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    UGDH UDP-glucose 6-dehydrogenase [ Homo sapiens (human) ]

    Gene ID: 7358, updated on 6-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Phenotypic and genetic characteristics of 24 cases of early infantile epileptic encephalopathy in East China, including a rare case of biallelic UGDH mutations.

    Phenotypic and genetic characteristics of 24 cases of early infantile epileptic encephalopathy in East China, including a rare case of biallelic UGDH mutations.
    Jiang L, Bi S, Lin L, He F, Deng F., Free PMC Article

    12/22/2023
    UGDH promotes tumor-initiating cells and a fibroinflammatory tumor microenvironment in ovarian cancer.

    UGDH promotes tumor-initiating cells and a fibroinflammatory tumor microenvironment in ovarian cancer.
    Harrington BS, Kamdar R, Ning F, Korrapati S, Caminear MW, Hernandez LF, Butcher D, Edmondson EF, Traficante N, Hendley J, Australian Ovarian Cancer Study, Gough M, Rogers R, Lourie R, Shetty J, Tran B, Elloumi F, Abdelmaksoud A, Nag ML, Mazan-Mamczarz K, House CD, Hooper JD, Annunziata CM., Free PMC Article

    11/1/2023
    UDP-glucose 6-dehydrogenase lessens sorafenib sensitivity via modulating unfolded protein response.

    UDP-glucose 6-dehydrogenase lessens sorafenib sensitivity via modulating unfolded protein response.
    Guo B, Xu X, Shao M, Yang X, He G, Qi K, Gu J, Wang L.

    06/11/2022
    Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase.

    Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase.
    Zimmer BM, Barycki JJ, Simpson MA., Free PMC Article

    05/22/2021
    Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis.

    Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis.
    Lin LH, Chou HC, Chang SJ, Liao EC, Tsai YT, Wei YS, Chen HY, Lin MW, Wang YS, Chien YA, Yu XR, Chan HL., Free PMC Article

    05/8/2021
    UDP-glucose 6-dehydrogenase knockout impairs migration and decreases in vivo metastatic ability of breast cancer cells.

    UDP-glucose 6-dehydrogenase knockout impairs migration and decreases in vivo metastatic ability of breast cancer cells.
    Teoh ST, Ogrodzinski MP, Lunt SY.

    02/20/2021
    UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression.

    UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression.
    Arnold JM, Gu F, Ambati CR, Rasaily U, Ramirez-Pena E, Joseph R, Manikkam M, San Martin R, Charles C, Pan Y, Chatterjee SS, Den Hollander P, Zhang W, Nagi C, Sikora AG, Rowley D, Putluri N, Zhang XH, Karanam B, Mani SA, Sreekumar A., Free PMC Article

    12/12/2020
    This study defines UGDH as a key player for the production of extracellular matrix components that are essential for human brain development.

    Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy.
    Hengel H, Bosso-Lefèvre C, Grady G, Szenker-Ravi E, Li H, Pierce S, Lebigot É, Tan TT, Eio MY, Narayanan G, Utami KH, Yau M, Handal N, Deigendesch W, Keimer R, Marzouqa HM, Gunay-Aygun M, Muriello MJ, Verhelst H, Weckhuysen S, Mahida S, Naidu S, Thomas TG, Lim JY, Tan ES, Haye D, Willemsen MAAP, Oegema R, Mitchell WG, Pierson TM, Andrews MV, Willing MC, Rodan LH, Barakat TS, van Slegtenhorst M, Gavrilova RH, Martinelli D, Gilboa T, Tamim AM, Hashem MO, AlSayed MD, Abdulrahim MM, Al-Owain M, Awaji A, Mahmoud AAH, Faqeih EA, Asmari AA, Algain SM, Jad LA, Aldhalaan HM, Helbig I, Koolen DA, Riess A, Kraegeloh-Mann I, Bauer P, Gulsuner S, Stamberger H, Ng AYJ, Tang S, Tohari S, Keren B, Schultz-Rogers LE, Klee EW, Barresi S, Tartaglia M, Mor-Shaked H, Maddirevula S, Begtrup A, Telegrafi A, Pfundt R, Schüle R, Ciruna B, Bonnard C, Pouladi MA, Stewart JC, Claridge-Chang A, Lefeber DJ, Alkuraya FS, Mathuru AS, Venkatesh B, Barycki JJ, Simpson MA, Jamuar SS, Schöls L, Reversade B., Free PMC Article

