Affinage

FUT8

Alpha-(1,6)-fucosyltransferase · UniProt Q9BYC5

Length
575 aa
Mass
66.5 kDa
Annotated
2026-04-28
100 papers in source corpus 45 papers cited in narrative 45 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

FUT8 is the sole mammalian α-1,6-fucosyltransferase, catalyzing the transfer of fucose from GDP-β-L-fucose to the innermost GlcNAc of N-glycans (core fucosylation) in the Golgi, thereby broadly regulating glycoprotein stability, trafficking, and receptor signaling across diverse cellular contexts. Structurally, FUT8 functions as a homodimer assembled through its N-terminal coiled-coil domain, with a GT-B fold catalytic domain that employs an ordered binding mechanism (GDP-fucose binding preceding acceptor recognition) and a C-terminal SH3 domain whose His-535 residue is essential for activity and whose interaction with RPN1 stimulates catalytic function, while a stem region governs oligomerization and protein stability (PMID:17172260, PMID:32350116, PMID:32147455, PMID:36336076, PMID:33004438). Core fucosylation by FUT8 modulates the function of numerous glycoprotein substrates—including EGFR, TGF-β receptors, IGF-1R, VEGFR-2, B7H3, TLR4, TMEM67, GLUT1, and mucins—affecting receptor dimerization, ligand binding, cell-surface expression, and protection from proteasomal or autophagic degradation, with downstream consequences for MAPK, PI3K/AKT, NF-κB, and TGF-β/Smad signaling, EMT, immune checkpoint regulation, ciliogenesis, and mucus barrier integrity (PMID:28982386, PMID:32888953, PMID:33976130, PMID:36252012, PMID:40728580, PMID:41027183). Biallelic loss-of-function mutations in FUT8 cause a congenital disorder of glycosylation (FUT8-CDG) with growth retardation, neurological impairment, and respiratory complications (PMID:29304374).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2004 High

    Establishing FUT8 as the enzyme responsible for core fucosylation resolved which gene product catalyzes α-1,6-fucose addition to N-glycans and demonstrated its functional impact on antibody effector function.

    Evidence Homologous recombination knockout in CHO cells with glycan analysis and ADCC assay

    PMID:15352059

    Open questions at the time
    • No structural basis for catalysis yet known
    • Endogenous glycoprotein substrates not identified
    • In vivo physiological role uncharacterized
  2. 2006 High

    Determination of the FUT8 crystal structure and kinetic mechanism revealed a three-domain architecture (coiled-coil, GT-B catalytic, SH3) and ordered donor-substrate binding, providing the first molecular framework for understanding catalysis and substrate recognition.

    Evidence X-ray crystallography at 2.6 Å resolution; recombinant enzyme kinetic analysis with substrate analogs

    PMID:16344263 PMID:17172260

    Open questions at the time
    • No acceptor-bound structures available
    • Role of SH3 domain in catalysis unknown
    • Mechanism of homodimerization unresolved
  3. 2006 High

    Fut8 knockout mice revealed that core fucosylation is essential for TGF-β and EGF receptor signaling and LRP-1-mediated endocytosis in vivo, establishing FUT8 as a master regulator of receptor glycoprotein function.

    Evidence Fut8-null mouse phenotyping with growth retardation and emphysema, receptor signaling rescue experiments, LRP-1 endocytosis assay

    PMID:16567404 PMID:17132494

    Open questions at the time
    • Specific glycosylation sites on receptors not mapped
    • Cell-type-specific contributions not dissected
    • Whether core fucosylation directly modifies receptor conformation or stability unresolved
  4. 2013 High

    Discovery that FUT8 differentially modulates TGF-β superfamily signaling—enhancing TGF-β but inhibiting activin signaling—and suppresses erythroid differentiation demonstrated context-dependent biological functions beyond simple receptor activation.

    Evidence siRNA knockdown and rescue in PC12 cells for activin/Smad2; gain/loss-of-function with domain mutagenesis in erythroleukemia cells

    PMID:23609441 PMID:23796784

    Open questions at the time
    • Structural basis for differential receptor modulation unknown
    • Whether erythroid role is strictly glycosylation-dependent not fully resolved
  5. 2017 High

    Identification of FUT8 as a driver of cancer invasion through core fucosylation of TGF-β receptors (promoting EMT via a positive feedback loop) and L1CAM (promoting melanoma dissemination) expanded FUT8's role to oncogenic glycoprotein regulation.

    Evidence CRISPR KO/shRNA + lentiviral overexpression in breast cancer with xenograft; systems glycomics in melanoma with in vivo dissemination model

    PMID:28609658 PMID:28982386

    Open questions at the time
    • Full catalog of cancer-relevant substrates unknown
    • Relative contribution of individual substrates to invasive phenotype not quantified
  6. 2018 High

    Identification of biallelic FUT8 loss-of-function mutations in humans causing FUT8-CDG established that core fucosylation is essential for normal human development, paralleling the mouse knockout phenotype.

    Evidence Whole-exome sequencing, patient fibroblast functional studies, N-glycan mass spectrometry

    PMID:29304374

    Open questions at the time
    • Genotype-phenotype correlation across different mutations not established
    • Whether partial loss of function produces milder phenotypes unknown
  7. 2020 High

    Dissection of FUT8's domain architecture resolved how the SH3 domain (via His-535 and RPN1 binding), coiled-coil domain (via homodimerization), and stem region (via oligomerization and protein stability) cooperate to support enzymatic function and proper Golgi retention.

    Evidence Truncation and point mutagenesis, disulfide cross-linking, RPN1 co-IP and siRNA, native-PAGE, protein half-life assays in FUT8-KO cells

    PMID:32147455 PMID:32350116 PMID:36336076

    Open questions at the time
    • Full-length homodimer structure not available
    • How RPN1 stimulation mechanistically enhances catalysis unclear
    • Whether SH3-mediated cell-surface trafficking has physiological relevance unknown
  8. 2020 High

    Comprehensive structural and substrate-specificity studies with multiple acceptor-bound crystal structures established that FUT8 recognizes all sugar units of biantennary N-glycans and the Asn-X-Thr sequon, with GDP-fucose binding required to create the acceptor recognition site, while sialylation inhibits substrate efficiency.

