Novel 2-oxoglutarate analogues modulate the epigenetic activity of the cancer-related human enzyme aspartate/asparagine-β-hydroxylase

Novel 2-oxoglutarate analogues modulate the epigenetic activity of the cancer-related human enzyme aspartate/asparagine-β-hydroxylase

Bibliografski detalji
Glavni autori:	Brewitz, L, Tumber, A, Nakashima, Y, Schofield, CJ
Format:	Conference item
Jezik:	English
Izdano:	Wiley 2020

Slični predmeti

Synthesis of 2-oxoglutarate derivatives and their evaluation as cosubstrates and inhibitors of human aspartate/asparagine-β-hydroxylase
od: Brewitz, L, i dr.
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Kinetic parameters of human aspartate/asparagine-β-hydroxylase suggest that it has a possible function in oxygen sensing
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Synthesis of novel pyridine-carboxylates as small-molecule inhibitors of human aspartate/asparagine-β-hydroxylase
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Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors
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Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors
od: Lennart Brewitz, i dr.
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Author Correction: Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors
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Small-molecule active pharmaceutical ingredients of approved cancer therapeutics inhibit human aspartate/asparagine-β-hydroxylas
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Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
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2-oxoglutarate analogue inhibitors of HIF prolyl hydroxylase.
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Izdano: (2003)

2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2.
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Izdano: (2009)

Fluorinated derivatives of pyridine-2,4-dicarboxylate are potent inhibitors of human 2-oxoglutarate dependent oxygenases
od: Brewitz, L, i dr.
Izdano: (2021)

2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases
od: Nakashima, Y, i dr.
Izdano: (2021)

Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern
od: Inga Pfeffer, i dr.
Izdano: (2019-10-01)

Mechanistic and structural study of human aspartate/asparagine-beta-hydroxylase
od: Brasnett, A
Izdano: (2023)

2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases
od: Yu Nakashima, i dr.
Izdano: (2021-11-01)

Human prolyl hydroxylase domain 2 reacts with O 2 and 2-oxoglutarate to enable formation of inactive Fe(III).2OG.hypoxia-inducible-factor α complexes
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Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
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Quantitative MS‐based proteomics: comparing the MCF‐7 cellular response to hypoxia and a 2‐oxoglutarate analogue
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Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
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Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6.
od: Mantri, M, i dr.
Izdano: (2010)

Human prolyl hydroxylase domain 2 reacts with O2 and 2-oxoglutarate to enable formation of inactive Fe(III).2OG.hypoxia-inducible-factor α complexes
od: Giorgia Fiorini, i dr.
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Asparagine reduces the risk of schizophrenia: a bidirectional two-sample mendelian randomization study of aspartate, asparagine and schizophrenia
od: Huang-Hui Liu, i dr.
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Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes.
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2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
od: Abboud, M, i dr.
Izdano: (2018)

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
od: McNeill, L, i dr.
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Unusual catalytic strategy by non-heme Fe(ii)/2-oxoglutarate-dependent aspartyl hydroxylase AspH
od: Krishnan, A, i dr.
Izdano: (2024)

Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor.
od: Yang, M, i dr.
Izdano: (2011)

Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate.
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Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor
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p53-mediated control of aspartate-asparagine homeostasis dictates LKB1 activity and modulates cell survival
od: Longfei Deng, i dr.
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Structure-based prediction of asparagine and aspartate degradation sites in antibody variable regions.
od: Jasmin F Sydow, i dr.
Izdano: (2014-01-01)

Natural and synthetic 2-oxoglutarate derivatives are substrates for oncogenic variants of human isocitrate dehydrogenase 1 and 2
od: Liu, X, i dr.
Izdano: (2023)

Interplay between 2-oxoglutarate oxygenases and cancer: studies on the aspartyl/asparaginyl-beta-hydroxylase
od: Pfeffer, I
Izdano: (2014)

Novel Approach to Overcome Defects of Cell-SELEX in Developing Aptamers against Aspartate β‑Hydroxylase
od: Hadi Bakhtiari, i dr.
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Structural basis for binding of the renal carcinoma target hypoxia-inducible factor 2α to prolyl hydroxylase domain 2
od: Figg, WD, i dr.
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Aspartate-β-hydroxylase (ASPH): A potential therapeutic target in human malignant gliomas
od: Lisa-Marie Sturla, i dr.
Izdano: (2016-12-01)

Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor.
od: Conejo-Garcia, A, i dr.
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Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase, and flavanone 3beta-hydroxylase.
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Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid.
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2-oxoglutarate-dependent oxygenases
od: Islam, M, i dr.
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