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Arthritis, Rheumatoid
Quantitative histochemical study of hyaluronic acid binding protein and the activity of uridine diphosphoglucose dehydrogenase in the synovium of patients with rheumatoid arthritis.
Arthritis, Rheumatoid
The synovial proteome: analysis of fibroblast-like synoviocytes.
Arthritis, Rheumatoid
Uridine diphosphoglucose dehydrogenase activity in synovial lining cells in the experimental antigen induced model of rheumatoid arthritis: an indication of synovial lining cell function.
Brain Diseases
Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy.
Breast Neoplasms
Correction: UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression.
Breast Neoplasms
Identification and cloning of a novel androgen-responsive gene, uridine diphosphoglucose dehydrogenase, in human breast cancer cells.
Breast Neoplasms
Identification and Cloning of a Novel Androgen-Responsive Gene, Uridine Diphosphoglucose Dehydrogenase, in Human Breast Cancer Cells1.
Breast Neoplasms
Inhibition of Human UDP-Glucose Dehydrogenase Expression Using siRNA Expression Vector in Breast Cancer Cells
Breast Neoplasms
Inhibition of human UDP-glucose dehydrogenase expression using siRNA expression vector in breast cancer cells.
Breast Neoplasms
Initial Identification of UDP-Glucose Dehydrogenase as a Prognostic Marker in Breast Cancer Patients, Which Facilitates Epirubicin Resistance and Regulates Hyaluronan Synthesis in MDA-MB-231 Cells.
Breast Neoplasms
UDP-glucose 6-dehydrogenase knockout impairs migration and decreases in vivo metastatic ability of breast cancer cells.
Breast Neoplasms
UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression.
Colorectal Neoplasms
Down-regulation of UDP-glucose dehydrogenase affects glycosaminoglycans synthesis and motility in HCT-8 colorectal carcinoma cells.
Granuloma
[Adrenocortical hormones and biosynthesis of acid mucopolysaccharides. II. UDPG:NAD oxidoreductase activity in the subcutaneous granuloma of adrenalectomized rats treated with cortisone, corticosterone and aldosterone]
Granulomatous Disease, Chronic
Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Granulibacter bethesdensis.
Graves Disease
Divergent Sp1 protein levels may underlie differential expression of UDP-glucose dehydrogenase by fibroblasts: role in susceptibility to orbital Graves disease.
Liver Neoplasms
Biochemical and histochemical properties of hepatic tumors of rainbow trout, Oncorhynchus mykiss.
Neoplasm Metastasis
Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis.
Neoplasms
Uridine diphosphoglucose dehydrogenase of mast cell tumours.
Osteoarthritis
UDP-glucose dehydrogenase modulates proteoglycan synthesis in articular chondrocytes: its possible involvement and regulation in osteoarthritis.
Ovarian Neoplasms
Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis.
Periodontitis
[UDP-glucose dehydrogenase and beta-glucuronidase activities in the gingival tissue of dogs with experimental periodontitis (author's transl)]
Prostatic Neoplasms
UDP-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer.
Rheumatoid Nodule
Palisading cells of rheumatoid nodules: comparison with synovial intimal cells.