    04/18/2020
    The crystal structures of UGDH(A104L) show that the allosteric switch still adopts the E and E* states, albeit with a more rigid protein core. However, the progress curves of UGDH(A104L) do not show hysteresis, which suggests that the E* and E states are now in rapid equilibrium.

    Hysteresis and Allostery in Human UDP-Glucose Dehydrogenase Require a Flexible Protein Core.
    Beattie NR, Pioso BJ, Sidlo AM, Keul ND, Wood ZA., Free PMC Article

    08/3/2019
    These data indicate that UGDH expression and localization are an early sero-diagnostic marker in addition to a poor prognostic indicator in lung AC patients.

    Clinicopathological and prognostic significance of nuclear UGDH localization in lung adenocarcinoma.
    Hagiuda D, Nagashio R, Ichinoe M, Tsuchiya B, Igawa S, Naoki K, Satoh Y, Murakumo Y, Saegusa M, Sato Y.

    06/8/2019
    the unfolded state of the ID-tail rectifies the dynamics and structure of UGDH to favour inhibitor binding; because this entropic rectifier does not have any sequence or structural constraints, it is an easily acquired adaptation; this model implies that evolution selects for disordered segments to tune the energy landscape of proteins, which may explain the persistence of intrinsic disorder in the proteome

    The entropic force generated by intrinsically disordered segments tunes protein function.
    Keul ND, Oruganty K, Schaper Bergman ET, Beattie NR, McDonald WE, Kadirvelraj R, Gross ML, Phillips RS, Harvey SC, Wood ZA., Free PMC Article

    05/25/2019
    Data show that KLF4 upregulates UGDH expression in a mCpG-dependent manner, and UGDH is required for KLF4-induced cell migration of glioblastoma (GBM) in vitro. UGDH knockdown decreases GAG abundance in GBM cells, as well as cell proliferation and migration in vitro. In intracranial xenografts, reduced UGDH inhibits tumor growth and migration, accompanied by a decrease in the expression of extracellular matrix proteins.

    Targeting UDP-α-D-glucose 6-dehydrogenase inhibits glioblastoma growth and migration.
    Oyinlade O, Wei S, Lal B, Laterra J, Zhu H, Goodwin CR, Wang S, Ma D, Wan J, Xia S., Free PMC Article

    03/2/2019
    Data indicate that the A136M substitution in UDP-glucose dehydrogenase (hUGDH) stabilizes the hexamer.

    Allostery and Hysteresis Are Coupled in Human UDP-Glucose Dehydrogenase.
    Beattie NR, Keul ND, Sidlo AM, Wood ZA., Free PMC Article

    05/27/2017
    study has identified several new proteins like RHOC, DLG5, UGDH, TMOD3 in addition to known chemoresistance associated proteins in non-small cell lung carcinoma.

    Global proteomic profiling identifies etoposide chemoresistance markers in non-small cell lung carcinoma.
    Paul D, Chanukuppa V, Reddy PJ, Taunk K, Adhav R, Srivastava S, Santra MK, Rapole S.

    12/24/2016
    UGDH protein level in osteoarthritis cartilage was much lower than in control cartilage.

