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GDP-beta-L-fucose + factor VII EGF
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GDP-beta-L-fucose + protein
GDP + ?
GDP-beta-L-fucose + protein
GDP + ?
GDP-fucose + TSR4
GDP + fucosyl-TSR4
additional information
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GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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GDP-beta-L-fucose + protein
GDP + ?
SN1-like mechanism. PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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?
GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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?
GDP-beta-L-fucose + protein
GDP + ?
SN2-like mechanism. PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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GDP-fucose + TSR4
GDP + fucosyl-TSR4
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GDP-fucose + TSR4
GDP + fucosyl-TSR4
GDP-fucose binding mode, overview. Activity with recombinant TSR4 mutants expressed in HEK293Tcells
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additional information
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adds o-fucose to epidermal growth factor-like repeats
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additional information
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adds o-fucose to epidermal growth factor-like repeats
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additional information
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the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
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additional information
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the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
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additional information
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). The O-linked fucose can also be elongated with other sugars
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additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). The O-linked fucose can also be elongated with other sugars
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additional information
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O-fucosylation of thrombospondin-1 at Ser 377, Thr 432 and Thr 489
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?
additional information
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may be involved in intracellular quality control
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?
additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs)
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-
additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs)
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Abortion, Spontaneous
poFUT1 promotes endometrial decidualization by enhancing the O-fucosylation of Notch1.
Abortion, Spontaneous
poFUT1 promotes uterine angiogenesis and vascular remodeling via enhancing the O-fucosylation on uPA.
Abortion, Spontaneous
Progesterone promotes embryo adhesion by upregulating c-Fos/c-Jun transcription factor-mediate poFUT1 expression.
Abortion, Threatened
LIF upregulates poFUT1 expression and promotes trophoblast cell migration and invasion at the fetal-maternal interface.
Adenocarcinoma
POFUT1 as a Promising Novel Biomarker of Colorectal Cancer.
Adenoma
Molecular characterization of colorectal adenomas reveals POFUT1 as a candidate driver of tumor progression.
Breast Neoplasms
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Carcinogenesis
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Carcinoma
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Carcinoma
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Carcinoma, Ductal
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Carcinoma, Hepatocellular
Author Correction: Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Carcinoma, Hepatocellular
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Carcinoma, Hepatocellular
Overexpression of protein O-fucosyltransferase 1 accelerates hepatocellular carcinoma progression via the Notch signaling pathway.
Colorectal Neoplasms
Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer.
Colorectal Neoplasms
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Colorectal Neoplasms
POFUT1 as a Promising Novel Biomarker of Colorectal Cancer.
Colorectal Neoplasms
POFUT1 promotes colorectal cancer development through the activation of Notch1 signaling.
Colorectal Neoplasms
Weighted gene coexpression analysis indicates that PLAGL2 and POFUT1 are related to the differential features of proximal and distal colorectal cancer.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Analyzing the Effects of O-Fucosylation on Secretion of ADAMTS Proteins Using Cell-Based Assays.
Dysostoses
Diseases related to Notch glycosylation.
Enterocolitis
Intestinal deletion of Pofut1 in the mouse inactivates notch signaling and causes enterocolitis.
Esophageal Neoplasms
Upregulation of Fucosyltransferase 3, 8 and protein O-Fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs).
Glioblastoma
Histology-based expression profiling yields novel prognostic markers in human glioblastoma.
Glioblastoma
POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.
Glioma
Focused microarray analysis of glyco-gene expression in human glioblastomas.
Heart Failure
Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Hidradenitis
Novel POFUT1 mutation associated with hidradenitis suppurativa-Dowling-Degos disease firm up a role for Notch signalling in the pathogenesis of this disorder.
Hidradenitis
Novel POFUT1 mutation associated with hidradenitis suppurativa-Dowling-Degos disease firm up a role for Notch signalling in the pathogenesis of this disorder: reply from the authors.
Hidradenitis Suppurativa
A new nonsense mutation in the POGLUT1 gene in two sisters with Dowling-Degos disease.
Hidradenitis Suppurativa
A novel mutation in POFUT1 gene associated with Dowling-Degos disease and hidradenitis suppurativa.
Hyperpigmentation
Phenotypic expansion of POFUT1 loss of function mutations in a disorder featuring segmental dyspigmentation with eczematous and folliculo-centric lesions.
Hyperpigmentation
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Hypopigmentation
Mutations in POFUT1, Encoding Protein O-fucosyltransferase 1, Cause Generalized Dowling-Degos Disease.
Infections
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Infections
Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.