    Evidence Crystal structures with four distinct glycan acceptors, STD NMR, glycan library screening, CHO cell glycan engineering

    PMID:33004438 PMID:35662980

    Open questions at the time
    • How protein context expands specificity to high-mannose glycans mechanistically unclear
    • No structure capturing the catalytic transition state
  9. 2021 High

    Demonstration that FUT8 core fucosylation stabilizes immune checkpoint B7H3 and modulates mucin trafficking/secretion extended the enzyme's functional reach to immune evasion and mucosal barrier maintenance.

    Evidence FUT8 KD with B7H3 stability and immune suppression assays in TNBC; FUT8 gain/loss-of-function for mucin trafficking in HT29 cells and Fut8-/- mouse colon analysis

    PMID:33976130 PMID:36252012

    Open questions at the time
    • Specific glycosylation sites on mucins responsible for trafficking effects not mapped
    • Whether B7H3 stabilization mechanism generalizes to other checkpoint proteins unknown
  10. 2023 High

    Elucidation of the chaperone-mediated autophagy degradation pathway for defucosylated B7H3 (via HSC70 recognition of an exposed motif) provided the first mechanistic link between loss of core fucosylation and a specific protein degradation route.

    Evidence Mass spectrometry identification of HSPA8 binding, CMA/LAMP2A pathway dissection, in vivo CRC model with FUT8 inhibitor FDW028

    PMID:37537172

    Open questions at the time
    • Whether CMA-mediated degradation applies to other defucosylated substrates unknown
    • Structural basis for motif exposure upon defucosylation not resolved
  11. 2024 High

    Discovery that FUT8 interacts with and core-fucosylates the ciliary transition zone protein TMEM67, preventing its autophagic degradation and enabling ciliogenesis, revealed a previously unrecognized role for core fucosylation in organelle biogenesis.

    Evidence Proteomics, Co-IP, autophagy degradation assay, conditional Fut8 KO mouse with kidney/brain/trachea ciliary phenotyping

    PMID:40728580

    Open questions at the time
    • Whether other ciliary proteins require core fucosylation unknown
    • Mechanism by which fucosylation blocks autophagic recognition not defined
  12. 2025 Medium

    QM/MM simulations resolved the catalytic mechanism as a highly asynchronous SN2 inversion with a transient intimate ion pair (not a stable oxocarbenium intermediate), while inhibitor studies confirmed GDP-induced loop closure creates the catalytically competent active site.

    Evidence QM/MM metadynamics and ELF topological analysis; HTS-derived covalent inhibitor with SPR and cellular validation

    PMID:39340265 PMID:41743314

    Open questions at the time
    • Computational mechanism awaits direct experimental validation by kinetic isotope effects or time-resolved crystallography
    • Covalent inhibitor selectivity profile across other glycosyltransferases not established
  13. 2025 Medium

    A non-enzymatic, scaffolding role for FUT8 was identified in viral replication, where it interacts with TGEV NSP3/NSP4 to promote double-membrane vesicle formation independently of its fucosyltransferase activity.

    Evidence CRISPR screen, Co-IP with viral NSPs, comparison of FUT8 KO vs. enzymatic inhibitor FDW028

    PMID:41205942

    Open questions at the time
    • Whether this non-enzymatic role extends to other coronaviruses unknown
    • Structural basis of NSP3/NSP4 interaction undefined
    • Single-lab observation not yet independently confirmed

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the full-length homodimer structure at atomic resolution, the structural basis for how core fucosylation differentially stabilizes versus activates distinct receptor substrates, whether a unified degradation mechanism (CMA or proteasomal) applies across defucosylated glycoproteins, and the extent of non-enzymatic scaffolding functions.
  • No full-length homodimer cryo-EM or crystal structure
  • Transition-state mechanism not validated by kinetic isotope effects
  • Systematic comparison of substrate-specific stabilization mechanisms lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 5 GO:0098772 molecular function regulator activity 4
Localization
GO:0005794 Golgi apparatus 3 GO:0005886 plasma membrane 1
Pathway
R-HSA-162582 Signal Transduction 5 R-HSA-392499 Metabolism of proteins 5 R-HSA-1430728 Metabolism 4 R-HSA-168256 Immune System 3 R-HSA-1266738 Developmental Biology 2 R-HSA-9612973 Autophagy 2
Complex memberships
FUT8 homodimer