    UDP-glucose dehydrogenase modulates proteoglycan synthesis in articular chondrocytes: its possible involvement and regulation in osteoarthritis.
    Wen Y, Li J, Wang L, Tie K, Magdalou J, Chen L, Wang H., Free PMC Article

    10/31/2015
    UGDH displays hysteresis because of a slow isomerization from an inactive state (E*) to an active state (E). We show that the structure of E* constrains UGDH in a conformation that favors feedback inhibition at physiological pH.

    Hysteresis in human UDP-glucose dehydrogenase is due to a restrained hexameric structure that favors feedback inhibition.
    Kadirvelraj R, Custer GS, Keul ND, Sennett NC, Sidlo AM, Walsh RM Jr, Wood ZA.

    04/25/2015
    Kinetic analysis of wild-type UGDH and hexamer T325A showed that upon increasing enzyme concentration, which favors the hexameric species, activity was decreased and exhibited cooperativity. Cooperative kinetics was not observed in obligate dimer T325D.

    UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces.
    Hyde AS, Thelen AM, Barycki JJ, Simpson MA., Free PMC Article

    02/15/2014
    Mammalian UGDH displays hysteresis (observed as a lag in progress curves), indicating that the enzyme undergoes a slow transition from an inactive to an active state. Human UGDH is sensitive to product inhibition during the lag.

    Hysteresis and negative cooperativity in human UDP-glucose dehydrogenase.
    Kadirvelraj R, Sennett NC, Custer GS, Phillips RS, Wood ZA.

    04/20/2013
    both missense mutations significantly reducing the ability of UGDH to provide precursors for cardiac cushion formation, which is essential to subsequent valve formation.

    UDP-glucose dehydrogenase polymorphisms from patients with congenital heart valve defects disrupt enzyme stability and quaternary assembly.
    Hyde AS, Farmer EL, Easley KE, van Lammeren K, Christoffels VM, Barycki JJ, Bakkers J, Simpson MA., Free PMC Article

    12/8/2012
    Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates.

    Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates.
    Egger S, Chaikuad A, Klimacek M, Kavanagh KL, Oppermann U, Nidetzky B., Free PMC Article

    03/10/2012
    An alternate crystal structure of human UGDH (hUGDH) in complex with UDP-glucose at 2.8 A resolution, is reported.

    Structural basis of cooperativity in human UDP-glucose dehydrogenase.
    Rajakannan V, Lee HS, Chong SH, Ryu HB, Bae JY, Whang EY, Huh JW, Cho SW, Kang LW, Choe H, Robinson RC., Free PMC Article

    02/4/2012
    A structurally detailed model of UDP-alpha-D-glucose 6-dehydrogenase (UGDH) demonstrates hinge-bending motion that represents allosteric feedback inhibition and substrate-product exchange during the catalytic cycle.

    Conformational flexibility in the allosteric regulation of human UDP-α-D-glucose 6-dehydrogenase.
    Sennett NC, Kadirvelraj R, Wood ZA.

    12/24/2011
    high UGDH levels may underlie susceptibility of the orbit to localized overproduction of hyaluronan in Graves disease.

    Divergent Sp1 protein levels may underlie differential expression of UDP-glucose dehydrogenase by fibroblasts: role in susceptibility to orbital Graves disease.
    Tsui S, Fernando R, Chen B, Smith TJ., Free PMC Article

    09/10/2011
    Structure and mechanism of human UDP-glucose 6-dehydrogenase.

    Structure and mechanism of human UDP-glucose 6-dehydrogenase.
    Egger S, Chaikuad A, Kavanagh KL, Oppermann U, Nidetzky B., Free PMC Article

    09/10/2011
    An atypical allosteric mechanism in human UDP-alpha-D-glucose 6-dehydrogenase (UGDH) based on an easily acquired and identifiable structural attribute: packing defects in the protein core.

    Role of packing defects in the evolution of allostery and induced fit in human UDP-glucose dehydrogenase.
    Kadirvelraj R, Sennett NC, Polizzi SJ, Weitzel S, Wood ZA.

    09/3/2011
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