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0.00726 - 2.21
UDP-alpha-D-glucose
0.011 - 0.017
UDP-glucose
0.05617
5-azido-UDP-glucose
-
22°C, pH 8.7
additional information
additional information
Michaelis-Menten kinetic, cooperative kinetic behavior occurs in the hexameric enzyme
-
0.048
NAD+
mutant A104L, K0.5 value, Hill coefficient 1, pH 7.5, 25°C
0.09
NAD+
mutant A136M, Hill coefficient, pH 7.5, 25°C
0.1
NAD+
mutant E161Q, pH 8.7, 25°C
0.384
NAD+
wild-type, pH 8.7, 25°C
0.646
NAD+
pH 7.4, 37°C, recombinant His-tagged wild-type enzyme
0.7
NAD+
wild-type, pH 8.7, 25°C
0.78
NAD+
wild-type, Hill coefficient 0.73, pH 7.5, 25°C
0.897
NAD+
pH 7.4, 37°C, recombinant His-tagged mutant T325A
0.942
NAD+
wild-type, pH 7.5, 25°C, Hill coefficient 0.74
1.084
NAD+
pH 7.4, 37°C, recombinant His-tagged mutant T325D
1.16
NAD+
wild-type, K0.5 value, Hill coefficient 0.69, pH 7.5, 25°C
2.92
NAD+
mutant K94E, pH 7.5, 25°C
6.3
NAD+
mutant K94E, pH 8.7, 25°C
0.00726
UDP-alpha-D-glucose
mutant A136M, Hill coefficient, pH 7.5, 25°C
0.0076
UDP-alpha-D-glucose
wild-type, K0.5 value, Hill coefficient 1, pH 7.5, 25°C
0.0094
UDP-alpha-D-glucose
mutant A104L, K0.5 value, Hill coefficient 1, pH 7.5, 25°C
0.0097
UDP-alpha-D-glucose
wild-type, Hill coefficient 1, pH 7.5, 25°C
0.015
UDP-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged mutant T325D
0.016
UDP-alpha-D-glucose
wild-type, pH 7.5, 25°C
0.025
UDP-alpha-D-glucose
wild-type, pH 8.7, 25°C
0.034
UDP-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged wild-type enzyme
0.035
UDP-alpha-D-glucose
wild-type, pH 8.7, 25°C
0.048
UDP-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged mutant T325A
0.055
UDP-alpha-D-glucose
mutant E161Q, pH 8.7, 25°C
0.269
UDP-alpha-D-glucose
mutant K94E, pH 7.5, 25°C
2.21
UDP-alpha-D-glucose
mutant K94E, pH 8.7, 25°C
0.011
UDP-glucose
pH 7.4, 22°C
0.017
UDP-glucose
pH 8.7, 25°C
0.13
NAD+
-
-
0.133
NAD+
-
wild-type, pH 8.7, 22°C
0.401
NAD+
-
mutant A222Q/S233G, pH 8.7, 22°C
0.42
NAD+
-
wild-type, pH 7.4, 22°C
0.53
NAD+
-
mutant K339A, pH 7.4, 22°C
2.1
NAD+
-
mutant K339A, pH 7.4, 22°C
0.017
UDP
-
wild-type, pH 8.7, 22°C
0.017
UDP
-
wild type enzyme, at pH 8.7 and 25°C
0.98
UDP
-
mutant A222Q/S233G, pH 8.7, 22°C
0.98
UDP
-
mutant enzyme A222Q/S233G, at pH 8.7 and 25°C
0.0092
UDP-glucose
-
wild-type, pH 7.4, 22°C
0.01703
UDP-glucose
-
22°C, pH 8.7
0.022
UDP-glucose
-
mutant K339A, pH 7.4, 22°C
1.5
UDP-glucose
-
mutant K339A, pH 7.4, 22°C
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A104L
ubstitution introduced to fill a cavity in the E state and sterically prevent repacking of the core into the inactive Eomega state. Mutant A104L does not show hysteresis or negative cooperativity, binds UDP-xylose with lower affinity and the inhibition is no longer cooperative
A136M
mutant does not exhibit substrate cooperativity. The inhibitor affinity of A136M is reduced 14fold and does not exhibit hysteresis. Substitution disrupts NAD+-induced negative cooperativity
A222Q/S233G
is a dimer in solution
A44V
mutation is the genetic cause of a developmental epileptic encephalopathy in a consanguineous Palestinian family with three affected siblings. The A44V variant is also found in two additional families from Puerto Rico and from Spain
C276A
is a hexamer-dimer mixture
D280A
extremely poor enzymic activity
D280N
shows, exclusively, a hexameric quaternary structure in solution
DELTA132
deletion of residue Val132 from the Thr131 loop to approximate an intermediate state in the allosteric transition. The crystal structure of the deletion construct reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the construct as a hexamer with point group symmetry 32, similar to that of the active complex. The DELTA132 and UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces
E110A
site-directed mutagenesis, the mutant, although dimeric in the apo form, exhibits only about 50% reduction in Vmax, but is highly unstable in solution and in cultured cells so it cannot be evaluated unambiguously
E161Q
hydrolysis step becomes completely rate-limiting so that a thioester enzyme intermediate accumulates at steady state. Crystallization of E161Q in the presence of 5 mM UDP-glucose and 2 mM NAD results in trapping a thiohemiacetal enzyme intermediate
G13E
normal expression and stability of mutant, no enzymic activity, no photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
N224A
steady-state kinetic parameters are within an order of magnitude of the native enzyme
T131S
steady-state kinetic parameters are within an order of magnitude of the native enzyme
T325A
site-directed mutagenesis, the mutant occurs as dimeric species that can be induced to form hexamers in the ternary complex with substrate and cofactor. The inducible hexamer shows that upon increasing enzyme concentration, which favors the hexameric species, activity is modestly decreased and exhibits cooperativity. The T325A mutant is significantly less efficient in promoting downstream hyaluronan production by HEK293 cells than the wild-type. The activity of the T325A mutant is the most labile, with a half-life of only 24 h that is not extended significantly by substrate and cofactor addition
T325D
site-directed mutagenesis, the mutant yields exclusively dimeric species. The T325D mutant is significantly less efficient in promoting downstream hyaluronan production by HEK293 cells than the wild-type. UGDH T325D retains its activity similarly to the wild-type enzyme but does not exhibit increased stability in the abortive ternary complex
A222Q/S233G
-
mutation does not affect expression, stability, and secondary structure. Mutant protein is a dimer and catalytic active, with increased Km values for substrates
C276A
-
site-directed mutagenesis, strong decrease in specific activity
C276E
-
activity is not measurable at pH 8.7, 22°C
C276G
-
activity is not measurable at pH 8.7, 22°C
C276K
-
activity is not measurable at pH 8.7, 22°C
C276L
-
activity is not measurable at pH 8.7, 22°C
C276S
-
site-directed mutagenesis, strong decrease in specific activity
C276Y
-
activity is not measurable at pH 8.7, 22°C
D280E
-
site-directed mutagenesis, 3-fold increase in Km for UDP-glucose and a 2-fold reduced Vmax relative to that of the wild type
K220A
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220H
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220R
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K279A
-
site-directed mutagenesis, strong decrease in specific activity
K339A
-
site-directed mutagenesis, 165fold decrease in affinity for UDP-glucose. Mutant forms a dimer, in contrast to hexameric wild-type
C276S
no enzymic activity, affinity for NAD+ similar to wild-type, retains predominantly hexameric structure
K220A
shows, exclusively, a hexameric quaternary structure in solution
K220A
extremely poor enzymic activity
K279A
no enzymic activity, affinity for NAD+ similar to wild-type, almost exclusively found as dimer
K279A
is essentially a dimer
K94E
mutation in the hexamer-building interface, generates a stable enzyme dimer. 160fold decrease in kcat value
K94E
substitution prevents hexamer formation. Mutant does not display hysteresis
D280N
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
D280N
-
an inactive UGDH mutant
additional information
perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH
additional information
-
perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH
additional information
UDP-glucose dehydrogenase mutants are engineered to perturb hexamer:dimer quaternary structure equilibrium. Dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. The purified enzymes reveal a significant decrease in the enzymatic activity of the obligate dimer and hexamer mutants. The activity of the truncated DELTA132 mutant is negligible. The half-life of UGDH catalytic activity in vitro is reduced by mutations at the dimer interface
additional information
UGDH specific siRNAs markedly inhibits UGDH mRNA and protein expression, and leads to an obvious suppression of PGs synthesis in human articular chondrocytes
additional information
introduction of site-specific unnatural amino acids to facilitate crosslinking of monomeric subunits into predominantly obligate oligomeric species. Optimal crosslinking is achieved by encoding 4-benzoyl-L-phenylalanine at position 458, and exposing to long wavelength UV in the presence of substrate and cofactor. Purified hexameric complexes contain significant fractions of dimer and trimer (approximately 50%) along with another 10% tetramer and higher molecular mass species. Activity of the crosslinked enzyme is reduced by almost 60% relative to the uncrosslinked UGDH mutant
additional information
-
introduction of site-specific unnatural amino acids to facilitate crosslinking of monomeric subunits into predominantly obligate oligomeric species. Optimal crosslinking is achieved by encoding 4-benzoyl-L-phenylalanine at position 458, and exposing to long wavelength UV in the presence of substrate and cofactor. Purified hexameric complexes contain significant fractions of dimer and trimer (approximately 50%) along with another 10% tetramer and higher molecular mass species. Activity of the crosslinked enzyme is reduced by almost 60% relative to the uncrosslinked UGDH mutant
additional information
-
UGDH overexpression stimulates hyaluronan production in HEK293 cells
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Grubb, M.F.; Kasofsky, J.; Strong, J.; Anderson, L.W.; Cysyk, R.L.
Serum stimulation of UDP-glucose dehydrogenase activity in swiss 3T3 fibroblasts
Biochem. Mol. Biol. Int.
30
819-827
1993
Homo sapiens
brenda
Sommer, B.J.; Barycki, J.J.; Simpson, M.A.
Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive oxidations
J. Biol. Chem.
279
23590-23596
2004
Homo sapiens (O60701), Homo sapiens
brenda
Huh, J.W.; Yoon, H.Y.; Lee, H.J.; Choi, W.B.; Yang, S.J.; Cho, S.W.
Importance of Gly-13 for the coenzyme binding of human UDP-glucose dehydrogenase
J. Biol. Chem.
279
37491-37498
2004
Homo sapiens (O60701), Homo sapiens
brenda
Huh, J.W.; Lee, H.J.; Choi, M.M.; Yang, S.J.; Yoon, S.Y.; Kim, D.W.; Kim, S.Y.; Choi, S.Y.; Cho, S.W.
Identification of a UDP-glucose-binding site of human UDP-glucose dehydrogenase by photoaffinity labeling and cassette mutagenesis
Bioconjug. Chem.
16
710-716
2005
Homo sapiens
brenda
Huh, J.W.; Choi, M.M.; Yang, S.J.; Yoon, S.Y.; Choi, S.Y.; Cho, S.W.
Inhibition of human UDP-glucose dehydrogenase expression using siRNA expression vector in breast cancer cells
Biotechnol. Lett.
27
1229-1232
2005
Homo sapiens
brenda
Huh, J.W.; Robinson, R.C.; Lee, H.S.; Lee, J.I.; Heo, Y.S.; Kim, H.T.; Lee, H.J.; Cho, S.W.; Choe, H.
Expression, purification, crystallization, and preliminary X-ray analysis of the human UDP-glucose dehydrogenase
Protein Pept. Lett.
13
859-862
2006
Homo sapiens
brenda
Easley, K.E.; Sommer, B.J.; Boanca, G.; Barycki, J.J.; Simpson, M.A.
Characterization of human UDP-glucose dehydrogenase reveals critical catalytic roles for lysine 220 and aspartate 280
Biochemistry
46
369-378
2007
Homo sapiens
brenda
Huh, J.W.; Yang, S.J.; Hwang, E.Y.; Choi, M.M.; Lee, H.J.; Kim, E.A.; Choi, S.Y.; Choi, J.; Hong, H.N.; Cho, S.W.
Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation
J. Biochem. Mol. Biol.
40
690-696
2007
Homo sapiens
brenda
Lee, H.S.; Son, Y.J.; Chong, S.H.; Bae, J.Y.; Leem, C.H.; Jang, Y.J.; Choe, H.
Computational analysis of the quaternary structural changes induced by point mutations in human UDP-glucose dehydrogenase
Arch. Biochem. Biophys.
486
35-43
2009
Homo sapiens (O60701), Homo sapiens
brenda
Hwang, E.Y.; Huh, J.W.; Choi, M.M.; Choi, S.Y.; Hong, H.N.; Cho, S.W.
Inhibitory effects of gallic acid and quercetin on UDP-glucose dehydrogenase activity
FEBS Lett.
582
3793-3797
2008
Homo sapiens
brenda
Huang, D.; Casale, G.P.; Tian, J.; Lele, S.M.; Pisarev, V.M.; Simpson, M.A.; Hemstreet, G.P.
UDP-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer
Int. J. Cancer
126
315-327
2009
Homo sapiens
brenda
Wei, Q.; Galbenus, R.; Raza, A.; Cerny, R.L.; Simpson, M.A.
Androgen-stimulated UDP-glucose dehydrogenase expression limits prostate androgen availability without impacting hyaluronan levels
Cancer Res.
69
2332-2339
2009
Homo sapiens
brenda
Sennett, N.C.; Kadirvelraj, R.; Wood, Z.A.
Conformational flexibility in the allosteric regulation of human UDP-alpha-D-glucose 6-dehydrogenase
Biochemistry
50
9651-9663
2011
Homo sapiens (O60701)
brenda
Sennett, N.C.; Kadirvelraj, R.; Wood, Z.A.
Cofactor binding triggers a molecular switch to allosterically activate human UDP-alpha-D-glucose 6-dehydrogenase
Biochemistry
51
9364-9374
2012
Homo sapiens (O60701)
brenda
Kadirvelraj, R.; Sennett, N.C.; Custer, G.S.; Phillips, R.S.; Wood, Z.A.
Hysteresis and negative cooperativity in human UDP-glucose dehydrogenase
Biochemistry
52
1456-1465
2013
Homo sapiens (O60701), Homo sapiens
brenda
Egger, S.; Chaikuad, A.; Klimacek, M.; Kavanagh, K.L.; Oppermann, U.; Nidetzky, B.
Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates
J. Biol. Chem.
287
2119-2129
2012
Homo sapiens (O60701), Homo sapiens
brenda
Rajakannan, V.; Lee, H.S.; Chong, S.H.; Ryu, H.B.; Bae, J.Y.; Whang, E.Y.; Huh, J.W.; Cho, S.W.; Kang, L.W.; Choe, H.; Robinson, R.C.
Structural basis of cooperativity in human UDP-glucose dehydrogenase
PLoS ONE
6
e25226
2011
Homo sapiens (O60701), Homo sapiens
brenda
Wen, Y.; Li, J.; Wang, L.; Tie, K.; Magdalou, J.; Chen, L.; Wang, H.
UDP-glucose dehydrogenase modulates proteoglycan synthesis in articular chondrocytes: its possible involvement and regulation in osteoarthritis
Arthritis Res. Ther.
16
484-494
2014
Homo sapiens (O60701), Rattus norvegicus (O70199), Rattus norvegicus Wistar (O70199)
brenda
Hyde, A.S.; Thelen, A.M.; Barycki, J.J.; Simpson, M.A.
UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces
J. Biol. Chem.
288
35049-35057
2013
Homo sapiens (O60701)
brenda
Grady, G.; Thelen, A.; Albers, J.; Ju, T.; Guo, J.; Barycki, J.J.; Simpson, M.A.
Inhibiting hexamer disassembly of human UDP-glucose dehydrogenase by photoactivated amino acid cross-linking
Biochemistry
55
3157-3164
2016
Homo sapiens (O60701), Homo sapiens
brenda
Beattie, N.; Keul, N.; Sidlo, A.; Wood, Z.
Allostery and hysteresis are coupled in human UDP-glucose dehydrogenase
Biochemistry
56
202-211
2017
Homo sapiens (O60701), Homo sapiens
brenda
Beattie, N.R.; Pioso, B.J.; Sidlo, A.M.; Keul, N.D.; Wood, Z.A.
Hysteresis and allostery in human UDP-glucose dehydrogenase require a flexible protein core
Biochemistry
57
6848-6859
2018
Homo sapiens (O60701), Homo sapiens
brenda
Vitale, D.L.; Caon, I.; Parnigoni, A.; Sevic, I.; Spinelli, F.M.; Icardi, A.; Passi, A.; Vigetti, D.; Alaniz, L.
Initial identification of UDP-glucose dehydrogenase as a prognostic marker in breast cancer patients, which facilitates epirubicin resistance and regulates hyaluronan synthesis in MDA-MB-231 cells
Biomolecules
11
246
2021
Homo sapiens (O60701), Homo sapiens
brenda
Weyler, C.; Bureik, M.; Heinzle, E.
Selective oxidation of UDP-glucose to UDP-glucuronic acid using permeabilized Schizosaccharomyces pombe expressing human UDP-glucose 6-dehydrogenase
Biotechnol. Lett.
38
477-481
2016
Homo sapiens (O60701), Homo sapiens
brenda
Teoh, S.T.; Ogrodzinski, M.P.; Lunt, S.Y.
UDP-glucose 6-dehydrogenase knockout impairs migration and decreases in vivo metastatic ability of breast cancer cells
Cancer Lett.
492
21-30
2020
Homo sapiens (O60701), Mus musculus (O70475), Mus musculus
brenda
Lin, L.H.; Chou, H.C.; Chang, S.J.; Liao, E.C.; Tsai, Y.T.; Wei, Y.S.; Chen, H.Y.; Lin, M.W.; Wang, Y.S.; Chien, Y.A.; Yu, X.R.; Chan, H.L.
Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis
J. Cell. Mol. Med.
24
11883-11902
2020
Homo sapiens (O60701), Homo sapiens
brenda
Scoglio, S.; Lo Curcio, V.; Catalani, S.; Palma, F.; Battistelli, S.; Benedetti, S.
Inhibitory effects of Aphanizomenon flos-aquae constituents on human UDP-glucose dehydrogenase activity
J. Enzyme Inhib. Med. Chem.
31
1492-1497
2016
Homo sapiens (O60701), Homo sapiens
brenda
Hengel, H.; Bosso-Lefevre, C.; Grady, G.; Szenker-Ravi, E.; Li, H.; Pierce, S.; Lebigot, E.; Tan, T.T.; Eio, M.Y.; Narayanan, G.; Utami, K.H.; Yau, M.; Handal, N.; Deigendesch, W.; Keimer, R.; Marzouqa, H.M.; Gunay-Aygun, M.; Muriello, M.J.; Verhelst, H.; Weckhuysen, S.; Mahida, S.; Naidu, S.; Thomas, T.G.
Loss-of-function mutations in UDP-glucose 6-dehydrogenase cause recessive developmental epileptic encephalopathy
Nat. Commun.
11
595
2020
Danio rerio (A8WGP7), Danio rerio, Homo sapiens (O60701), Homo sapiens
brenda
Arnold, J.M.; Gu, F.; Ambati, C.R.; Rasaily, U.; Ramirez-Pena, E.; Joseph, R.; Manikkam, M.; San Martin, R.; Charles, C.; Pan, Y.; Chatterjee, S.S.; Den Hollander, P.; Zhang, W.; Nagi, C.; Sikora, A.G.; Rowley, D.; Putluri, N.; Zhang, X.H.; Karanam, B.; Mani, S.A.; Sreekumar, A.
UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression
Oncogene
39
3089-3101
2020
Homo sapiens (O60701), Homo sapiens
brenda