Evidence

Reading pass · 45 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 FUT8 encodes an α-1,6-fucosyltransferase that catalyzes the transfer of fucose from GDP-fucose to N-acetylglucosamine in an α-1,6 linkage on N-glycans (core fucosylation); knockout of both FUT8 alleles in CHO cells completely abolishes core fucosylation of antibody Fc regions, dramatically enhancing FcγRIIIa binding and ADCC (~100-fold increase). Homologous recombination knockout in CHO cells, glycan analysis, FcγRIIIa binding assay, ADCC assay Biotechnology and bioengineering High 15352059
2006 Crystal structure of human FUT8 at 2.6 Å resolution reveals three domains: an N-terminal coiled-coil (α-helical) domain, a GT-B fold catalytic domain with a Rossmann fold housing the GDP-fucose donor binding site, and a C-terminal SH3 domain; conserved residues in the Rossmann fold participate in donor substrate binding and catalysis. X-ray crystallography at 2.6 Å resolution Glycobiology High 17172260
2005 FUT8 is a type II Golgi-localized membrane protein that follows a rapid equilibrium random kinetic mechanism; it strongly recognizes the base portion and diphosphoryl group of GDP-β-L-fucose as donor substrate; two conserved arginine residues play an important role in donor substrate binding. Large-scale recombinant protein production in baculovirus/insect cells, kinetic analysis, inhibition studies with GDP-fucose derivatives Glycobiology High 16344263
2006 Core fucosylation by Fut8 is required for normal TGF-β1 receptor and EGF receptor signaling; Fut8-null mice show severe growth retardation and emphysema-like lung destruction due to dysregulated TGF-β1 receptor activation, overexpression of MMP12/MMP13, and downregulation of elastin; reintroduction of Fut8 rescues receptor-mediated signaling in null cells. Fut8 knockout mouse phenotyping, TGF-β1 therapeutic rescue experiment, gene reintroduction rescue in null cells Methods in enzymology High 17132494
2006 Core fucosylation by Fut8 is required for normal LRP-1 scavenger/endocytic function; loss of Fut8 impairs LRP-1-mediated endocytosis of IGFBP-3, leading to markedly elevated serum IGFBP-3 in Fut8-null mice; reintroduction of Fut8 rescues endocytosis. Fut8 knockout mouse model, endocytosis assay, serum IGFBP-3 measurement, Fut8 gene reintroduction rescue Journal of biochemistry High 16567404
2009 Fut8 is required for normal VEGFR-2 expression in the lung; knockdown of Fut8 suppresses VEGFR-2 mRNA and protein at the transcriptional level; loss of VEGFR-2 increases ceramide and apoptosis of septal epithelia and endothelia, contributing to emphysema-like changes in Fut8-/- mice. Fut8 KO mouse lung analysis, siRNA knockdown in A549/TGP49 cells, VEGFR-2 mRNA/protein quantification, TUNEL assay Journal of biochemistry High 19179362
2012 Donor substrate GDP-fucose binding to FUT8 involves specific recognition of the guanine base by His363 and Asp453, tight binding of the pyrophosphate moiety, and simultaneous binding of Arg365 to both the β-phosphate and the fucose moiety; prior binding of GDP is required for optimal N-glycan acceptor recognition. STD NMR, SPR binding assays, in silico molecular docking and MD simulations based on structural analogy to cePOFUT Biochimica et biophysica acta Medium 22982178
2013 α1,6-Fucosylation of activin receptors by Fut8 negatively regulates activin-mediated signaling (phospho-Smad2); knockdown of Fut8 in PC12 cells decreases α1,6-fucosylation of activin receptors and enhances activin-induced phospho-Smad2 and neurite formation, while restoring Fut8 reverses this; demonstrating a dual role for Fut8 in TGF-β versus activin signaling. siRNA knockdown in PC12 cells, phospho-Smad2 immunoblot, neurite formation assay, activin receptor lectin analysis, Fut8 re-expression rescue FASEB journal High 23796784
2013 FUT8 overexpression inhibits hemoglobin production and erythroid differentiation; the donor substrate-binding domain and a flexible loop are essential for this inhibitory function; FUT8 expression is positively regulated by c-Myc and c-Myb during erythroid differentiation. Gene expression profiling, overexpression and shRNA knockdown in murine erythroleukemia and K562 cells, domain mutagenesis, hemoglobin assay, transferrin receptor/glycophorin A FACS Journal of biological chemistry High 23609441
2016 Mammalian FUT8 is the sole enzyme responsible for GnT I-independent core fucosylation of high-mannose N-glycans (Man5GlcNAc2); knockdown of FUT8 in GnT I-/- HEK293S cells eliminates core fucosylation of high-mannose glycoforms, while FUT8 overexpression produces fully core-fucosylated oligomannose glycans. Lentivirus-mediated FUT8 knockdown and overexpression in HEK293S GnT I-/- cells, glycan analysis of recombinant EPO Journal of biological chemistry High 27008861
2017 FUT8 mediates core fucosylation of TGF-β receptor complexes, enhancing TGF-β1 binding and downstream signaling to promote EMT and breast cancer invasion; FUT8 is transcriptionally upregulated during TGF-β-induced EMT, creating a positive feedback loop. shRNA/CRISPR KO and lentiviral overexpression, lectin blot, luciferase signaling assay, in vitro ligand binding assay, transwell invasion, mammary fat pad xenograft Breast cancer research : BCR High 28982386
2017 FUT8 silencing suppresses melanoma invasion and tumor dissemination; L1CAM is identified as a glycoprotein target of FUT8 core fucosylation, and core fucosylation of L1CAM impacts its cleavage and ability to support melanoma invasion. Systems-based glycomics of patient samples, siRNA silencing, in vitro invasion assays, in vivo tumor dissemination model, glycoprotein target enrichment Cancer cell High 28609658
