antibody glycoengineering and fucosylation studies [4,8] |
| B4GALT1 | Beta-1,4-galactosyltransferase 1; uses UDP-Gal | Glycan branching and bioprocess optimization [4,8] |
| ST6GAL1 | ST6 beta-galactoside alpha-2,6-sialyltransferase 1; uses CMP-sialic acid | Sialylation and therapeutic protein engineering [4,8] |
| MGAT1 | Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | N-glycan processing and high-mannose glycan studies |
How Is nucleotide-sugar metabolic process Regulated?
Nucleotide-sugar metabolic process is regulated at multiple levels. The hexosamine biosynthetic pathway, which produces UDP-N-acetylglucosamine, is sensitive to glucose, glutamine and acetyl-CoA availability, so nutrient status directly influences donor pools [1,5]. Enzyme expression and activity are also regulated transcriptionally and post-translationally, and nucleotide-sugar transporters control the flux of donors into the endoplasmic reticulum and Golgi lumen. In cultured cells, media composition such as raffinose supplementation can shift high-mannose glycan formation, indicating that extracellular nutrients feed back on nucleotide-sugar metabolism and glycosylation. Additives such as suramin can also alter glycosylation of recombinant proteins, further showing that the pathway responds to environmental and pharmacological inputs. Machine learning-guided bioprocess optimization is now being used to predict and control these regulatory interactions for improved glycosylation.
nucleotide-sugar metabolic process and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PGM1 | Congenital disorder of glycosylation with glycogen storage and endocrine features | Knockout and point-mutation cell models in hepatocyte-like cells |
| PGM3 | Congenital disorder of glycosylation with immunodeficiency | Knockout T-cell or fibroblast models |
| SLC35A2 | Congenital disorder of glycosylation with epilepsy and brain anomalies [2,3] | Knock-in of patient variants in neuronal cell lines |
| SLC35C1 | Leukocyte adhesion deficiency type II [2,3] | Knockout myeloid cell models and fucosylation assays |
| GFPT1 | Hexosamine pathway and cancer glycometabolic stress [1,5] | Overexpression and knockout cancer cell models |
Congenital disorders of glycosylation
Inherited defects in nucleotide-sugar metabolism and transport cause congenital disorders of glycosylation, a clinically and biochemically heterogeneous group of diseases. A proposed nosology based on clinical and biochemical footprints has classified these disorders and highlighted the central role of nucleotide-sugar synthesis, interconversion and transport genes such as PGM1, PGM3, GMPPA, GMPPB, SLC35A1, SLC35A2 and SLC35C1. Patients can present with multisystem involvement including neurological, immunological, hepatic and skeletal features, reflecting the broad requirement for glycosylation in development and homeostasis.
Cancer and glycometabolic stress
Cancer cells reprogram metabolism to support growth, and nucleotide-sugar metabolism is part of this adaptation. Tolerable glycometabolic stress has been shown to boost cancer cell resilience through altered N-glycosylation and Notch signaling activation, linking nucleotide-sugar flux to oncogenic signaling. Because glycosylation affects receptor trafficking and cell-cell communication, changes in nucleotide-sugar pools can influence tumor growth, invasion and immune interactions.
Leukocyte adhesion and immune disorders
Defects in GDP-fucose transport into the Golgi, caused by mutations in SLC35C1, impair fucosylation of selectin ligands and cause leukocyte adhesion deficiency type II. This disorder illustrates how a single nucleotide-sugar transporter step can produce a specific immune phenotype [2,3]. More broadly, altered nucleotide-sugar metabolism can affect immune receptor glycosylation and immune cell function.
Bioproduction and therapeutic protein quality
In biopharmaceutical production, nucleotide-sugar metabolism determines the glycan profile of recombinant proteins, which affects their stability, half-life and effector functions. Media supplementation with raffinose can reproducibly enhance high-mannose glycan formation, and additives such as suramin can alter glycosylation of Fc-fusion proteins [6,7]. Machine learning-guided optimization of CHO bioprocesses and media is being developed to control glycosylation and titer, underscoring the industrial importance of this pathway.
