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von Hippel–Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/9780470123188.ch9openalex-snapshot
Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4‐Hydroxylases
inferredcites →https://doi.org/10.1002/prot.1145openalex-snapshot
Linear programming optimization and a double statistical filter for protein threading protocols
inferredcites →https://doi.org/10.1006/jmbi.1999.3091openalex-snapshot
Protein secondary structure prediction based on position-specific scoring matrices 1 1Edited by G. Von Heijne
inferredcites →https://doi.org/10.1006/jmbi.2000.3741openalex-snapshot
Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. Thornton
inferredcites →https://doi.org/10.1016/s0006-291x(02)00534-xopenalex-snapshot
Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel–Lindau tumor suppressor
inferredcites →https://doi.org/10.1016/s0092-8674(01)00507-4openalex-snapshot
C. elegans EGL-9 and Mammalian Homologs Define a Family of Dioxygenases that Regulate HIF by Prolyl Hydroxylation
inferredcites →https://doi.org/10.1016/s0378-1119(01)00633-3openalex-snapshot
Characterization and comparative analysis of the EGLN gene family
inferredcites →https://doi.org/10.1038/35017054openalex-snapshot
Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel–Lindau protein
inferredcites →https://doi.org/10.1038/nature00767openalex-snapshot
Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
inferredcites →https://doi.org/10.1038/nrm703openalex-snapshot
Mechanisms of transcription-coupled DNA repair
inferredcites →https://doi.org/10.1038/sj.onc.1203985openalex-snapshot
The von Hippel-Lindau tumor suppressor gene protects cells from UV-mediated apoptosis
inferredcites →https://doi.org/10.1042/0264-6021:3530333openalex-snapshot
Inhibition of prolyl 4-hydroxylase in vitro and in vivo by members of a novel series of phenanthrolinones
inferredcites →https://doi.org/10.1073/pnas.072068399openalex-snapshot
Transcription-coupled and DNA damage-dependent ubiquitination of RNA polymerase II in vitro
inferredcites →https://doi.org/10.1073/pnas.180169797openalex-snapshot
UV-induced inhibition of transcription involves repression of transcription initiation and phosphorylation of RNA polymerase II
inferredcites →https://doi.org/10.1073/pnas.181341498openalex-snapshot
HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
inferredcites →https://doi.org/10.1073/pnas.190332597openalex-snapshot
Activation of HIF1α ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex
inferredcites →https://doi.org/10.1073/pnas.93.20.10595openalex-snapshot
Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein.
inferredcites →https://doi.org/10.1073/pnas.93.21.11586openalex-snapshot
UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells.
inferredcites →https://doi.org/10.1073/pnas.94.6.2156openalex-snapshot
The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
inferredcites →https://doi.org/10.1073/pnas.96.11.6054openalex-snapshot
Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain
inferredcites →https://doi.org/10.1074/jbc.271.32.19009openalex-snapshot
Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II
inferredcites →https://doi.org/10.1074/jbc.273.8.4689openalex-snapshot
Growth-related Changes in Phosphorylation of Yeast RNA Polymerase II
inferredcites →https://doi.org/10.1074/jbc.273.9.5184openalex-snapshot
Ultraviolet Radiation-induced Ubiquitination and Proteasomal Degradation of the Large Subunit of RNA Polymerase II
inferredcites →https://doi.org/10.1074/jbc.274.42.30109openalex-snapshot
von Hippel-Lindau Protein Induces Hypoxia-regulated Arrest of Tyrosine Hydroxylase Transcript Elongation in Pheochromocytoma Cells
inferredcites →https://doi.org/10.1074/jbc.m002740200openalex-snapshot
Hypoxia Inducible Factor-α Binding and Ubiquitylation by the von Hippel-Lindau Tumor Suppressor Protein
inferredcites →https://doi.org/10.1074/jbc.m107880200openalex-snapshot
The von Hippel-Lindau Tumor Suppressor Protein Mediates Ubiquitination of Activated Atypical Protein Kinase C
inferredcites →https://doi.org/10.1074/jbc.m108269200openalex-snapshot
Ubiquitination of a Novel Deubiquitinating Enzyme Requires Direct Binding to von Hippel-Lindau Tumor Suppressor Protein
inferredcites →https://doi.org/10.1083/jcb.129.2.287openalex-snapshot
Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains.