Infections
Protein O-fucosyltransferase 2-mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection.
Keratosis, Seborrheic
Novel deletion of the POFUT1 gene associated with multiple seborrheic keratosis Dowling-Degos disease.
Liver Diseases
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Lung Neoplasms
Fucosylation genes as circulating biomarkers for lung cancer.
Lymphatic Metastasis
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Lymphatic Metastasis
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Malaria
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Malaria
Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.
Malignant Atrophic Papulosis
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Microcephaly
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Mouth Neoplasms
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Muscular Dystrophies, Limb-Girdle
Diseases related to Notch glycosylation.
Myocardial Infarction
Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Neoplasm Metastasis
Author Correction: Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasm Metastasis
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasm Metastasis
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Neoplasm Metastasis
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Neoplasms
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Neoplasms
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasms
Diseases related to Notch glycosylation.
Neoplasms
Downregulated protein O-fucosyl transferase 1 (Pofut1) expression exerts antiproliferative and antiadhesive effects on hepatocytes by inhibiting Notch signalling.
Neoplasms
Fucosylation genes as circulating biomarkers for lung cancer.
Neoplasms
Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer.
Neoplasms
Integrated analysis of genome-wide copy number alterations and gene expression in microsatellite stable, CpG island methylator phenotype-negative colon cancer.
Neoplasms
Molecular characterization of colorectal adenomas reveals POFUT1 as a candidate driver of tumor progression.
Neoplasms
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Neoplasms
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Neoplasms
POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.
Neoplasms
POFUT1 and PLAGL2 gene pair linked by a bidirectional promoter: the two in one of tumour progression in colorectal cancer?
Neoplasms
POFUT1 as a Promising Novel Biomarker of Colorectal Cancer.
Neoplasms
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Neoplasms
POFUT1 promotes colorectal cancer development through the activation of Notch1 signaling.
Neoplasms
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Neoplasms
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations.
Neoplasms
Upregulation of Fucosyltransferase 3, 8 and protein O-Fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs).
Neoplasms
Weighted gene coexpression analysis indicates that PLAGL2 and POFUT1 are related to the differential features of proximal and distal colorectal cancer.
peptide-o-fucosyltransferase deficiency
POFUT1 is dispensable for structure, function and survival of mouse podocytes.
peptide-o-fucosyltransferase deficiency
Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of notch receptor ligand interactions.
peptide-o-fucosyltransferase deficiency
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.
Psoriasis
Genetic diagnosis history and osteoarticular phenotype of a non-transfusion secondary hemochromatosis.
Skin Diseases
Phenotypic expansion of POFUT1 loss of function mutations in a disorder featuring segmental dyspigmentation with eczematous and folliculo-centric lesions.
Squamous Cell Carcinoma of Head and Neck
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Stomach Neoplasms
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Teratoma
O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation.
Urinary Bladder Neoplasms
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
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evolution
POFUT2 belongs to the classical GT-B fold family of glycosyltransferases with two closely interacting Rossmann-like domains. POFUT2 shows a variation of the classical GT-B fold
malfunction
cell proliferation of POFUT1 knockdown cells is significantly inhibited compared with that of control cells, phenotypes, overview
malfunction
knockdown and overexpression of Pofut1 inhibits and accelerates the growth, migration and invasion of hepatocellular carcinoma cells, respectively
malfunction
CRISPR-mediated knockout of POFUT1 in U2OS cells suppresses both normal Notch1 signaling, and the ligand-independent signaling associated with leukemogenic mutations of Notch1. Normal and oncogenic signaling are rescued by wild-type POFUT1 but rescue is impaired by an active-site R240A mutation
malfunction
heterozygous mutations in POFUT1 are linked to a rare skin condition, Dowling-Degos Disease. Amplification of POFUT1 is associated with several types of cancer
physiological function
the enzyme adds O-fucose through O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cellular surface and secreted proteins. ENzyme POFUT1 expression can contribute to cancer progression
physiological function
the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch. Pofut1 overexpression accelerates cell proliferation and migration in hepatocellular carcinoma cells and it promotes the binding of Notch ligand Dll1 to Notch receptor, and hence activates Notch signaling pathway in hepatocellular carcinoma cells
physiological function
both POFUT1 and POFUT2 are proposed to participate in non-canonical endoplasmic reticulum quality control pathways for the folding of Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs), respectively
physiological function
protein O-fucosylation is an important glycosylation modification and plays an important role in embryonic development. Protein O-fucosyltransferase 1 promotes trophoblast cell proliferation through activation of MAPK and PI3K/Akt signaling pathways
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
physiological function
protein O-fucosyltransferase 2 catalyzes the protein O-fucosylation, a post-translational modification found on serine/threonine residues of thrombospondin type 1 repeats
physiological function
both POFUT1 and POFUT2 participate in non-canonical endoplasmic reticulum quality control pathways for the folding of Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs), respectively
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
additional information
recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A. Structure-function analysis of POFUT2 and comparison to POFUT1
additional information
-
recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A. Structure-function analysis of POFUT2 and comparison to POFUT1
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Hofsteenge, J.; Huwiler, K.G.; Bacik B.; Hess, D.; Lawler, J.; Mosher, D.F.; Peter-Katalinic, J.