From nucleotide-sugar metabolic process-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of a nucleotide-sugar enzyme alter glycan structures? | CRISPR knockout in HEK293 or CHO cells followed by glycomics |
| Does a patient variant impair enzyme function? | Point-mutation knock-in of the variant in a wild-type cell line |
| Can a fluorescent tag report nucleotide-sugar transporter localization? | Tagged knock-in of SLC35 family genes |
| Does overexpression of a hexosamine pathway gene increase UDP-GlcNAc? | Doxycycline-inducible overexpression in cancer cell lines |
| Which nucleotide-sugar genes modify a glycan-dependent phenotype? | CRISPR library screening with glycan-binding lectin selection |
| Can glycosylation be engineered for therapeutic protein production? | CHO knockout and knock-in models with bioprocess readouts |
How to Study the nucleotide-sugar metabolic process Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Mass spectrometry glycomics | Glycan structures and composition | Comparing wild-type and knockout cells [6,7] |
| Lectin blotting and flow cytometry | Specific glycan epitopes | Screening glycosylation changes [4,6] |
| Targeted metabolomics | Nucleotide-sugar abundance | Quantifying donor pools [1,5] |
| Stable isotope tracing | Flux into nucleotide-sugars | Mapping precursor contributions |
| CRISPR knockout screening | Gene requirement for glycan phenotypes | Identifying pathway regulators [2,8] |
| Fluorescent tagging and imaging | Protein localization and organelle dynamics | Studying transporters and enzymes [3,4] |
| RNA-seq and proteomics | Expression of pathway genes and proteins | Characterizing regulatory responses [5,8] |
| Machine learning bioprocess modeling | Predictive glycosylation and titer outcomes | CHO process optimization |
Glycomics and glycan profiling
Mass spectrometry-based glycomics and lectin blotting are used to measure the glycan structures produced by cells with altered nucleotide-sugar metabolism. These methods can detect changes in high-mannose, complex and sialylated glycans after gene knockout or media manipulation [6,7]. Comparative glycomics is essential to link nucleotide-sugar pathway perturbations to functional glycan changes [4,8].
Metabolomics and nucleotide-sugar quantification
Targeted metabolomics using liquid chromatography-mass spectrometry can quantify nucleotide-sugars such as UDP-GlcNAc, UDP-Gal, GDP-mannose and CMP-sialic acid. These measurements reveal how genetic or environmental changes alter donor pools and flux through the pathway [1,5]. Stable isotope tracing can further define precursor contributions to nucleotide-sugar synthesis.
CRISPR screening and functional genomics
Pooled CRISPR knockout and activation screens can identify nucleotide-sugar metabolic genes that regulate glycan-dependent phenotypes, such as lectin binding, receptor signaling or drug sensitivity [2,8]. Screens are typically combined with lectin staining, flow cytometry or sequencing-based readouts to connect genotype to glycosylation phenotype [5,8].
Imaging and subcellular localization
Fluorescent tagging of nucleotide-sugar transporters and enzymes allows live-cell imaging of their localization in the endoplasmic reticulum and Golgi apparatus. These approaches help determine whether disease variants mislocalize or alter organelle function [3,4]. Imaging can be combined with glycosylation reporters to visualize donor availability in specific compartments.
How CRISPR Can Be Used to Study GO:0009225 nucleotide-sugar metabolic process
Knockout
CRISPR knockout of nucleotide-sugar metabolic genes is used to eliminate enzyme or transporter activity and measure the resulting changes in glycan structures, donor pools and cell phenotypes. For example, knocking out SLC35 family transporters can reveal which glycans depend on a specific donor import step [2,3]. Knockout models are also used in CHO cells to engineer glycosylation for bioproduction.
Point Mutation
Point-mutation knock-in models introduce patient-specific missense variants into endogenous nucleotide-sugar genes to test whether a variant impairs enzyme activity, stability or localization. These models are valuable for congenital disorders of glycosylation, where many disease alleles are missense mutations. Comparing isogenic wild-type and mutant cells controls for genetic background and enables precise functional interpretation [2,3].
Knock-in
Knock-in of reporter tags, such as fluorescent proteins or epitope tags, allows tracking of nucleotide-sugar enzymes and transporters in their native genomic context. Tagged knock-in models can be used to study subcellular localization, protein interactions and turnover without overexpression artifacts [3,4]. Knock-in of inducible expression cassettes can also provide controlled gene activation for pathway studies.
Overexpression
Overexpression of nucleotide-sugar biosynthetic enzymes or transporters is used to increase donor availability and test whether glycosylation becomes limiting for a phenotype. Inducible overexpression systems allow dose-dependent manipulation of pathway flux [1,5]. In bioprocessing, overexpression of glycosyltransferases and nucleotide-sugar pathway genes is explored to improve therapeutic protein glycoforms [4,8].
How EDITGENE Supports nucleotide-sugar metabolic process Research
Researchers studying nucleotide-sugar metabolic process-related genes often need to determine whether a candidate gene is causally involved in glycosylation, disease or bioproduction phenotypes. EDITGENE provides CRISPR-based cell model services that enable precise, isogenic experiments on nucleotide-sugar enzymes, transporters and regulatory genes.
Contact EDITGENE today to design your custom CRISPR model for nucleotide-sugar metabolic process research.