inferredcites →https://doi.org/10.1083/jcb.136.1.19openalex-snapshot
Splicing Factors Associate with Hyperphosphorylated RNA Polymerase II in the Absence of Pre-mRNA
inferredcites →https://doi.org/10.1093/nar/30.1.235openalex-snapshot
The PROSITE database, its status in 2002
inferredcites →https://doi.org/10.1097/00005392-199909010-00004openalex-snapshot
CLINICAL AND GENETIC CHARACTERIZATION OF PHEOCHROMOCYTOMA IN VON HIPPEL-LINDAU FAMILIES: COMPARISON WITH SPORADIC PHEOCHROMOCYTOMA GIVES INSIGHT INTO NATURAL HISTORY OF PHEOCHROMOCYTOMA
inferredcites →https://doi.org/10.1126/science.1059493openalex-snapshot
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
inferredcites →https://doi.org/10.1126/science.1059796openalex-snapshot
Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation
inferredcites →https://doi.org/10.1126/science.1059817openalex-snapshot
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
inferredcites →https://doi.org/10.1126/science.1066373openalex-snapshot
A Conserved Family of Prolyl-4-Hydroxylases That Modify HIF
inferredcites →https://doi.org/10.1126/science.1073440openalex-snapshot
Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling
inferredcites →https://doi.org/10.1126/science.284.5414.657openalex-snapshot
Rbx1, a Component of the VHL Tumor Suppressor Complex and SCF Ubiquitin Ligase
inferredcites →https://doi.org/10.1126/science.289.5476.85openalex-snapshot
fw2.2 : A Quantitative Trait Locus Key to the Evolution of Tomato Fruit Size
inferredcites →https://doi.org/10.1126/science.7660122openalex-snapshot
Inhibition of Transcription Elongation by the VHL Tumor Suppressor Protein
inferredcites →https://doi.org/10.1126/science.7660130openalex-snapshot
Binding of the von Hippel-Lindau Tumor Suppressor Protein to Elongin B and C
inferredcites →https://doi.org/10.1128/mcb.19.10.6972openalex-snapshot
Rsp5 Ubiquitin-Protein Ligase Mediates DNA Damage-Induced Degradation of the Large Subunit of RNA Polymerase II in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1128/mcb.20.4.1263-1270.2000openalex-snapshot
The Rpb6 Subunit of Fission Yeast RNA Polymerase II Is a Contact Target of the Transcription Elongation Factor TFIIS
inferredcites →https://doi.org/10.1210/jc.86.5.1999openalex-snapshot
Pheochromocytomas in von Hippel-Lindau Syndrome and Multiple Endocrine Neoplasia Type 2 Display Distinct Biochemical and Clinical Phenotypes
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4073012openalex-extracted
Identification of an E3 Ligase Regulating the Catalytic Subunit of RNA Polymerase I
inferred← citeshttps://doi.org/10.1002/9780470015902.a0006062.pub2openalex-snapshot
Renal Carcinoma and von Hippel–Lindau Disease
inferred← citeshttps://doi.org/10.1002/9780470015902.a0006062.pub3openalex-snapshot
Renal Carcinoma and von H ippel– L indau Disease
inferred← citeshttps://doi.org/10.1002/9780470048672.wecb232openalex-snapshot
Hypoxic Response and Associated Diseases
inferred← citeshttps://doi.org/10.1007/978-0-387-71518-6_32openalex-snapshot
Therapeutic Strategies that Target the HIF System
inferred← citeshttps://doi.org/10.1007/978-1-4899-7678-9_18openalex-snapshot
Modulation of the Hypoxic Response
inferred← citeshttps://doi.org/10.1007/978-1-4939-1622-1_4openalex-snapshot
VHL and HIF in Clear Cell Renal Cell Carcinoma: Molecular Abnormalities and Potential Clinical Applications
inferred← citeshttps://doi.org/10.1007/978-3-319-17903-2_3openalex-snapshot
Molecular Biology of Kidney Cancer
inferred← citeshttps://doi.org/10.1007/978-3-642-21858-3_3openalex-snapshot
Molecular Biology of Kidney Cancer
inferred← citeshttps://doi.org/10.1007/978-94-007-2199-9_4openalex-snapshot
Beyond the Antioxidant: The Double Life of Vitamin C
inferred← citeshttps://doi.org/10.1007/978-981-15-1025-0_11openalex-snapshot
The Roles of Cullin-2 E3 Ubiquitin Ligase Complex in Cancer
inferred← citeshttps://doi.org/10.1007/s00018-003-3203-8openalex-snapshot
Hopes, disillusions and more hopes from vitamin C
inferred← citeshttps://doi.org/10.1007/s00018-009-0147-7openalex-snapshot
Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing
inferred← citeshttps://doi.org/10.1007/s00018-023-04796-7openalex-snapshot
Development of VHL-recruiting STING PROTACs that suppress innate immunity
inferred← citeshttps://doi.org/10.1007/s00109-020-01951-6openalex-snapshot
Interaction with p53 explains a pro-proliferative function for VHL in cancer
inferred← citeshttps://doi.org/10.1007/s00467-007-0632-xopenalex-snapshot
Cellular oxygen sensing in health and disease
inferred← citeshttps://doi.org/10.1007/s11064-006-9268-7openalex-snapshot
Hypoxia Inducible Factor Prolyl 4-Hydroxylase Enzymes: Center Stage in the Battle Against Hypoxia, Metabolic Compromise and Oxidative Stress
inferred← citeshttps://doi.org/10.1007/s11427-006-0265-5openalex-snapshot
Interaction between Mnk2 and CBCVHL ubiquitin ligase E3 complex
inferred← citeshttps://doi.org/10.1007/s12192-021-01240-2openalex-snapshot
Hsp90 chaperone code and the tumor suppressor VHL cooperatively regulate the mitotic checkpoint
inferred← citeshttps://doi.org/10.1007/s13402-023-00780-2openalex-snapshot
The negative effect of G1958A polymorphism on MTHFD1 protein stability and HCC growth
inferred← citeshttps://doi.org/10.1016/b978-012373983-4.50014-6openalex-snapshot
REPRESSION OF GENE EXPRESSION BY TRANSCRIPTION FACTORS
inferred← citeshttps://doi.org/10.1016/b978-012373983-4.50016-xopenalex-snapshot
REGULATION OF TRANSCRIPTION FACTOR ACTIVITY
inferred← citeshttps://doi.org/10.1016/b978-012437178-1/50012-6openalex-snapshot
Repression of Gene Expression by Transcription Factors
inferred← citeshttps://doi.org/10.1016/b978-012437178-1/50014-xopenalex-snapshot
