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    GPD1 glycerol-3-phosphate dehydrogenase 1 [ Homo sapiens (human) ]

    Gene ID: 2819, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Glycerol 3-phosphate dehydrogenases (1 and 2) in cancer and other diseases.

    Glycerol 3-phosphate dehydrogenases (1 and 2) in cancer and other diseases.
    Oh S, Mai XL, Kim J, de Guzman ACV, Lee JY, Park S., Free PMC Article

    09/4/2024
    Non-bioenergetic roles of mitochondrial GPD2 promote tumor progression.

    Non-bioenergetic roles of mitochondrial GPD2 promote tumor progression.
    Oh S, Jo S, Bajzikova M, Kim HS, Dao TTP, Rohlena J, Kim JM, Neuzil J, Park S., Free PMC Article

    03/8/2023
    Decreased serum levels of glycerol-3- phosphate dehydrogenase 1 and monoacylglycerol lipase act as diagnostic biomarkers for breast cancer.

    Decreased serum levels of glycerol-3- phosphate dehydrogenase 1 and monoacylglycerol lipase act as diagnostic biomarkers for breast cancer.
    Karaosmanoglu Yoneten K, Kasap M, Arga KY, Akpinar G, Utkan NZ.

    05/14/2022
    A HIF1alpha-GPD1 feedforward loop inhibits the progression of renal clear cell carcinoma via mitochondrial function and lipid metabolism.

    A HIF1α-GPD1 feedforward loop inhibits the progression of renal clear cell carcinoma via mitochondrial function and lipid metabolism.
    Liu R, Feng Y, Deng Y, Zou Z, Ye J, Cai Z, Zhu X, Liang Y, Lu J, Zhang H, Luo Y, Han Z, Zhuo Y, Xie Q, Hon CT, Liang Y, Wu CL, Zhong W., Free PMC Article

    12/11/2021
    The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes.

    The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes.
    Cristobal JR, Reyes AC, Richard JP., Free PMC Article

    03/27/2021
    [Transient infantile hypertriglyceridemia caused by GPD1 deficiency: report of two cases and literature review].

    [Transient infantile hypertriglyceridemia caused by GPD1 deficiency: report of two cases and literature review].
    Xie XB, Li MP, Wang JS.

    01/16/2021
    Bioinformatics analyses performed with differentially regulated proteins highlighted the changes occurring in triacylglyceride (TAG) metabolism, and directed our attention to TAG metabolism-associated proteins, namely glycerol-3-phosphate dehydrogenase 1 (GPD1) and monoacylglycerol lipase (MAGL).

    Comparative Proteome Analysis of Breast Cancer Tissues Highlights the Importance of Glycerol-3-phosphate Dehydrogenase 1 and Monoacylglycerol Lipase in Breast Cancer Metabolism.
    Yoneten KK, Kasap M, Akpinar G, Gunes A, Gurel B, Utkan NZ., Free PMC Article

    02/1/2020
    These results support the conclusion that the rate acceleration for Glycerol-3-Phosphate Dehydrogenase-catalyzed reactions is due to the stabilization of the transition state for hydride transfer by interactions with the protein catalyst.

    Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate Dehydrogenase.
    Reyes AC, Amyes TL, Richard JP., Free PMC Article

    04/13/2019
    To recognize this entity by considering GPD1 mutations in appropriate clinical settings.

    Expanding the molecular diversity and phenotypic spectrum of glycerol 3-phosphate dehydrogenase 1 deficiency.
    Dionisi-Vici C, Shteyer E, Niceta M, Rizzo C, Pode-Shakked B, Chillemi G, Bruselles A, Semeraro M, Barel O, Eyal E, Kol N, Haberman Y, Lahad A, Diomedi-Camassei F, Marek-Yagel D, Rechavi G, Tartaglia M, Anikster Y.

    12/9/2017
    Although these data indicate that a lack of GPD1 inhibits gluconeogenesis from glycerol, chronic GPD1 deficiency may induce an adaptation that enhances gluconeogenesis from glycogenic amino acids

    Glycerol-3-phosphate dehydrogenase 1 deficiency induces compensatory amino acid metabolism during fasting in mice.
    Sato T, Yoshida Y, Morita A, Mori N, Miura S.

    05/20/2017
    The R269A mutation of GPDH1 results in a 110-fold increase in K(m) (2.8 kcal/mol effect) and a 41,000-fold decrease in k(cat) (6.3 kcal/mol effect), which corresponds to a 9.1 kcal/mol destabilization of the transition state.

    Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.
    Reyes AC, Koudelka AP, Amyes TL, Richard JP., Free PMC Article

    03/26/2016
    massive hepatomegaly, fatty liver and severe hypertriglyceridemia carrying a compound heterozygous mutation in GPD1

    A compound heterozygous mutation in GPD1 causes hepatomegaly, steatohepatitis, and hypertriglyceridemia.
    Joshi M, Eagan J, Desai NK, Newton SA, Towne MC, Marinakis NS, Esteves KM, De Ferranti S, Bennett MJ, McIntyre A, Beggs AH, Berry GT, Agrawal PB., Free PMC Article

    06/20/2015
    Mutation analysis revealed a homozygous splicing mutation, c.361-1G>C, which resulted in an aberrantly spliced mRNA in the ten affected individuals.

    Transient infantile hypertriglyceridemia, fatty liver, and hepatic fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate dehydrogenase 1.
    Basel-Vanagaite L, Zevit N, Har Zahav A, Guo L, Parathath S, Pasmanik-Chor M, McIntyre AD, Wang J, Albin-Kaplanski A, Hartman C, Marom D, Zeharia A, Badir A, Shoerman O, Simon AJ, Rechavi G, Shohat M, Hegele RA, Fisher EA, Shamir R., Free PMC Article

    03/17/2012
    The expression levels of the GPD1 gene did not differ between patients with OSA and their matched controls. The results were not affected by the clinical and biochemical measurements, the sleep parameters or the severity of nocturnal hypoxemia.

    The influence of obstructive sleep apnea on the expression of glycerol-3-phosphate dehydrogenase 1 gene.
    Guindalini C, Lee KS, Andersen ML, Santos-Silva R, Bittencourt LR, Tufik S.

    05/10/2010
    The activities of glycerol phosphate dehydrogenase were decreased by 73% in pancreatic islets of patients with type 2 diabetes.

    Decreased levels of metabolic enzymes in pancreatic islets of patients with type 2 diabetes.
    MacDonald MJ, Longacre MJ, Langberg EC, Tibell A, Kendrick MA, Fukao T, Ostenson CG., Free PMC Article

    01/21/2010
    the discovery overexpression of GPD1 and RRBP1 proteins and lack of expression for HNRNPH1 and SERPINB6 proteins which are new candidate biomarkers of colon cancer.

    [Colorectal cancer 2D-proteomics: identification of altered protein expression].
    Krasnov GS, Oparina NIu, Khankin SL, Mashkova TD, Ershov AN, Zatsepina OG, Karpov VL, Beresten' SF.

    01/21/2010
    GPD1 has a role in increased triacylglycerol production in adipose tissue of obese humans

    Enhanced glycerol 3-phosphate dehydrogenase activity in adipose tissue of obese humans.
    Swierczynski J, Zabrocka L, Goyke E, Raczynska S, Adamonis W, Sledzinski Z.

    01/21/2010
    GpD1 is a weight-loss-responsive gene in skeletal muscle. Its observed transcriptional modulation may decrease triglyceride synthesis, with weight loss.

    GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle.
    Park JJ, Berggren JR, Hulver MW, Houmard JA, Hoffman EP.

    01/21/2010
    Identification and function of mutations in FAD-binding domain of mitochonrial glycerophosphate dehydrogenase in caucasians with type 2 diabetes mellitus.

    Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in caucasian patients with type 2 diabetes mellitus.
    Gudayol M, Vidal J, Usac EF, Morales A, Fabregat ME, Fernández-Checa JC, Novials A, Gomis R.

    01/21/2010
    The apoenzyme structure of GPD1 has been determined; an electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of structural analyses.

    Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1).
    Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z.

    01/21/2010
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