Frequently Asked Questions About nucleotide-sugar metabolic process
What is nucleotide-sugar metabolic process GO:0009225?
GO:0009225 is a biological process ontology term describing the cellular chemical reactions and pathways involving nucleotide-sugars, which are activated sugar donors used in glycosylation.
What are nucleotide-sugars?
Nucleotide-sugars are nucleotide-carbohydrates in which the distal phosphoric residue of a nucleoside 5'-diphosphate is glycosidically linked to a monosaccharide or monosaccharide derivative, such as UDP-GlcNAc or GDP-mannose.
What genes are involved in nucleotide-sugar metabolic process?
Genes include UAP1, GFPT1, GFPT2, PGM1, PGM3, GALE, UGP2, GMPPA, GMPPB and SLC35 family transporters such as SLC35A1, SLC35A2 and SLC35C1 [1,2,3].
Why is nucleotide-sugar metabolism important for glycosylation?
Glycosyltransferases require nucleotide-sugars as donor substrates, so nucleotide-sugar metabolism determines which glycans can be assembled in the endoplasmic reticulum and Golgi apparatus [1,4].
What diseases are linked to nucleotide-sugar metabolic process defects?
Defects cause congenital disorders of glycosylation, and altered nucleotide-sugar flux has been linked to cancer glycometabolic stress and immune disorders such as leukocyte adhesion deficiency type II [2,3,5].
How do nucleotide-sugars enter the endoplasmic reticulum and Golgi?
Nucleotide-sugar transporters of the SLC35 family mediate their import into the endoplasmic reticulum and Golgi lumen, where glycosyltransferases use them.
Can CRISPR knockout be used to study nucleotide-sugar metabolism?
Yes, CRISPR knockout of nucleotide-sugar enzymes and transporters is widely used to test their roles in glycan biosynthesis and cell phenotypes [2,8].
How is nucleotide-sugar metabolism measured experimentally?
Targeted metabolomics, glycomics, lectin blotting and stable isotope tracing are commonly used to measure nucleotide-sugar pools and glycan outputs [1,5,6].
What is the role of SLC35B1 in nucleotide metabolism?
Human SLC35B1 mediates stepwise ATP translocation into the endoplasmic reticulum, linking nucleotide transport to secretory pathway function.
How does media composition affect nucleotide-sugar metabolism in cell culture?
Media supplements such as raffinose and additives such as suramin can alter nucleotide-sugar pools and glycosylation profiles of recombinant proteins [6,7].
Conclusion
GO:0009225 nucleotide-sugar metabolic process is a central metabolic pathway that supplies activated sugar donors for glycosylation and connects nutrient metabolism to cell-surface glycan function. Its enzymes and transporters are implicated in congenital disorders of glycosylation, cancer glycometabolic stress and biotherapeutic protein quality [1,2,3,5,8]. Understanding this pathway requires integrated approaches including metabolomics, glycomics and CRISPR-based functional models [2,6,8]. EDITGENE supports this research with knockout, point-mutation, knock-in, overexpression and CRISPR library screening services tailored to nucleotide-sugar metabolic genes, enabling rigorous causal studies in disease and bioproduction contexts [2,3,8].
References
- 1. Lairson LL et al.. 2008. Glycosyltransferases: structures, functions, and mechanisms.. Annu Rev Biochem 77:521-55 PMID: 18518825
- 2. Ng BG et al.. 2024. Clinical and biochemical footprints of congenital disorders of glycosylation: Proposed nosology.. Mol Genet Metab 142(1):108476 PMID: 38653092
- 3. Gulati A et al.. 2025. Stepwise ATP translocation into the endoplasmic reticulum by human SLC35B1.. Nature 643(8072):855-864 PMID: 40399679
- 4. Stanley P. 2011. Golgi glycosylation.. Cold Spring Harb Perspect Biol 3(4) PMID: 21441588
- 5. Iwamoto S et al.. 2024. Tolerable glycometabolic stress boosts cancer cell resilience through altered N-glycosylation and Notch signaling activation.. Cell Death Dis 15(1):53 PMID: 38225221
- 6. Brühlmann D et al.. 2017. Cell culture media supplemented with raffinose reproducibly enhances high mannose glycan formation.. J Biotechnol 252:32-42 PMID: 28465212
- 7. Lim JH et al.. 2019. Evaluating the impact of suramin additive on CHO cells producing Fc-fusion protein.. Biotechnol Lett 41(11):1255-1263 PMID: 31541331
- 8. Walsh I et al.. 2025. Toward Machine Learning-Guided CHO Bioprocess and Media Optimization for Improved Titer and Glycosylation.. Biotechnol J 20(11):e70149 PMID: 41170670
