Relevant bibliographies by topics / HIF asparaginyl hydroxylase

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Academic literature on the topic 'HIF asparaginyl hydroxylase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "HIF asparaginyl hydroxylase"

1

McNEILL, Luke A., Kirsty S. HEWITSON, Timothy D. CLARIDGE, Jürgen F. SEIBEL, Louise E. HORSFALL та Christopher J. SCHOFIELD. "Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803". Biochemical Journal 367, № 3 (2002): 571–75. http://dx.doi.org/10.1042/bj20021162.

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Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 α-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1α/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the β-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.
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Pappalardi, Melissa B., Dean E. McNulty, John D. Martin, et al. "Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites." Biochemical Journal 436, no. 2 (2011): 363–69. http://dx.doi.org/10.1042/bj20101201.

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The HIF (hypoxia-inducible factor) plays a central regulatory role in oxygen homoeostasis. HIF proteins are regulated by three Fe(II)- and α-KG (α-ketoglutarate)-dependent prolyl hydroxylase enzymes [PHD (prolyl hydroxylase domain) isoenzymes 1–3 or PHD1, PHD2 and PHD3] and one asparaginyl hydroxylase [FIH (factor inhibiting HIF)]. The prolyl hydroxylases control the abundance of HIF through oxygen-dependent hydroxylation of specific proline residues in HIF proteins, triggering subsequent ubiquitination and proteasomal degradation. FIH inhibits the HIF transcription activation through asparagi
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3

Flashman, Emily, Sarah L. Davies, Kar Kheng Yeoh, and Christopher J. Schofield. "Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents." Biochemical Journal 427, no. 1 (2010): 135–42. http://dx.doi.org/10.1042/bj20091609.

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The HIF (hypoxia-inducible factor) hydroxylases [PHDs or EGLNs (prolyl hydroxylases), which in humans are PHD isoforms 1–3, and FIH (factor inhibiting HIF)] regulate HIF levels and activity. These enzymes are Fe(II)/2-oxoglutarate-dependent oxygenases, many of which are stimulated by ascorbate. We have investigated the ascorbate dependence of PHD2-catalysed hydroxylation of two prolyl hydroxylation sites in human HIF-1α, and of FIH-catalysed hydroxylation of asparaginyl hydroxylation sites in HIF-1α and in a consensus ankyrin repeat domain peptide. The initial rate and extent of hydroxylation
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Strowitzki, Moritz, Eoin Cummins, and Cormac Taylor. "Protein Hydroxylation by Hypoxia-Inducible Factor (HIF) Hydroxylases: Unique or Ubiquitous?" Cells 8, no. 5 (2019): 384. http://dx.doi.org/10.3390/cells8050384.

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All metazoans that utilize molecular oxygen (O2) for metabolic purposes have the capacity to adapt to hypoxia, the condition that arises when O2 demand exceeds supply. This is mediated through activation of the hypoxia-inducible factor (HIF) pathway. At physiological oxygen levels (normoxia), HIF-prolyl hydroxylases (PHDs) hydroxylate proline residues on HIF-α subunits leading to their destabilization by promoting ubiquitination by the von-Hippel Lindau (VHL) ubiquitin ligase and subsequent proteasomal degradation. HIF-α transactivation is also repressed in an O2-dependent way due to asparagin
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DALGARD, Clifton Lee, Huasheng LU, Ahmed MOHYELDIN, and Ajay VERMA. "Endogenous 2-oxoacids differentially regulate expression of oxygen sensors." Biochemical Journal 380, no. 2 (2004): 419–24. http://dx.doi.org/10.1042/bj20031647.

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Adaptations to change in oxygen availability are crucial for survival of multi-cellular organisms and are also implicated in several disease states. Such adaptations rely upon gene expression regulated by the heterodimeric transcription factors HIFs (hypoxia-inducible factors). Enzymes that link changes in oxygen tensions with the stability and transcriptional activity of HIFs are considered as oxygen sensors. These enzymes are oxygen-, iron- and 2-oxoglutarate-dependent dioxygenases that hydroxylate key proline and asparagine residues in HIFα subunits. The constitutive inhibitory action of th
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6

Semenza, Gregg L. "Involvement of oxygen-sensing pathways in physiologic and pathologic erythropoiesis." Blood 114, no. 10 (2009): 2015–19. http://dx.doi.org/10.1182/blood-2009-05-189985.

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Abstract Red blood cells deliver O2 from the lungs to every cell in the human body. Reduced tissue oxygenation triggers increased production of erythropoietin by hypoxia-inducible factor 1 (HIF-1), which is a transcriptional activator composed of an O2-regulated α subunit and a constitutively expressed β subunit. Hydroxylation of HIF-1α or HIF-2α by the asparaginyl hydroxylase FIH-1 blocks coactivator binding and transactivation. Hydroxylation of HIF-1α or HIF-2α by the prolyl hydroxylase PHD2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitination and proteas
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7

Kanelakis, Kimon C., Heather L. Palomino, Lina Li, et al. "Characterization of a Robust Enzymatic Assay for Inhibitors of 2-Oxoglutarate-Dependent Hydroxylases." Journal of Biomolecular Screening 14, no. 6 (2009): 627–35. http://dx.doi.org/10.1177/1087057109333976.

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The prolyl-4-hydroxylase proteins regulate the hypoxia-inducible transcription factors (HIFs) by hydroxylation of proline residues targeting HIF-1α for proteasomal degradation. Using the purified catalytic domain of prolyl hydroxylase 2 (PHD2181-417), an enzymatic assay has been developed to test inhibitors of the enzyme in vitro. Because PHD2 hydroxylates HIF-1α, with succinic acid produced as an end product, radiolabeled [5-14C]-2-oxoglutaric acid was used and formation of [14C]-succinic acid was measured to quantify PHD2181-417 enzymatic activity. Comparison of the separation of 2-oxoglutar
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8

Webb, James D., Andrea Murányi, Christopher W. Pugh, Peter J. Ratcliffe, and Mathew L. Coleman. "MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)." Biochemical Journal 420, no. 2 (2009): 327–36. http://dx.doi.org/10.1042/bj20081905.

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The asparaginyl hydroxylase FIH [factor inhibiting HIF (hypoxia-inducible factor)] was first identified as a protein that inhibits transcriptional activation by HIF, through hydroxylation of an asparagine residue in the CAD (C-terminal activation domain). More recently, several ARD [AR (ankyrin repeat) domain]-containing proteins were identified as FIH substrates using FIH interaction assays. Although the function(s) of these ARD hydroxylations is unclear, expression of the ARD protein Notch1 was shown to compete efficiently with HIF CAD for asparagine hydroxylation and thus to enhance HIF act
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9

Lawton, Margot, Ming Tong, Fusun Gundogan, Jack R. Wands та Suzanne M. de la Monte. "Aspartyl-(asparaginyl) β-Hydroxylase, Hypoxia-Inducible Factor-1α and Notch Cross-Talk in Regulating Neuronal Motility". Oxidative Medicine and Cellular Longevity 3, № 5 (2010): 347–56. http://dx.doi.org/10.4161/oxim.3.5.13296.

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Aspartyl-(Asparaginyl)-β-Hydroxylase (AAH ) promotes cell motility by hydroxylating Notch. Insulin and insulin-like growth factor, type 1 (IGF-I) stimulate AAH through Erk MAP K and phosphoinositol-3-kinase-Akt (PI3K-Akt). However, hypoxia/oxidative stress may also regulate AAH . Hypoxia-inducible factor-1alpha (HIF-1α) regulates cell migration, signals through Notch, and is regulated by hypoxia/oxidative stress, insulin/IGF signaling and factor inhibiting HIF-1α (FIH) hydroxylation. To examine cross-talk between HIF-1α and AAH , we measured AAH , Notch-1, Jagged-1, FIH, HIF-1α, HIF-1β and the
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10

Koivunen, Peppi, Maija Hirsilä, Anne M. Remes, Ilmo E. Hassinen, Kari I. Kivirikko, and Johanna Myllyharju. "Inhibition of Hypoxia-inducible Factor (HIF) Hydroxylases by Citric Acid Cycle Intermediates." Journal of Biological Chemistry 282, no. 7 (2006): 4524–32. http://dx.doi.org/10.1074/jbc.m610415200.

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The stability and transcriptional activity of the hypoxia-inducible factors (HIFs) are regulated by two oxygen-dependent events that are catalyzed by three HIF prolyl 4-hydroxylases (HIF-P4Hs) and one HIF asparaginyl hydroxylase (FIH). We have studied possible links between metabolic pathways and HIF hydroxylases by analyzing the abilities of citric acid cycle intermediates to inhibit purified human HIF-P4Hs and FIH. Fumarate and succinate were identified as in vitro inhibitors of all three HIF-P4Hs, fumarate having Ki values of 50–80 μm and succinate 350–460 μm, whereas neither inhibited FIH.
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Dissertations / Theses on the topic "HIF asparaginyl hydroxylase"

1

Zhang, Na. "The asparaginyl hydroxylase factor Inhibiting HIF-1alpha is an essential regulator of metabolism." Diss., [La Jolla] : University of California, San Diego, 2010. http://wwwlib.umi.com/cr/ucsd/fullcit?p3404183.

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Thesis (Ph. D.)--University of California, San Diego, 2010.<br>Title from first page of PDF file (viewed June 3, 2010). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (leaves 141-143).
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2

Lancaster, David Ewan. "The post-translational hydroxylation of ankyrin repeats by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor-inhibiting HIF (FIH)." Thesis, University of Oxford, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.509972.

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Hyvärinen, J. (Jaana). "Enzymes involved in hypoxia response:characterization of the in vivo role of HIF-P4H-2 in mouse heart, of a novel P4H in human and zebrafish and of the catalytic properties of FIH." Doctoral thesis, University of Oulu, 2010. http://urn.fi/urn:isbn:9789514261947.

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Abstract Oxygen homeostasis is critical to all animals, as both excess (hyperoxia) and reduced (hypoxia) levels of oxygen can result in pathological changes and ultimately in the loss of cellular and organismal viability. Complex systems have evolved to sense and adapt to changes in cellular oxygen availability, and the hypoxia-inducible factor HIF plays a pivotal role in this elaborate molecular network. In normoxic conditions the α-subunit of HIF becomes hydroxylated by HIF prolyl 4-hydroxylases (HIF-P4Hs 1-3), earmarking HIF-α for proteasomal degradation. Additionally, in the presence of ox
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