Regulation of Transcription Factor Activity
inferred← citeshttps://doi.org/10.1016/j.advenzreg.2003.11.017openalex-snapshot
The prolyl hydroxylase enzymes that act as oxygen sensors regulating destruction of hypoxia-inducible factor α
inferred← citeshttps://doi.org/10.1016/j.advenzreg.2008.12.004openalex-snapshot
iTRAQ proteomic identification of pVHL-dependent and -independent targets of Egln1 prolyl hydroxylase knockdown in renal carcinoma cells
inferred← citeshttps://doi.org/10.1016/j.advenzreg.2008.12.005openalex-snapshot
Identification of novel VHL regulated genes by transcriptomic analysis of RCC10 renal carcinoma cells
inferred← citeshttps://doi.org/10.1016/j.bbagen.2004.04.007openalex-snapshot
Cytoplasmic glycosylation of protein-hydroxyproline and its relationship to other glycosylation pathways
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2012.08.002openalex-snapshot
Ubiquitylation and degradation of elongating RNA polymerase II: The last resort
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2024.195024openalex-snapshot
Global control of RNA polymerase II
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2004.09.027openalex-snapshot
A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
inferred← citeshttps://doi.org/10.1016/j.bbrc.2005.08.140openalex-snapshot
Dioxygenases as O2-dependent regulators of the hypoxic response pathway
inferred← citeshttps://doi.org/10.1016/j.cardiores.2006.05.005openalex-snapshot
Regulating cellular oxygen sensing by hydroxylation
inferred← citeshttps://doi.org/10.1016/j.cell.2020.02.009openalex-snapshot
Regulation of the RNAPII Pool Is Integral to the DNA Damage Response
inferred← citeshttps://doi.org/10.1016/j.cellsig.2004.04.010openalex-snapshot
Signalling via the hypoxia-inducible factor-1α requires multiple posttranslational modifications
inferred← citeshttps://doi.org/10.1016/j.cellsig.2011.10.009openalex-snapshot
Roles of ubiquitin signaling in transcription regulation
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114420openalex-snapshot
DNA break induces rapid transcription repression mediated by proteasome-dependent RNAPII removal
inferred← citeshttps://doi.org/10.1016/j.chembiol.2020.06.012openalex-snapshot
Targeting Endogenous K-RAS for Degradation through the Affinity-Directed Protein Missile System
inferred← citeshttps://doi.org/10.1016/j.critrevonc.2004.09.003openalex-snapshot
When hypoxia signalling meets the ubiquitin-proteasomal pathway, new targets for cancer therapy
inferred← citeshttps://doi.org/10.1016/j.dnarep.2007.02.017openalex-snapshot
Avoiding and resolving conflicts between DNA replication and transcription
inferred← citeshttps://doi.org/10.1016/j.dnarep.2009.01.017openalex-snapshot
Damage control: DNA repair, transcription, and the ubiquitin–proteasome system
inferred← citeshttps://doi.org/10.1016/j.dnarep.2021.103128openalex-snapshot
Timely upstream events regulating nucleotide excision repair by ubiquitin-proteasome system: ubiquitin guides the way
inferred← citeshttps://doi.org/10.1016/j.dnarep.2022.103343openalex-snapshot
UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase II and are the human orthologues of yeast Def1
inferred← citeshttps://doi.org/10.1016/j.ejca.2005.08.012openalex-snapshot
Transcription inhibition: A potential strategy for cancer therapeutics
inferred← citeshttps://doi.org/10.1016/j.eururo.2015.08.007openalex-snapshot
Hypoxia, Hypoxia-inducible Transcription Factors, and Renal Cancer
inferred← citeshttps://doi.org/10.1016/j.febslet.2009.10.070openalex-snapshot
Adding structural information to the von Hippel–Lindau (VHL) tumor suppressor interaction network
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.02.026openalex-snapshot
The multifaceted von Hippel–Lindau tumour suppressor protein
inferred← citeshttps://doi.org/10.1016/j.gene.2016.05.027openalex-snapshot
The VHL short variant involves in protein quality control
inferred← citeshttps://doi.org/10.1016/j.ics.2004.08.073openalex-snapshot
Hypoxic stabilization and proteolytic degradation of erythroid-specific 5-aminolevulinate synthase
inferred← citeshttps://doi.org/10.1016/j.intimp.2004.11.009openalex-snapshot
Cytokines and the regulation of hypoxia-inducible factor (HIF)-1α
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102690openalex-snapshot
Identification of an E3 ligase that targets the catalytic subunit of RNA Polymerase I upon transcription stress
inferred← citeshttps://doi.org/10.1016/j.jhep.2007.12.021openalex-snapshot
2-Oxoglutarate-dependent oxygenases control hepcidin gene expression
inferred← citeshttps://doi.org/10.1016/j.jmb.2016.11.006openalex-snapshot
Traveling Rocky Roads: The Consequences of Transcription-Blocking DNA Lesions on RNA Polymerase II
inferred← citeshttps://doi.org/10.1016/j.jsbmb.2004.12.015openalex-snapshot
Rush hour at the promoter: How the ubiquitin-proteasome pathway polices the traffic flow of nuclear receptor-dependent transcription
inferred← citeshttps://doi.org/10.1016/j.mad.2011.03.003openalex-snapshot
Multiple roles of ubiquitination in the control of nucleotide excision repair
inferred← citeshttps://doi.org/10.1016/j.mad.2013.03.003openalex-snapshot
Arresting transcription and sentencing the cell: The consequences of blocked transcription
inferred← citeshttps://doi.org/10.1016/j.molcel.2019.09.018openalex-snapshot
PTPS Facilitates Compartmentalized LTBP1 S-Nitrosylation and Promotes Tumor Growth under Hypoxia
inferred← citeshttps://doi.org/10.1016/j.molimm.2004.09.029openalex-snapshot
l-γ-Glutamyl-l-cysteinyl-glycine (glutathione; GSH) and GSH-related enzymes in the regulation of pro- and anti-inflammatory cytokines: a signaling transcriptional scenario for redox(y) immunologic sensor(s)?
inferred← citeshttps://doi.org/10.1016/j.molmed.2004.02.004openalex-snapshot
von Hippel–Lindau tumor suppressor: not only HIF's executioner
inferred← citeshttps://doi.org/10.1016/j.neuroscience.2008.11.025openalex-snapshot
Intermittent hypoxia regulates RNA polymerase II in hippocampus and prefrontal cortex
inferred← citeshttps://doi.org/10.1016/j.path.2008.08.003openalex-snapshot
Molecular Pathology of the Genitourinary Tract: Molecular Pathology of Kidney and Testes
inferred← citeshttps://doi.org/10.1016/j.pep.2005.03.036openalex-snapshot
Cloning and characterization of the rat HIF-1α prolyl-4-hydroxylase-1 gene
inferred← citeshttps://doi.org/10.1016/j.semcancer.2020.03.012openalex-snapshot
Coalescing lessons from oxygen sensing, tumor metabolism, and epigenetics to target VHL loss in kidney cancer
inferred← citeshttps://doi.org/10.1016/j.semcdb.2005.03.006openalex-snapshot
The VHL tumor suppressor in development and disease: Functional studies in mice by conditional gene targeting
inferred← citeshttps://doi.org/10.1016/j.tibs.2007.02.005openalex-snapshot
Contending with transcriptional arrest during RNAPII transcript elongation
inferred← citeshttps://doi.org/10.1016/j.ymeth.2019.02.005openalex-snapshot
Analysis of RNA polymerase II ubiquitylation and proteasomal degradation
inferred← citeshttps://doi.org/10.1016/s0074-7696(04)42004-xopenalex-snapshot
The Hypoxia-Inducible Factor and Tumor Progression Along the Angiogenic Pathway
inferred← citeshttps://doi.org/10.1016/s1016-8478(23)13758-7openalex-snapshot
SM-20, EGL-9, and the EGLN Family of Hypoxia-inducible Factor Prolyl Hydroxylases
inferred← citeshttps://doi.org/10.1016/s1569-9056(18)33803-xopenalex-snapshot
Transcriptomic profiling of VHL-dependent long noncoding RNAs in clear cell renal cell carcinoma
inferred← citeshttps://doi.org/10.1021/cr040466qopenalex-snapshot
RNA Polymerase Encounters with DNA Damage: Transcription-Coupled Repair or Transcriptional Mutagenesis?
inferred← citeshttps://doi.org/10.1021/pr200642copenalex-snapshot
Proteomic Dissection of the von Hippel–Lindau (VHL) Interactome
inferred← citeshttps://doi.org/10.1038/emboj.2008.249openalex-snapshot
Mammalian Elongin A complex mediates DNA‐damage‐induced ubiquitylation and degradation of Rpb1
inferred← citeshttps://doi.org/10.1038/ncb2082openalex-snapshot
Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation
inferred← citeshttps://doi.org/10.1038/nchembio863openalex-snapshot
Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?
inferred← citeshttps://doi.org/10.1038/ncomms15337openalex-snapshot
VHL deficiency augments anthracycline sensitivity of clear cell renal cell carcinomas by down-regulating ALDH2
inferred← citeshttps://doi.org/10.1038/ncpneph1032openalex-snapshot
Renal involvement in tuberous sclerosis complex and von Hippel–Lindau disease: shared disease mechanisms?
inferred← citeshttps://doi.org/10.1038/nm0603-677openalex-snapshot
Regulation of angiogenesis by hypoxia: role of the HIF system
inferred← citeshttps://doi.org/10.1038/nrc1435openalex-snapshot
Transcription — guarding the genome by sensing DNA damage
inferred← citeshttps://doi.org/10.1038/nrc2502openalex-snapshot
The von Hippel–Lindau tumour suppressor protein: O2 sensing and cancer
inferred← citeshttps://doi.org/10.1038/nrc3844openalex-snapshot
VHL, the story of a tumour suppressor gene
inferred← citeshttps://doi.org/10.1038/onc.2016.495openalex-snapshot
Ubiquitination and regulation of AURKA identifies a hypoxia-independent E3 ligase activity of VHL
inferred← citeshttps://doi.org/10.1038/s41388-020-1247-yopenalex-snapshot
Di-Ras2 promotes renal cell carcinoma formation by activating the mitogen-activated protein kinase pathway in the absence of von Hippel–Lindau protein
inferred← citeshttps://doi.org/10.1038/s41388-022-02378-8openalex-snapshot
The multifaceted role of EGLN family prolyl hydroxylases in cancer: going beyond HIF regulation
inferred← citeshttps://doi.org/10.1038/s41467-022-31329-wopenalex-snapshot
DNA damage-induced transcription stress triggers the genome-wide degradation of promoter-bound Pol II
inferred← citeshttps://doi.org/10.1038/s41580-025-00915-3openalex-snapshot
Mechanisms of transcription-coupled repair and DNA damage surveillance in health and disease
inferred← citeshttps://doi.org/10.1038/s41598-017-05685-3openalex-snapshot
Interaction between von Hippel-Lindau Protein and Fatty Acid Synthase Modulates Hypoxia Target Gene Expression
inferred← citeshttps://doi.org/10.1038/s41598-018-21524-5openalex-snapshot
Consequences of VHL Loss on Global DNA Methylome
inferred← citeshttps://doi.org/10.1038/s41598-024-83187-9openalex-snapshot
SOCS domain targets ECM assembly in lung fibroblasts and experimental lung fibrosis
inferred← citeshttps://doi.org/10.1038/sj.cdd.4402313openalex-snapshot
The VHL tumor suppressor and HIF: insights from genetic studies in mice
inferred← citeshttps://doi.org/10.1038/sj.embor.7400598openalex-snapshot
The hypoxia‐inducible‐factor hydroxylases bring fresh air into hypoxia signalling
inferred← citeshttps://doi.org/10.1038/sj.ki.5000221openalex-snapshot
The VHL/HIF oxygen-sensing pathway and its relevance to kidney disease
inferred← citeshttps://doi.org/10.1039/9781782621959-00169openalex-snapshot
The Role of 2-Oxoglutarate-Dependent Oxygenases in Hypoxia Sensing
inferred← citeshttps://doi.org/10.1039/9781788012836-00219openalex-snapshot
Mammalian O2 Sensing and Signalling
inferred← citeshttps://doi.org/10.1039/b701676jopenalex-snapshot
The human oxygen sensing machinery and its manipulation
inferred← citeshttps://doi.org/10.1042/bj20050675openalex-snapshot
Analysis of the hypoxia-sensing pathway in Drosophila melanogaster
inferred← citeshttps://doi.org/10.1042/bj20071306openalex-snapshot
Enzyme substrate recognition in oxygen sensing: how the HIF trap snaps
inferred← citeshttps://doi.org/10.1073/pnas.0907052106openalex-snapshot
Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation
inferred← citeshttps://doi.org/10.1074/jbc.m110.145904openalex-snapshot
Deficiency of a Transmembrane Prolyl 4-Hydroxylase in the Zebrafish Leads to Basement Membrane Defects and Compromised Kidney Function
inferred← citeshttps://doi.org/10.1074/jbc.m115.694562openalex-snapshot
Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling
inferred← citeshttps://doi.org/10.1074/jbc.m302244200openalex-snapshot
Hypoxia Up-regulates Prolyl Hydroxylase Activity
inferred← citeshttps://doi.org/10.1074/jbc.m311412200openalex-snapshot
A Novel Hydrogen Peroxide-induced Phosphorylation and Ubiquitination Pathway Leading to RNA Polymerase II Proteolysis
inferred← citeshttps://doi.org/10.1074/jbc.m410287200openalex-snapshot
Many Amino Acid Substitutions in a Hypoxia-inducible Transcription Factor (HIF)-1α-like Peptide Cause Only Minor Changes in Its Hydroxylation by the HIF Prolyl 4-Hydroxylases
inferred← citeshttps://doi.org/10.1074/jbc.m411109200openalex-snapshot
Characterization of a Second Arabidopsis thaliana Prolyl 4-Hydroxylase with Distinct Substrate Specificity
inferred← citeshttps://doi.org/10.1074/jbc.m500600200openalex-snapshot
The Skp1 Prolyl Hydroxylase from Dictyostelium Is Related to the Hypoxia-inducible Factor-α Class of Animal Prolyl 4-Hydroxylases
inferred← citeshttps://doi.org/10.1074/jbc.m502197200openalex-snapshot
A High Throughput Screen to Identify Substrates for the Ubiquitin Ligase Rsp5
inferred← citeshttps://doi.org/10.1074/jbc.m504963200openalex-snapshot
Hypoxia-inducible Factor Prolyl 4-Hydroxylase Inhibition
inferred← citeshttps://doi.org/10.1074/jbc.m509688200openalex-snapshot
RNA Polymerase II Blockage by Cisplatin-damaged DNA
inferred← citeshttps://doi.org/10.1074/jbc.m511773200openalex-snapshot
Transcriptional Repression of Human Immunodeficiency Virus Type 1 by AP-4
inferred← citeshttps://doi.org/10.1074/jbc.m608748200openalex-snapshot
EGLN3 Prolyl Hydroxylase Regulates Skeletal Muscle Differentiation and Myogenin Protein Stability
inferred← citeshttps://doi.org/10.1074/jbc.m611648200openalex-snapshot
Interaction of Hydroxylated Collagen IV with the von Hippel-Lindau Tumor Suppressor
inferred← citeshttps://doi.org/10.1074/jbc.m704988200openalex-snapshot
An Endoplasmic Reticulum Transmembrane Prolyl 4-Hydroxylase Is Induced by Hypoxia and Acts on Hypoxia-inducible Factor α
inferred← citeshttps://doi.org/10.1080/07853890801986594openalex-snapshot
Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
inferred← citeshttps://doi.org/10.1080/10409230600648736openalex-snapshot
The General Transcription Machinery and General Cofactors
inferred← citeshttps://doi.org/10.1080/21541264.2026.2698182openalex-snapshot
RNA polymerase II removal: transcription quality control and gene regulation
inferred← citeshttps://doi.org/10.1089/ars.2007.1683openalex-snapshot
Regulated Function of the Prolyl-4-Hydroxylase Domain (PHD) Oxygen Sensor Proteins
inferred← citeshttps://doi.org/10.1089/ars.2009.2790openalex-snapshot
Iron Homeostasis and Its Interaction with Prolyl Hydroxylases
inferred← citeshttps://doi.org/10.1089/ars.2013.5186openalex-snapshot
Molecular Mechanisms of Action and Therapeutic Uses of Pharmacological Inhibitors of HIF–Prolyl 4-Hydroxylases for Treatment of Ischemic Diseases
inferred← citeshttps://doi.org/10.1091/mbc.e08-06-0566openalex-snapshot
Regulation of Renal Epithelial Tight Junctions by the von Hippel-Lindau Tumor Suppressor Gene Involves Occludin and Claudin 1 and Is Independent of E-Cadherin
inferred← citeshttps://doi.org/10.1093/emboj/cdg392openalex-snapshot
HIF prolyl‐hydroxylase 2 is the key oxygen sensor setting low steady‐state levels of HIF‐1α in normoxia
inferred← citeshttps://doi.org/10.1093/emboj/cdg410openalex-snapshot
Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel—Lindau protein
inferred← citeshttps://doi.org/10.1093/nar/gkac483openalex-snapshot
ARMC5 is part of an RPB1-specific ubiquitin ligase implicated in adrenal hyperplasia
inferred← citeshttps://doi.org/10.1093/nar/gkae618openalex-snapshot
Differential processing of RNA polymerase II at DNA damage correlates with transcription-coupled repair syndrome severity
inferred← citeshttps://doi.org/10.1097/01.asn.0000092803.69761.41openalex-snapshot
The von Hippel-Lindau Gene, Kidney Cancer, and Oxygen Sensing
inferred← citeshttps://doi.org/10.1097/cco.0b013e3282f310deopenalex-snapshot
Beyond the hypoxia-inducible factor-centric tumour suppressor model of von Hippel-Lindau
inferred← citeshttps://doi.org/10.1098/rsob.200109openalex-snapshot
The pVHL neglected functions, a tale of hypoxia-dependent and -independent regulations in cancer
inferred← citeshttps://doi.org/10.1101/2021.02.22.432201openalex-snapshot
Old players in new posts: the role of P53, ATM and DNAPK in DNA damage-related ubiquitylation-dependent removal of S2P RNAPII
inferred← citeshttps://doi.org/10.1101/2022.01.12.474993openalex-snapshot
Deep Proteome Profiling Enabled Functional Annotation and Data-Independent Quantification of Proline Hydroxylation Targets
inferred← citeshttps://doi.org/10.1101/2023.05.17.541110openalex-snapshot
Prolonged stalling of RNA Polymerase II at DNA damage explains phenotypical differences between Cockayne and UV-sensitive syndromes
inferred← citeshttps://doi.org/10.1101/2025.03.21.644538openalex-snapshot
RNA polymerase II processing facilitates DNA repair and prevents DNA damage-induced neuronal and developmental failure
inferred← citeshttps://doi.org/10.1101/2025.09.18.677100openalex-snapshot
Systems-level feedback loops maintain gene expression homeostasis following RNA polymerase II dosage perturbation
inferred← citeshttps://doi.org/10.1101/683821openalex-snapshot
Di-Ras2 Promotes Renal Cell Carcinoma Formation by Activating the MAPK Pathway in the Absence of VHL
inferred← citeshttps://doi.org/10.1101/gad.1145503openalex-snapshot
Oxygen sensing in the hypoxic response pathway: regulation of the hypoxia-inducible transcription factor
inferred← citeshttps://doi.org/10.1111/apha.12096openalex-snapshot
Prolyl 4‐hydroxylases, master regulators of the hypoxia response
inferred← citeshttps://doi.org/10.1111/boc.201200080openalex-snapshot
TCTP increases stability of hypoxia‐inducible factor 1α by interaction with and degradation of the tumour suppressor VHL
inferred← citeshttps://doi.org/10.1111/j.1469-1809.2011.00647.xopenalex-snapshot
Identification and In Silico Analysis of Novel von Hippel-Lindau (VHL) Gene Variants from a Large Population
inferred← citeshttps://doi.org/10.1111/j.1471-4159.2010.06917.xopenalex-snapshot
HIF prolyl hydroxylase inhibition increases cell viability and potentiates dopamine release in dopaminergic cells
inferred← citeshttps://doi.org/10.1111/j.1582-4934.2010.01030.xopenalex-snapshot
The role of HIF prolyl hydroxylases in tumour growth
inferred← citeshttps://doi.org/10.1111/j.1582-4934.2011.01500.xopenalex-snapshot
Activation of the prolyl‐hydroxylase oxygen‐sensing signal cascade leads to AMPK activation in cardiomyocytes
inferred← citeshttps://doi.org/10.1111/php.12647openalex-snapshot
Nucleotide Excision Repair: Finely Tuned Molecular Orchestra of Early Pre‐incision Events
inferred← citeshttps://doi.org/10.1126/scisignal.124pe30openalex-snapshot
pVHL: A Multipurpose Adaptor Protein
inferred← citeshttps://doi.org/10.1126/scisignal.2000444openalex-snapshot
Oxygen-Regulated β 2 -Adrenergic Receptor Hydroxylation by EGLN3 and Ubiquitylation by pVHL
inferred← citeshttps://doi.org/10.1128/mcb.00091-07openalex-snapshot
ELA1 and CUL3 Are Required Along with ELC1 for RNA Polymerase II Polyubiquitylation and Degradation in DNA-Damaged Yeast Cells
inferred← citeshttps://doi.org/10.1128/mcb.00757-08openalex-snapshot
Schizosaccharomyces pombe Ddb1 Recruits Substrate-Specific Adaptor Proteins through a Novel Protein Motif, the DDB-Box
inferred← citeshttps://doi.org/10.1128/mcb.01231-07openalex-snapshot
The von Hippel-Lindau Tumor Suppressor Protein and Egl-9-Type Proline Hydroxylases Regulate the Large Subunit of RNA Polymerase II in Response to Oxidative Stress
inferred← citeshttps://doi.org/10.1128/mcb.23.20.7083-7095.2003openalex-snapshot
Influence of the RNA-Binding Protein HuR in pVHL-Regulated p53 Expression in Renal Carcinoma Cells
inferred← citeshttps://doi.org/10.1139/o05-045openalex-snapshot
Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition
inferred← citeshttps://doi.org/10.1146/annurev-biochem-052621-091205openalex-snapshot
Transcription-Coupled Nucleotide Excision Repair and the Transcriptional Response to UV-Induced DNA Damage
inferred← citeshttps://doi.org/10.1146/annurev.biochem.74.082803.133142openalex-snapshot
PROLINE HYDROXYLATION AND GENE EXPRESSION
inferred← citeshttps://doi.org/10.1146/annurev.pathol.2.010506.092049openalex-snapshot
von Hippel-Lindau Disease
inferred← citeshttps://doi.org/10.1152/ajpcell.00100.2006openalex-snapshot
The prolyl hydroxylase oxygen-sensing pathway is cytoprotective and allows maintenance of mitochondrial membrane potential during metabolic inhibition
inferred← citeshttps://doi.org/10.1152/ajpcell.00466.2007openalex-snapshot
O2-sensing signal cascade: clamping of O2 respiration, reduced ATP utilization, and inducible fumarate respiration
inferred← citeshttps://doi.org/10.1152/ajpgi.90287.2008openalex-snapshot
Activation of the oxygen-sensing signal cascade prevents mitochondrial injury after mouse liver ischemia-reperfusion
inferred← citeshttps://doi.org/10.1152/ajprenal.00424.2003openalex-snapshot
The role of von Hippel-Lindau tumor suppressor protein and hypoxia in renal clear cell carcinoma
inferred← citeshttps://doi.org/10.1158/0008-5472.can-03-3139openalex-snapshot
Topoisomerase I-Mediated Inhibition of Hypoxia-Inducible Factor 1
inferred← citeshttps://doi.org/10.1158/0008-5472.can-08-0811openalex-snapshot
Melanoma Antigen-11 Inhibits the Hypoxia-Inducible Factor Prolyl Hydroxylase 2 and Activates Hypoxic Response
inferred← citeshttps://doi.org/10.1158/1078-0432.ccr-08-0730openalex-snapshot
Von Hippel-Lindau–Coupled and Transcription-Coupled Nucleotide Excision Repair–Dependent Degradation of RNA Polymerase II in Response to Trabectedin
inferred← citeshttps://doi.org/10.1158/1078-0432.ccr-09-3416openalex-snapshot
von Hippel-Lindau–Dependent Patterns of RNA Polymerase II Hydroxylation in Human Renal Clear Cell Carcinomas
inferred← citeshttps://doi.org/10.1158/1078-0432.ccr-sup-040025openalex-snapshot
The Von Hippel-Lindau Tumor Suppressor Gene and Kidney Cancer
inferred← citeshttps://doi.org/10.1158/1541-7786.89.2.2openalex-snapshot
Inhibition of Hypoxia-Inducible Factor Is Sufficient for Growth Suppression of VHL−/− Tumors
inferred← citeshttps://doi.org/10.1158/1541-7786.mcr-05-0233openalex-snapshot
The Emerging Role of the COP9 Signalosome in Cancer
inferred← citeshttps://doi.org/10.1159/000075346openalex-snapshot
von Hippel-Lindau Tumor Suppressor Protein and Hypoxia-Inducible Factor in Kidney Cancer
inferred← citeshttps://doi.org/10.1159/000093631openalex-snapshot
Molecular Pathogenetics of Renal Cancer
inferred← citeshttps://doi.org/10.1186/1897-4287-11-11openalex-snapshot
Acute myeloid leukemia in a 38-year-old hemodialyzed patient with von Hippel-Lindau disease
inferred← citeshttps://doi.org/10.1186/s13008-016-0020-7openalex-snapshot
The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions
inferred← citeshttps://doi.org/10.1186/s13059-023-03147-wopenalex-snapshot
ARMC5 controls the degradation of most Pol II subunits, and ARMC5 mutation increases neural tube defect risks in mice and humans
inferred← citeshttps://doi.org/10.1186/s40364-026-00986-0openalex-snapshot
Beyond hypoxia and ccRCC: the expanding universe of VHL novel targets and next-generation therapeutics
inferred← citeshttps://doi.org/10.1200/jco.2004.05.061openalex-snapshot
Role of VHL Gene Mutation in Human Cancer
inferred← citeshttps://doi.org/10.1200/jco.2006.08.8948openalex-snapshot
Molecular Biology of Renal Cell Cancer and the Identification of Therapeutic Targets
inferred← citeshttps://doi.org/10.1200/jco.2015.65.6140openalex-snapshot
Von Hippel-Lindau Disease: Genetics and Role of Genetic Counseling in a Multiple Neoplasia Syndrome
inferred← citeshttps://doi.org/10.1242/dev.000893openalex-snapshot
Prolyl 4-hydroxylase-1 mediates O2 signaling during development ofDictyostelium
inferred← citeshttps://doi.org/10.1242/jcs.00655openalex-snapshot
HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O2 levels
inferred← citeshttps://doi.org/10.1242/jcs.078030openalex-snapshot
A DNA-dependent stress response involving DNA-PK occurs in hypoxic cells and contributes to cellular adaptation to hypoxia
inferred← citeshttps://doi.org/10.1242/jcs.219923openalex-snapshot
Bexarotene – a novel modulator of AURKA and the primary cilium in VHL-deficient cells
inferred← citeshttps://doi.org/10.13028/2t73-hd94openalex-snapshot
Hypoxia Inducible Factors in Alcoholic Liver Disease: A Dissertation
inferred← citeshttps://doi.org/10.1351/pac200880081837openalex-snapshot
Oxygenases for oxygen sensing
inferred← citeshttps://doi.org/10.1371/journal.pbio.3001757openalex-snapshot
HypDB: A functionally annotated web-based database of the proline hydroxylation proteome
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1006478openalex-snapshot
Genotype-phenotype relations of the von Hippel-Lindau tumor suppressor inferred from a large-scale analysis of disease mutations and interactors
inferred← citeshttps://doi.org/10.1371/journal.pone.0016975openalex-snapshot
Quantitative Proteomics Identifies the Myb-Binding Protein p160 as a Novel Target of the von Hippel-Lindau Tumor Suppressor
inferred← citeshttps://doi.org/10.1371/journal.pone.0029167openalex-snapshot
The Nrf1 CNC-bZIP Protein Is Regulated by the Proteasome and Activated by Hypoxia
inferred← citeshttps://doi.org/10.1371/journal.pone.0035848openalex-snapshot
pVHL Mediates K63-Linked Ubiquitination of nCLU
inferred← citeshttps://doi.org/10.1371/journal.pone.0070030openalex-snapshot
Folliculin Contributes to VHL Tumor Suppressing Activity in Renal Cancer through Regulation of Autophagy
inferred← citeshttps://doi.org/10.1371/journal.pone.0267615openalex-snapshot
The role of p53 in the DNA damage-related ubiquitylation of S2P RNAPII
inferred← citeshttps://doi.org/10.1515/bc.2004.016openalex-snapshot
HIF hydroxylation and cellular oxygen sensing
inferred← citeshttps://doi.org/10.1515/bc.2005.146openalex-snapshot
Inhibition of mRNA deadenylation and degradation by ultraviolet light
inferred← citeshttps://doi.org/10.1586/14789450.2.3.307openalex-snapshot
Manipulation of oxygen tensions forin vitrocell culture using a hypoxic workstation
inferred← citeshttps://doi.org/10.1593/neo.06442openalex-snapshot
Ubiquitin Pathway in VHL Cancer Syndrome
inferred← citeshttps://doi.org/10.17305/bjbms.2022.7850openalex-snapshot
VHL tumor suppressor as a novel potential candidate biomarker in papillary thyroid carcinoma
inferred← citeshttps://doi.org/10.17615/29tv-bb60openalex-snapshot
Type 2B von Hippel-Lindau disease: molecular biology, tumor growth, and development
inferred← citeshttps://doi.org/10.18130/v3bp22openalex-snapshot
Regulation and Function of the Fanconi Anemia Pathway for Genome Maintenance
inferred← citeshttps://doi.org/10.18632/oncotarget.14205openalex-snapshot
UV-induced proteolysis of RNA polymerase II is mediated by VCP/p97 segregase and timely orchestration by Cockayne syndrome B protein
inferred← citeshttps://doi.org/10.2147/hp.s174655openalex-snapshot
Born to sense: biophysical analyses of the oxygen sensing prolyl hydroxylase from the simplest animal Trichoplax adhaerens
inferred← citeshttps://doi.org/10.2147/hp.s53576openalex-snapshot
PHD2: from hypoxia regulation to disease progression
inferred← citeshttps://doi.org/10.2174/138161209789649394openalex-snapshot
The VHL Tumor Suppressor: Master Regulator of HIF
inferred← citeshttps://doi.org/10.2174/138161209789649411openalex-snapshot
HIF Prolyl-4-hydroxylase Interacting Proteins: Consequences for Drug Targeting
inferred← citeshttps://doi.org/10.22215/etd/2011-09623openalex-snapshot
Identification of Nrf1 (NFE2L1) as a hypoxia-inducible factor and its oxygen-dependent regulation in vitro and in vivo
inferred← citeshttps://doi.org/10.2353/ajpath.2006.050867openalex-snapshot
Clusterin Is a Secreted Marker for a Hypoxia-Inducible Factor-Independent Function of the von Hippel-Lindau Tumor Suppressor Protein
inferred← citeshttps://doi.org/10.2353/ajpath.2006.060360openalex-snapshot
Peroxisomal Localization of Hypoxia-Inducible Factors and Hypoxia-Inducible Factor Regulatory Hydroxylases in Primary Rat Hepatocytes Exposed to Hypoxia-Reoxygenation
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