2018 FUT8 modifies the α1,6-fucosylation of IGF-1R, and this core fucosylation regulates IGF-1-dependent activation of IGF-1R and downstream MAPK and PI3K/Akt signaling in trophoblastic cells; FUT8 knockdown suppresses trophoblast proliferation, EMT, migration, and invasion. siRNA knockdown in JAR/JEG-3 cells, immunoprecipitation of core-fucosylated IGF-1R, phospho-IGF-1R western blot, functional cell assays Placenta High 30712666
2020 The C-terminal SH3 domain of FUT8 is essential for its enzymatic activity both in cells and in vitro; His-535 in the SH3 domain is the critical residue for activity; the SH3 domain also mediates partial trafficking of FUT8 to the cell surface; ribophorin I (RPN1), a subunit of the oligosaccharyltransferase complex, binds FUT8 in an SH3-dependent manner and stimulates FUT8 activity and core fucosylation. Truncation mutants, site-directed mutagenesis, immunofluorescence, FACS, cell-surface biotinylation, proteomics, LC-ESI-MS, RPN1 siRNA knockdown Journal of biological chemistry High 32350116
2020 FUT8-mediated core fucosylation of EGFR upregulates cell-surface EGFR and corresponding downstream signaling, contributing to castration resistance in prostate cancer; castration in xenograft models induces FUT8 overexpression which is associated with increased EGFR expression. FUT8 overexpression in prostate cancer cells, comprehensive proteomics, EGFR cell-surface quantification, androgen-depleted xenograft model Cancers Medium 32085441
2020 FUT8 core fucosylation of EGFR promotes EGFR dimerization, EGF-EGFR complex trafficking, and AKT signaling; shRNA-mediated FUT8 knockdown reduces EGFR dimerization, slows EGF-EGFR complex trafficking, and decreases EGFR/AKT signaling, leading to reduced keratinocyte proliferation; conditional FUT8 knockout in an IL-23 psoriasis-like mouse model ameliorates disease phenotypes. shRNA knockdown, EGFR dimerization assay, EGF-EGFR trafficking assay, EGFR/AKT western blot, conditional KO mouse model Journal of investigative dermatology High 32888953
2020 FUT8-mediated core fucosylation of EGFR in cancer-associated fibroblasts (CAFs) promotes their cancer-supporting capacity, leading to increased NSCLC cell proliferation and invasiveness in co-culture; FUT8 overexpression in CAFs promotes formation of an invasive tumor microenvironment in vivo. CAF isolation from NSCLC patients, FUT8 modulation, 3D-printed non-contact co-culture, CAF/NSCLC co-injection nude mouse model American journal of cancer research Medium 32266093
2020 The α-helical (N-terminal coiled-coil) and SH3 domains of FUT8 are both required for enzymatic activity; FUT8 forms a homodimer via intermolecular hydrophobic interactions through its α-helical domains; the SH3 domain is located in close proximity to the α-helical domain in an intermolecular manner, as shown by in vivo disulfide cross-linking. Domain truncation and site-directed mutagenesis, in vivo disulfide cross-linking, heterologous expression in Sf21/COS-1 cells, enzymatic activity assays Biochimica et biophysica acta. General subjects High 32147455
2020 FUT8 substrate specificity requires the biantennary complex N-glycan structure; FUT8 recognizes all sugar units of the G0 N-glycan and most residues of the Asn-X-Thr sequon; prior binding of GDP-β-L-fucose (or GDP) is required for optimal N-glycan acceptor recognition; the underlying peptide/protein context influences fucosylation of high-mannose and paucimannose but not complex-type N-glycans. Crystal structures of FUT8 with donor analog and four distinct glycan acceptors, STD NMR, kinetic assays on active site mutants, glycan acceptor library screening, CHO cell glycan engineering Journal of biological chemistry High 33004438
2021 FUT8 catalyzes core fucosylation of B7H3 (CD276) at N-glycan sites, stabilizing B7H3 protein; FUT8 knockdown causes loss of B7H3 glycosylation and rescues B7H3-mediated immunosuppressive function in TNBC cells; combined FUT8 inhibition and anti-PDL1 shows enhanced therapeutic efficacy. FUT8 knockdown, glycan analysis, B7H3 protein stability assay, immune suppression functional assay, in vivo tumor model with 2F-Fuc inhibitor + anti-PDL1 Nature communications High 33976130
2021 FUT8 overexpression in colonic cells increases delivery of MUC1 to the plasma membrane and extracellular release of MUC2 and MUC5AC; FUT8-modified mucins are more resistant to removal from the cell surface; FUT8 KD causes intracellular accumulation of MUC1 and alters the MUC2:MUC5AC ratio; Fut8-/- mice exhibit thinner proximal colon mucus with altered neutral-to-acidic mucin ratio. FUT8 overexpression and KD in HT29-18N2 cells, MUC1 cell-surface localization, mucin secretion assay, Fut8-/- mouse mucus analysis PNAS High 36252012
2021 FUT8 activity is directed by glycan structure and protein context: complex-type N-glycans are the preferred substrates in cells; peptide/protein context expands FUT8 activity to high-mannose and paucimannose N-glycans; sialylation of N-glycans significantly reduces FUT8 substrate efficiency. In vitro FUT8 assay with N-glycan library, N-glycopeptides, STD NMR, CHO cell glycan engineering (KO of specific glycosylation enzymes), mass spectrometry glycan analysis ACS catalysis High 35662980
2021 FUT8 modifies core fucosylation levels on TNF receptors (TNFRs); lower TNFR fucosylation in osteosarcoma cells activates the non-canonical NF-κB signaling pathway and decreases mitochondria-dependent apoptosis, promoting OS cell survival. FUT8 expression analysis in OS cell lines, gain/loss-of-function, TNFR fucosylation analysis, non-canonical NF-κB pathway assay, apoptosis assay Cell death & disease Medium 34857735