C-mannosylation and o-fuxosylation of the thrombospondin type 1 module
J. Biol. Chem.
276
6485-6498
2001
Homo sapiens
brenda
ang, Y.; Shao, L.; Shi, S.; Harris, R.J.; Spellman, M.W.; Stanley, P.; Haltiwanger, R.S.
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase
J. Biol. Chem.
276
40338-40345
2001
Candida elegans, Drosophila melanogaster, Homo sapiens (Q9H488), Homo sapiens, Mus musculus (Q91ZW2), Mus musculus
brenda
Luo, Y.; Haltiwanger, R.S.
O-fucosylation of notch occurs in the endoplasmic reticulum
J. Biol. Chem.
280
11289-11294
2005
Homo sapiens
brenda
Chigira, Y.; Oka, T.; Okajima, T.; Jigami, Y.
Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains
Glycobiology
18
303-314
2008
Homo sapiens
brenda
Chen, C.I.; Keusch, J.J.; Klein, D.; Hess, D.; Hofsteenge, J.; Gut, H.
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation
EMBO J.
31
3183-3197
2012
Homo sapiens (Q9Y2G5), Homo sapiens
brenda
Ma, L.; Dong, P.; Liu, L.; Gao, Q.; Duan, M.; Zhang, S.; Chen, S.; Xue, R.; Wang, X.
Overexpression of protein O-fucosyltransferase 1 accelerates hepatocellular carcinoma progression via the Notch signaling pathway
Biochem. Biophys. Res. Commun.
473
503-510
2016
Homo sapiens (Q9H488), Homo sapiens
brenda
Yokota, S.; Ogawara, K.; Kimura, R.; Shimizu, F.; Baba, T.; Minakawa, Y.; Higo, M.; Kasamatsu, A.; Endo-Sakamoto, Y.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Protein O-fucosyltransferase 1: a potential diagnostic marker and therapeutic target for human oral cancer
Int. J. Oncol.
43
1864-1870
2013
Homo sapiens (Q9H488), Homo sapiens
brenda
Lira-Navarrete, E.; Hurtado-Guerrero, R.
A perspective on structural and mechanistic aspects of protein O-fucosylation
Acta Crystallogr. Sect. F
74
443-450
2018
Caenorhabditis elegans (Q18014), Caenorhabditis elegans (Q8WR51), Mus musculus (Q91ZW2), Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Liu, C.; Liang, X.; Wang, J.; Zheng, Q.; Zhao, Y.; Khan, M.N.; Liu, S.; Yan, Q.
Protein O-fucosyltransferase 1 promotes trophoblast cell proliferation through activation of MAPK and PI3K/Akt signaling athways
Biomed. Pharmacother.
88
95-101
2017
Homo sapiens (Q9H488), Homo sapiens
brenda
Holdener, B.C.; Haltiwanger, R.S.
Protein O-fucosylation structure and function
Curr. Opin. Struct. Biol.
56
78-86
2019
Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Sanz, S.; Aquilini, E.; Tweedell, R.E.; Verma, G.; Hamerly, T.; Hritzo, B.; Tripathi, A.; Machado, M.; Churcher, T.S.; Rodrigues, J.A.; Izquierdo, L.; Dinglasan, R.R.
Protein O-fucosyltransferase 2 is not essential for Plasmodium berghei development
Front. Cell. Infect. Microbiol.
9
238
2019
Homo sapiens (Q9H488), Homo sapiens
brenda
McMillan, B.J.; Zimmerman, B.; Egan, E.D.; Lofgren, M.; Xu, X.; Hesser, A.; Blacklow, S.C.
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations
Glycobiology
27
777-786
2017
Homo sapiens (Q9H488), Homo sapiens
brenda
Sadeghzadeh, Z.; Khosravi, A.; Jazi, M.S.; Asadi, J.
Upregulation of fucosyltransferase 3, 8 and protein O-fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs)
Glycoconj. J.
37
319-327
2020
Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda