| E3 ubiquitin ligase UBR5 promotes gemcitabine resistance in pancreatic cancer by inducing O-GlcNAcylation-mediated EMT via destabilization of OGA. | E3 ubiquitin ligase UBR5 promotes gemcitabine resistance in pancreatic cancer by inducing O-GlcNAcylation-mediated EMT via destabilization of OGA.
Du Y, Yang Z, Shi H, Chen Z, Chen R, Zhou F, Peng X, Hong T, Jiang L., Free PMC Article | 08/13/2024 |
| O-GlcNAcase regulates pluripotency states of human embryonic stem cells. | O-GlcNAcase regulates pluripotency states of human embryonic stem cells.
Liu Q, Chen C, Fan Z, Song H, Sha Y, Yu L, Wang Y, Qin W, Yi W., Free PMC Article | 08/6/2024 |
| Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex. | Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex.
Lu P, Liu Y, He M, Cao T, Yang M, Qi S, Yu H, Gao H., Free PMC Article | 11/3/2023 |
| Inhibition of O-GlcNAcase Inhibits Hematopoietic and Leukemic Stem Cell Self-Renewal and Drives Dendritic Cell Differentiation via STAT3/5 Signaling. | Inhibition of O-GlcNAcase Inhibits Hematopoietic and Leukemic Stem Cell Self-Renewal and Drives Dendritic Cell Differentiation via STAT3/5 Signaling.
Luanpitpong S, Rodboon N, Samart P, Janan M, Klaihmon P, Lorthongpanich C, U-Pratya Y, Issaragrisil S. | 01/14/2023 |
| Bacterial O-GlcNAcase genes abundance decreases in ulcerative colitis patients and its administration ameliorates colitis in mice. | Bacterial O-GlcNAcase genes abundance decreases in ulcerative colitis patients and its administration ameliorates colitis in mice.
He X, Gao J, Peng L, Hu T, Wan Y, Zhou M, Zhen P, Cao H., Free PMC Article | 01/8/2022 |
| OGA is associated with deglycosylation of NONO and the KU complex during DNA damage repair. | OGA is associated with deglycosylation of NONO and the KU complex during DNA damage repair.
Cui Y, Xie R, Zhang X, Liu Y, Hu Y, Li Y, Liu X, Yu X, Wu C., Free PMC Article | 09/25/2021 |
| Pharmacological inhibition and knockdown of O-GlcNAcase reduces cellular internalization of alpha-synuclein preformed fibrils. | Pharmacological inhibition and knockdown of O-GlcNAcase reduces cellular internalization of α-synuclein preformed fibrils.
Tavassoly O, Yue J, Vocadlo DJ. | 06/19/2021 |
| Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe. | Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe.
Kositzke A, Fan D, Wang A, Li H, Worth M, Jiang J., Free PMC Article | 04/24/2021 |
| Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity. | Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
Chatterjee A, Eshwaran R, Poschet G, Lomada S, Halawa M, Wilhelm K, Schmidt M, Hammes HP, Wieland T, Feng Y., Free PMC Article | 04/3/2021 |
| Study reports that OGA is upregulated in a wide range of human cancers and drives aerobic glycolysis and tumor growth by inhibiting pyruvate kinase M2 (PKM2). PKM2 is dynamically O-GlcNAcylated in response to changes in glucose availability. Under high glucose conditions, PKM2 is a target of OGA-associated acetyltransferase activity, which facilitates O-GlcNAcylation of PKM2 by O-GlcNAc transferase (OGT). | O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth.
Singh JP, Qian K, Lee JS, Zhou J, Han X, Zhang B, Ong Q, Ni W, Jiang M, Ruan HB, Li MD, Zhang K, Ding Z, Lee P, Singh K, Wu J, Herzog RI, Kaech S, Wendel HG, Yates JR 3rd, Han W, Sherwin RS, Nie Y, Yang X., Free PMC Article | 06/20/2020 |
| role of the tubular biomarkers NAG, kidney injury molecule-1 and neutrophil gelatinase-associated lipocalin in patients with chest pain before contrast media exposition | The role of the tubular biomarkers NAG, kidney injury molecule-1 and neutrophil gelatinase-associated lipocalin in patients with chest pain before contrast media exposition.
Schlossbauer MH, Hubauer U, Stadler S, Hupf J, Sag S, Birner C, Zimmermann M, Orso E, Fischer M, Luchner A, Maier LS, Jungbauer CG. | 03/28/2020 |
| OGT promotes carcinogenesis and metastasis of cervical cancer cells. OGT's expression is significantly upregulated in cervical cancer, and low OGT level is correlated with improved prognosis | Proteomic analysis of the OGT interactome: novel links to epithelial-mesenchymal transition and metastasis of cervical cancer.
Gao J, Yang Y, Qiu R, Zhang K, Teng X, Liu R, Wang Y., Free PMC Article | 04/27/2019 |
| Beta-N-acetylhexosaminidase substrate recognition and specificity | Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.
Li B, Li H, Hu CW, Jiang J., Free PMC Article | 02/10/2018 |
| Tax interacts with the host OGT/OGA complex and inhibits the activity of OGT-bound OGA. | Hijacking of the O-GlcNAcZYME complex by the HTLV-1 Tax oncoprotein facilitates viral transcription.
Groussaud D, Khair M, Tollenaere AI, Waast L, Kuo MS, Mangeney M, Martella C, Fardini Y, Coste S, Souidi M, Benit L, Pique C, Issad T., Free PMC Article | 12/16/2017 |
| TGFBR3 and/or MGEA5 rearrangements are much more common in hybrid hemosiderotic fibrolipomatous tumor-myxoinflammatory fibroblastic sarcomas than in classical myxoinflammatory fibroblastic sarcomas. | TGFBR3 and MGEA5 rearrangements are much more common in "hybrid" hemosiderotic fibrolipomatous tumor-myxoinflammatory fibroblastic sarcomas than in classical myxoinflammatory fibroblastic sarcomas: a morphological and fluorescence in situ hybridization study.
Zreik RT, Carter JM, Sukov WR, Ahrens WA, Fritchie KJ, Montgomery EA, Weiss SW, Folpe AL. | 08/19/2017 |
| Data suggest that the substrate specificity of O-GlcNAcase/OGA does not extend to proteins/peptides modified with S-GlcNAc (an analog of O-GlcNAc); proteins modified with S-GlcNAc appear to be stable against O-GlcNAcase/OGA hydrolysis. | The Sulfur-Linked Analogue of O-GlcNAc (S-GlcNAc) Is an Enzymatically Stable and Reasonable Structural Surrogate for O-GlcNAc at the Peptide and Protein Levels.
De Leon CA, Levine PM, Craven TW, Pratt MR., Free PMC Article | 07/29/2017 |
| hOGA forms an unusual arm-in-arm homodimer in which the catalytic domain of one monomer is covered by the stalk domain of the sister monomer to create a substrate-binding cleft. | Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.
Li B, Li H, Lu L, Jiang J., Free PMC Article | 06/24/2017 |
| OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1beta, and a purified OGA-SPT5-TIF1beta complex has elongation properties. | O-GlcNAcase Is an RNA Polymerase II Elongation Factor Coupled to Pausing Factors SPT5 and TIF1β.
Resto M, Kim BH, Fernandez AG, Abraham BJ, Zhao K, Lewis BA., Free PMC Article | 05/27/2017 |
| the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA), interact with the (A)gamma-globin promoter at the -566 GATA repressor site | O-Linked N-Acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Interact with Mi2β Protein at the Aγ-Globin Promoter.
Zhang Z, Costa FC, Tan EP, Bushue N, DiTacchio L, Costello CE, McComb ME, Whelan SA, Peterson KR, Slawson C., Free PMC Article | 05/13/2017 |
| E2F1 negatively regulates both Ogt and Mgea5 expression in an Rb1 protein-dependent manner. | E2F1 Transcription Factor Regulates O-linked N-acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Expression.
Muthusamy S, Hong KU, Dassanayaka S, Hamid T, Jones SP., Free PMC Article | 04/23/2016 |
| OGA overexpression in endothelial cells improves endothelial function and may have a beneficial effect on coronary vascular complications in diabetes. | O-GlcNAcase overexpression reverses coronary endothelial cell dysfunction in type 1 diabetic mice.
Makino A, Dai A, Han Y, Youssef KD, Wang W, Donthamsetty R, Scott BT, Wang H, Dillmann WH., Free PMC Article | 02/13/2016 |
| Amino acid composition of splice variants, post-translational modifications, and stable associations with regulatory proteins influence subcellular distribution/substrate specificity of OGA and OGT (O-linked N-acetylglucosamine transferase). [REVIEW] | O-GlcNAc transferase and O-GlcNAcase: achieving target substrate specificity.
Nagel AK, Ball LE., Free PMC Article | 06/6/2015 |
| This work identifies the first target of miR-539 in the heart and the first miRNA that regulates OGA. | MicroRNA-539 is up-regulated in failing heart, and suppresses O-GlcNAcase expression.
Muthusamy S, DeMartino AM, Watson LJ, Brittian KR, Zafir A, Dassanayaka S, Hong KU, Jones SP., Free PMC Article | 02/14/2015 |
| Report the presence of TGFBR3 and/or MGEA5 rearrangements in pleomorphic hyalinizing angiectatic tumors and the spectrum of related neoplasms. | TGFBR3 and MGEA5 rearrangements in pleomorphic hyalinizing angiectatic tumors and the spectrum of related neoplasms.
Carter JM, Sukov WR, Montgomery E, Goldblum JR, Billings SD, Fritchie KJ, Folpe AL. | 10/11/2014 |
| Estrogen replacement therapy and plyometric training influence muscle OGT and OGA gene expression, which may be one of the mechanisms by which HRT and PT prevent aging-related loss of muscle mass. | OGT and OGA expression in postmenopausal skeletal muscle associates with hormone replacement therapy and muscle cross-sectional area.
Toivonen MH, Pöllänen E, Ahtiainen M, Suominen H, Taaffe DR, Cheng S, Takala T, Kujala UM, Tammi MI, Sipilä S, Kovanen V. | 08/9/2014 |