2022 FUT8 stem region (two α-helices) is essential for FUT8 oligomerization/multimer formation but not for catalytic activity; the first helix of the stem region is critical for multimer formation; loss of the stem region destabilizes FUT8 protein, increases ER localization, and shortens its half-life. FUT8Δstem mutants expressed in FUT8-KO HEK293 cells, immunoprecipitation, native-PAGE, ER localization analysis, protein half-life assay Journal of biological chemistry High 36336076
2022 Quantitative glycoproteomics identifies 140 common core-fucosylated FUT8 target glycoproteins in invasive breast cancer cells; core fucosylation of integrin αvβ5 is crucial for breast cancer cell adhesion to vitronectin; core fucosylation of IL6ST is crucial for enhanced cellular signaling by IL-6 and oncostatin M. Quantitative glycoproteomics on FUT8-KO vs. wild-type cells, LCA blot, LC-MS/MS validation, functional adhesion assays, ingenuity pathway analysis Breast cancer research : BCR High 35303925
2022 FUT8 interacts with galectin-3 (Gal-3) by co-immunoprecipitation; FUT8 knockdown downregulates Gal-3 expression and inhibits FAK/Akt signaling, thereby suppressing TGF-β1-induced fibroblast proliferation, migration, and fibrosis; overexpression of Gal-3 reverses the effects of FUT8 silencing. Co-IP assay, siRNA knockdown in MRC-5 cells, rescue with Gal-3 overexpression, CCK-8/BrdU/wound healing assays, western blot, bleomycin mouse model Journal of Southern Medical University Medium 36073215
2023 FUT8-silence-induced defucosylation at N104 on B7-H3 in colorectal cancer cells exposes a 106-110 SLRLQ motif recognized by HSC70 (HSPA8), which then drives lysosomal degradation of B7-H3 via the chaperone-mediated autophagy (CMA) pathway; the FUT8 inhibitor FDW028 recapitulates this mechanism. FUT8 siRNA, mass spectrometry identification of HSPA8 binding, CMA pathway assay with LAMP2A, in vivo CRC pulmonary metastasis model with FDW028 Cell death & disease High 37537172
2023 FUT8-catalyzed core fucosylation is required for AβO-induced pro-inflammatory microglial activation; FUT8 inhibition (siRNA or pharmacological) reduces pro-inflammatory cytokines and p38MAPK activation in AβO-stimulated hiMG; p53 binds to the Fut8 promoter and is required for FUT8 overexpression in AβO-activated microglia. Human iPSC-derived microglia model, siRNA knockdown, cytokine assays, p38MAPK western blot, p53 promoter binding analysis, p53 siRNA rescue Glia Medium 36692036
2023 FUT8 directly catalyzes core fucosylation of SEMA7A at five N-linked glycosylation sites (Asn 105, 157, 258, 330, 602) via a direct protein-protein interaction; this glycosylation is required for SEMA7A trafficking from cytoplasm to cell membrane; EGF increases SEMA7A-FUT8 binding affinity; glycosylated SEMA7A drives CD8+ T cell exhaustion and defines RBM4 as downstream effector of PD-L1 alternative splicing. Co-IP, MS identification of glycosylation sites, trafficking/localization assay, EGF stimulation, T cell exhaustion assay, RBM4/PD-L1 functional analysis International journal of oral science Medium 38548747
2023 FUT8-mediated core fucosylation of VEGFR-2 activates the AKT pathway in pulmonary artery smooth muscle cells; FUT8 knockdown inhibits PDGF-BB-induced PASMC proliferation, migration, phenotypic switching, and apoptosis resistance; AKT activator SC79 partially reverses siFUT8 effects. siRNA knockdown in PASMCs, AKT pathway western blot, cell proliferation/migration/apoptosis assays, monocrotaline PAH rat model with 2FF inhibitor Aging and disease Medium 37196106
2023 Loss of FUT8 in renal tubular epithelial cells ameliorates IRI-induced renal inflammation-to-fibrosis transition via the TLR3 core fucosylation-NF-κB signaling pathway; tubular epithelial cell-specific FUT8 knockout mouse demonstrates cell type-specific role. TEC-specific conditional FUT8 knockout mouse, IRI model, TLR3 core fucosylation analysis, NF-κB signaling assay FASEB journal High 37432656
2024 FUT8 interacts with TMEM67, a ciliary transition zone component, and catalyzes its core fucosylation; core fucosylation stabilizes TMEM67 by preventing its autophagy-mediated degradation and ensures its proper localization to the transition zone for ciliogenesis; Fut8-deficient mice exhibit ciliary defects in kidney, brain, and trachea; ectopic Cntn2 (core fucosylation target) rescues neuronal defects from Fut8 deficiency. Mass spectrometry proteomics, Co-IP of FUT8-TMEM67, core fucosylation assay, autophagy degradation assay, TMEM67 localization, Fut8 conditional KO mouse with organ-specific ciliary phenotyping Journal of cell biology High 40728580
2024 FUT8 inhibitor development: GDP binding induces a closed, catalytically competent active site via conformational rearrangement of two flexible loops; a selective small-molecule inhibitor (KD = 49 nM) binds only in the presence of GDP, generating a reactive naphthoquinone methide that covalently reacts with FUT8; prodrug derivatization enables cellular suppression of EGFR and T-cell signaling. High-throughput screening, SPR binding, mechanistic inhibitor studies, cell-based core fucose assay, EGFR/T-cell signaling assays Angewandte Chemie High 39340265
2025 FUT8 catalysis proceeds via a GDP-fucose-induced concerted loop closure creating a competent active site; the reaction follows a highly asynchronous SN2 inverting mechanism involving cleavage of the fucose-GDP glycosidic bond, formation of the new glycosidic bond, and H-transfer to the catalytic Glu373 as three stages with a transient intimate ion pair (lifetime 350–800 fs); no stable oxocarbenium intermediate forms. Molecular dynamics, QM/MM simulations, metadynamics, electron localization function (ELF) topological analysis ACS catalysis Medium 41743314
2011 Increased FUT8 expression and activity in the liver are strongly linked to age-related increases in core-fucosylated N-glycans; age-related increased FUT8 activity influences IGF-1R signaling sensitivity. N-glycan profiling of mouse serum in different age groups, C57BL/6 mice including klotho-deficient and Snell Dwarf mice, caloric restriction model, FUT8 expression and activity measurement in liver Aging cell Medium 21951615
2018 Biallelic loss-of-function mutations in human FUT8 cause a congenital disorder of glycosylation (FUT8-CDG) characterized by complete absence of FUT8 protein and substantial deficiency of core-fucosylated N-glycans in fibroblasts and serum, causing intrauterine growth retardation, developmental delays, neurological impairments, and respiratory complications. Whole-exome sequencing, functional studies in patient-derived primary fibroblasts, N-glycan analysis by mass spectrometry, splicing analysis American journal of human genetics High 29304374
2020 FUT8 knockout in CHO cells alters not only core fucosylation but broadly changes other glycosylation processes; sialyltransferases and glucosyltransferases are sharply decreased in FUT8KO cells; 28.6% of 442 identified glycoproteins show significantly altered expression, revealing FUT8's broad impact on the glycosylation machinery. FUT8 KO CHO cells, large-scale glycoproteomics with HILIC enrichment, high-resolution LC-MS, SILAC-based proteomics Frontiers in chemistry Medium 34778211
2025 FUT8 interacts with TGEV nonstructural proteins NSP3 and NSP4 (independent of its fucosyltransferase enzymatic activity) to facilitate formation of double-membrane vesicles (DMVs) required for viral replication; FUT8 enzymatic inhibitor FDW028 had no effect, confirming this role is non-enzymatic. Genome-wide CRISPR/Cas9 screen, FUT8 KO characterization, viral internalization and replication assays, DMV formation assay, Co-IP with NSP3/NSP4, FDW028 enzymatic inhibitor comparison International journal of biological macromolecules Medium 41205942
2025 FUT8 promotes core fucosylation of CD36 in pericytes, increasing CD36 expression and activating the mitochondrial-dependent apoptosis signaling pathway, thereby driving pericyte-to-myofibroblast transition and AKI-to-CKD progression. GEO/DISCO database analysis, IRI mouse model, hypoxia/reoxygenation pericyte model, IP/confocal-IF for CD36 CF, flow cytometry apoptosis, JC-1 mitochondrial membrane potential assay Molecular medicine Medium 39563263
2025 FUT8 promotes PKM2 K115 lactylation by enhancing HIF-1α-driven glycolysis and lactate production in clear cell RCC; increased PKM2 lactylation boosts PKM2 enzymatic activity while reducing its nuclear localization, driving EMT and malignant progression. FUT8 knockdown in ccRCC cells and xenografts, HIF-1α-glycolysis assay, lactylation mass spectrometry, PKM2 activity assay, nuclear/cytoplasmic fractionation Cell death discovery Medium 41857011
2025 FUT8-mediated core fucosylation of NCEH1 stabilizes NCEH1 by preventing proteasomal degradation; core-fucosylated NCEH1 facilitates LPA secretion, driving M2-like tumor-associated macrophage polarization and promoting HGSC peritoneal metastasis. Glycoproteomic assay identifying NCEH1 as core fucosylation substrate, proteasomal degradation assay, non-targeted metabolomics for LPA, macrophage polarization assay, in vitro and in vivo metastasis models Oncogene Medium 41786877
2025 FUT8 upregulates Unc5b core fucosylation (primarily in the ER), which activates the p-CDC42/p-PAK pathway and reduces macrophage migration capacity, thereby promoting foam cell retention and atherosclerosis progression; defucosylation of Unc5b rescues macrophage migration. IP assay for Fut8-Unc5b core fucosylation, genetic deletion of fucosylation sites, ApoE-/- mouse model, Unc5b KD/overexpression, p-CDC42/p-PAK western blot, wound healing migration assay Cell & bioscience Medium 36670464
2025 FUT8 promotes core fucosylation of Toll-like receptor 4 (TLR4) in gingival fibroblasts, enhancing NF-κB signaling sensitivity and inflammatory cytokine secretion; dual-gene silencing of Fut8 and TLR4 confirms their synergistic role in the inflammatory cascade; core fucosylation inhibitor 2FF alleviates periodontitis in a mouse model. Co-immunoprecipitation, TLR4 glycosylation assay, gene silencing, NF-κB pathway analysis, cytokine assay, periodontitis mouse model with 2FF International dental journal Medium 41653834
2025 FUT8 depletion reduces cAMP production following FSH stimulation in granulosa cells, impairing FSHR signaling; Fut8-/- mouse oocytes exhibit abnormal zona pellucida formation and impaired embryonic development; FIGLA expression and other embryonic development genes are downregulated in Fut8-/- ovaries. FUT8 knockdown in KGN cells, cAMP assay, Fut8-/- mouse oocyte/embryo analysis, zona pellucida imaging, FIGLA expression analysis Journal of assisted reproduction and genetics Medium 40473957
2025 FUT8 promotes HDM-induced epithelial-mesenchymal transition and IL-25/IL-33 inflammatory responses in bronchial epithelial cells by catalyzing core fucosylation of GLUT1 at Asn45 (N45), stabilizing GLUT1 protein and enhancing glycolysis; the GLUT1 N45Q mutant abolishes this effect. Lectin pull-down assay for GLUT1-FUT8 interaction, FUT8 overexpression/silencing, GLUT1 half-life assay, N45Q mutagenesis rescue, ECAR/ATP/lactate assays, IL-25/IL-33 secretion assay Biochemical and biophysical research communications High 41027183

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnology and bioengineering 428 15352059
2017 A Systems Biology Approach Identifies FUT8 as a Driver of Melanoma Metastasis. Cancer cell 247 28609658
2017 FUT8 promotes breast cancer cell invasiveness by remodeling TGF-β receptor core fucosylation. Breast cancer research : BCR 177 28982386
2021 FUT8-mediated aberrant N-glycosylation of B7H3 suppresses the immune response in triple-negative breast cancer. Nature communications 151 33976130
2004 Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA. Biotechnology and bioengineering 122 15515168
2006 Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8. Glycobiology 117 17172260
2007 Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC. BMC biotechnology 114 18047682
2010 Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies. Biotechnology and bioengineering 112 20564614
2003 Expression of alpha1,6-fucosyltransferase (FUT8) in papillary carcinoma of the thyroid: its linkage to biological aggressiveness and anaplastic transformation. Cancer letters 82 14568171
2006 Phenotype changes of Fut8 knockout mouse: core fucosylation is crucial for the function of growth factor receptor(s). Methods in enzymology 72 17132494
2016 Comprehensive N-glycan profiles of hepatocellular carcinoma reveal association of fucosylation with tumor progression and regulation of FUT8 by microRNAs. Oncotarget 65 27533464
2013 Effects of microRNAs on fucosyltransferase 8 (FUT8) expression in hepatocarcinoma cells. PloS one 63 24130780
2021 FUT8 and Protein Core Fucosylation in Tumours: From Diagnosis to Treatment. Journal of Cancer 56 34093814
2005 Reaction mechanism and substrate specificity for nucleotide sugar of mammalian alpha1,6-fucosyltransferase--a large-scale preparation and characterization of recombinant human FUT8. Glycobiology 56 16344263
2018 Biallelic Mutations in FUT8 Cause a Congenital Disorder of Glycosylation with Defective Fucosylation. American journal of human genetics 55 29304374
2016 Mammalian α-1,6-Fucosyltransferase (FUT8) Is the Sole Enzyme Responsible for the N-Acetylglucosaminyltransferase I-independent Core Fucosylation of High-mannose N-Glycans. The Journal of biological chemistry 54 27008861
2020 α1,6-Fucosyltransferase (FUT8) regulates the cancer-promoting capacity of cancer-associated fibroblasts (CAFs) by modifying EGFR core fucosylation (CF) in non-small cell lung cancer (NSCLC). American journal of cancer research 47 32266093
2023 FDW028, a novel FUT8 inhibitor, impels lysosomal proteolysis of B7-H3 via chaperone-mediated autophagy pathway and exhibits potent efficacy against metastatic colorectal cancer. Cell death & disease 45 37537172
2021 FUT8-Directed Core Fucosylation of N-glycans Is Regulated by the Glycan Structure and Protein Environment. ACS catalysis 43 35662980
2011 Molecular cloning, characterization, genomic organization and promoter analysis of the α1,6-fucosyltransferase gene (fut8) expressed in the rat hybridoma cell line YB2/0. BMC biotechnology 41 21208406
2020 Impact of Increased FUT8 Expression on the Extracellular Vesicle Proteome in Prostate Cancer Cells. Journal of proteome research 37 32378902
2020 Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases. The Journal of biological chemistry 37 33004438
2006 Loss of core fucosylation of low-density lipoprotein receptor-related protein-1 impairs its function, leading to the upregulation of serum levels of insulin-like growth factor-binding protein 3 in Fut8-/- mice. Journal of biochemistry 37 16567404
2009 Requirement of Fut8 for the expression of vascular endothelial growth factor receptor-2: a new mechanism for the emphysema-like changes observed in Fut8-deficient mice. Journal of biochemistry 35 19179362
2022 The ulcerative colitis-associated gene FUT8 regulates the quantity and quality of secreted mucins. Proceedings of the National Academy of Sciences of the United States of America 34 36252012
2021 FUT8-AS1 Inhibits the Malignancy of Melanoma Through Promoting miR-145-5p Biogenesis and Suppressing NRAS/MAPK Signaling. Frontiers in oncology 33 34094894
2013 α1,6-Fucosylation regulates neurite formation via the activin/phospho-Smad2 pathway in PC12 cells: the implicated dual effects of Fut8 for TGF-β/activin-mediated signaling. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 33 23796784
2010 Enhancement of DNA uptake in FUT8-deleted CHO cells for transient production of afucosylated antibodies. Biotechnology and bioengineering 33 20564613
2020 The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation. The Journal of biological chemistry 31 32350116
2018 FUT8 drives the proliferation and invasion of trophoblastic cells via IGF-1/IGF-1R signaling pathway. Placenta 31 30712666
2011 Alteration in N-glycomics during mouse aging: a role for FUT8. Aging cell 30 21951615
2020 A Comprehensive Analysis of FUT8 Overexpressing Prostate Cancer Cells Reveals the Role of EGFR in Castration Resistance. Cancers 28 32085441
2000 Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8). Glycobiology 26 10814706
2017 Producing defucosylated antibodies with enhanced in vitro antibody-dependent cellular cytotoxicity via FUT8 knockout CHO-S cells. Engineering in life sciences 24 32624826
2020 A lectin-based glycomic approach identifies FUT8 as a driver of radioresistance in oesophageal squamous cell carcinoma. Cellular oncology (Dordrecht, Netherlands) 23 32474852
2021 Alpha-(1,6)-fucosyltransferase (FUT8) affects the survival strategy of osteosarcoma by remodeling TNF/NF-κB2 signaling. Cell death & disease 22 34857735
2018 Enhanced motility and proliferation by miR-10b/FUT8/p-AKT axis in breast cancer cells. Oncology letters 22 30008906
2012 Donor substrate binding and enzymatic mechanism of human core α1,6-fucosyltransferase (FUT8). Biochimica et biophysica acta 22 22982178
2023 Beyond antibody fucosylation: α-(1,6)-fucosyltransferase (Fut8) as a potential new therapeutic target for cancer immunotherapy. Antibody therapeutics 21 37077473
2022 HOTAIR modulates hepatocellular carcinoma progression by activating FUT8/core-fucosylated Hsp90/MUC1/STAT3 feedback loop via JAK1/STAT3 cascade. Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 21 35504805
2006 From glycomics to functional glycomics of sugar chains: Identification of target proteins with functional changes using gene targeting mice and knock down cells of FUT8 as examples. Biochimica et biophysica acta 21 17174880
2023 The role of FUT8-catalyzed core fucosylation in Alzheimer's amyloid-β oligomer-induced activation of human microglia. Glia 20 36692036
2021 LncRNA LEF1-AS1/LEF1/FUT8 Axis Mediates Colorectal Cancer Progression by Regulating α1, 6-Fucosylationvia Wnt/β-Catenin Pathway. Digestive diseases and sciences 20 34021424
2022 Production of afucosylated antibodies in CHO cells by coexpression of an anti-FUT8 intrabody. Biotechnology and bioengineering 18 35509261
2019 Bioprocess development of a stable FUT8-/--CHO cell line to produce defucosylated anti-HER2 antibody. Bioprocess and biosystems engineering 18 30982137
2000 Ancestral exonic organization of FUT8, the gene encoding the alpha6-fucosyltransferase, reveals successive peptide domains which suggest a particular three-dimensional core structure for the alpha6-fucosyltransferase family. Molecular biology and evolution 18 11070054
1999 Mapping of the alpha-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3. Cytogenetics and cell genetics 18 10343104
2024 FUT8-mediated aberrant N-glycosylation of SEMA7A promotes head and neck squamous cell carcinoma progression. International journal of oral science 17 38548747
2021 Glycoproteomic Characterization of FUT8 Knock-Out CHO Cells Reveals Roles of FUT8 in the Glycosylation. Frontiers in chemistry 17 34778211
2020 Caveolin-1 upregulates Fut8 expression by activating the Wnt/β-catenin pathway to enhance HCC cell proliferative and invasive ability. Cell biology international 17 32710651
2020 FUT8 Remodeling of EGFR Regulates Epidermal Keratinocyte Proliferation during Psoriasis Development. The Journal of investigative dermatology 17 32888953
2011 Association of fucosyltransferase 8 (FUT8) polymorphism Thr267Lys with pulmonary emphysema. Journal of human genetics 17 22011814
2022 Quantitative glycoproteomics analysis identifies novel FUT8 targets and signaling networks critical for breast cancer cell invasiveness. Breast cancer research : BCR 16 35303925
2022 FUT8 is regulated by miR-122-5p and promotes malignancies in intrahepatic cholangiocarcinoma via PI3K/AKT signaling. Cellular oncology (Dordrecht, Netherlands) 16 36348252
2020 Involvement of the α-helical and Src homology 3 domains in the molecular assembly and enzymatic activity of human α1,6-fucosyltransferase, FUT8. Biochimica et biophysica acta. General subjects 16 32147455
2021 SNHG1/miR-186/FUT8 regulates cell migration and invasion in oral squamous cell carcinoma. Oral diseases 15 33872442
2019 Hepatitis C Virus-Induced FUT8 Causes 5-FU Drug Resistance in Human Hepatoma Huh7.5.1 Cells. Viruses 15 31022917
2013 α-1,6-Fucosyltransferase (FUT8) inhibits hemoglobin production during differentiation of murine and K562 human erythroleukemia cells. The Journal of biological chemistry 13 23609441
2022 The stem region of α1,6-fucosyltransferase FUT8 is required for multimer formation but not catalytic activity. The Journal of biological chemistry 12 36336076
2023 Fucosyltransferase 8 (FUT8) and core fucose expression in oxidative stress response. PloS one 10 36780470
2023 FUT8-Mediated Core Fucosylation Promotes the Pulmonary Vascular Remodeling in Pulmonary Arterial Hypertension. Aging and disease 10 37196106
2021 Appropriate aglycone modification significantly expands the glycan substrate acceptability of α1,6-fucosyltransferase (FUT8). The Biochemical journal 10 33734311
2016 Expression of α-1,6-fucosyltransferase (FUT8) in rice grain and immunogenicity evaluation of plant-specific glycans. Journal of biotechnology 10 28013072
2023 Loss of FUT8 in renal tubules ameliorates ischemia-reperfusion injury-induced renal interstitial inflammation transition to fibrosis via the TLR3-NF-κB pathway. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 9 37432656
2014 The α1,6-fucosyltransferase gene (fut8) from the Sf9 lepidopteran insect cell line: insights into fut8 evolution. PloS one 9 25333276
2024 The Multifaceted Role of FUT8 in Tumorigenesis: From Pathways to Potential Clinical Applications. International journal of molecular sciences 8 38256141
2024 Development of a FUT8 Inhibitor with Cellular Inhibitory Properties. Angewandte Chemie (International ed. in English) 8 39340265
2023 Hypofucosylation of Unc5b regulated by Fut8 enhances macrophage emigration and prevents atherosclerosis. Cell & bioscience 8 36670464
2023 N6 -methyladenosine-modified circFUT8 competitively interacts with YTHDF2 and miR-186-5p to stabilize FUT8 mRNA to promote malignant progression in lung adenocarcinoma. Thoracic cancer 8 37669906
2020 Role of FUT8 expression in clinicopathology and patient survival for various malignant tumor types: a systematic review and meta-analysis. Aging 8 33323540
2024 Distinctive domains and activity regulation of core fucosylation enzyme FUT8. Biochimica et biophysica acta. General subjects 7 38218458
2024 FUT8 upregulates CD36 and its core fucosylation to accelerate pericyte-myofibroblast transition through the mitochondrial-dependent apoptosis pathway during AKI-CKD. Molecular medicine (Cambridge, Mass.) 7 39563263
2021 Up-regulation of FUT8 inhibits TGF-β1-induced activation of hepatic stellate cells during liver fibrogenesis. Glycoconjugate journal 7 33608773
2025 Targeting fucosyltransferase FUT8 as a prospective therapeutic approach for DLBCL. Oncogenesis 6 39881135
2024 High-Throughput Mass Spectrometry Analysis of N-Glycans and Protein Markers after FUT8 Knockdown in the Syngeneic SW480/SW620 Colorectal Cancer Cell Model. Journal of proteome research 6 38507902
2025 Advances in cancer research on FUT8 molecular mechanisms and clinical applications. International journal of surgery (London, England) 4 40497775
2024 Identification of molecular characteristics of FUT8 and alteration of core fucosylation in kidney renal clear cell cancer. Aging 4 38277230
2023 FUT8-AS1/miR-944/Fused in Sarcoma/Transcription Factor 4 Feedback Loop Participates in the Development of Oral Squamous Cell Carcinoma through Activation of Wnt/β-Catenin Signaling Pathway. The American journal of pathology 4 36697118
2023 The Association of the Polymorphisms in the FUT8-Related Locus with the Plasma Glycosylation in Post-Traumatic Stress Disorder. International journal of molecular sciences 4 36982780
2002 Assignment of FUT8 to chicken chromosome band 5q1.4 and to human chromosome 14q23.2-->q24.1 by in situ hybridization. Conserved and compared synteny between human and chicken. Cytogenetic and genome research 4 12438718
2022 Effect and Mechanism Analysis of Pig FUT8 Gene on Resistance to Escherichia coli F18 Infection. International journal of molecular sciences 3 36499043
2025 Fut8 regulated Unc5b hyperfucosylation reduces macrophage emigration and accelerates atherosclerosis development via the ferroptosis pathway. Free radical biology & medicine 2 40262667
2025 FUT8 Is a Critical Driver of Prostate Tumour Growth and Can Be Targeted Using Fucosylation Inhibitors. Cancer medicine 2 40387385
2025 FUT8-mediated core fucosylation stabilizes TMEM67 to promote ciliogenesis. The Journal of cell biology 2 40728580
2024 FUT8 Regulates Cerebellar Neurogenesis and Development Through Maintaining the Level of Neural Cell Adhesion Molecule Cntn2. Molecular neurobiology 2 39604780
2022 Positive association of serum FUT8 activity with renal tubulointerstitial injury in IgA nephropathy patients. Immunity, inflammation and disease 2 36039648
2025 Exosomal miR-27a-5p inhibits indoxyl sulfate-induced cardiac dysfunction by targeting the USF2/FUT8 axis. Free radical biology & medicine 1 40992517
2022 [FUT8 modulates galectin-3 expression to regulate TGF-β1-mediated fibrosis of lung fibroblasts]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 1 36073215
2026 Huaier-derived neutral polysaccharide WHPB mitigates renal fibrosis via CSF-1R/PI3K/AKT-mediated FUT8 inhibition. Phytomedicine : international journal of phytotherapy and phytopharmacology 0 41505915
2026 CRISPR-based precise methylation of specific FUT8 promoter regions allows isolation of CHO cells with a fine-tuned glycoprofile. Journal of biotechnology 0 41506457
2026 Fut8-Mediated Core Fucosylation of Toll-Like Receptor 4 Exacerbates Periodontitis Via Hyperactivation of NF-κB Signalling. International dental journal 0 41653834
2026 Core fucosylation of NCEH1 by FUT8 promotes progression of high-grade serous ovarian cancer by driving tumor-associated macrophage M2 polarization. Oncogene 0 41786877
2026 FUT8 reprograms glycolytic metabolism to promote PKM2 lactylation and drive clear cell renal cell carcinoma progression. Cell death discovery 0 41857011
2025 Clinicopathologic significance of FUT8, STX4, and calpain2 expression in ovarian cancer. American journal of translational research 0 39959200
2025 Loss of FUT8 impairs embryonic development by reducing cAMP production in granulosa cells. Journal of assisted reproduction and genetics 0 40473957
2025 FUT8 promotes HDM-induced glycolysis, epithelial-mesenchymal transition and inflammation in bronchial epithelial cells by inducing N-glycosylation modification of GLUT1. Biochemical and biophysical research communications 0 41027183
2025 Genome-wide CRISPR screen identifies ALG5, ALG6, NF2, and FUT8 as key host proteins involved in transmissible gastroenteritis virus infection. International journal of biological macromolecules 0 41205942
2025 Fucoidan oligosaccharides alleviated alcoholic liver fibrosis by blocking the core fucosylation of TGF-β receptors via the JAK/STAT3/FUT8 axis. International immunopharmacology 0 41270641
2025 FUT8 Catalysis Involves GDP-Fucose-Induced Loop Activation Promoting a Reaction at the SN1‑SN2 Frontier. ACS catalysis 0 41743314
2024 Knockdown of LINC01128 Downregulates FUT8 to Inhibit OxLDL-Induced Vascular Smooth Muscle Cell Apoptosis in Atherosclerosis. Discovery medicine 0 38531797