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ProteomicsProlyl Hydroxylase Substrate Adenylosuccinate Lyase Is An Oncogenic Driver In Triple Negative Breast Cancer
Protein hydroxylation extensively regulates cellular signaling by affecting protein stability, protein-protein interaction and protein activity, and its dysregulation contributes to the pathogenesis of various diseases including cancers. However, because of the transient nature of the enzyme-substra...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-10-02 | MSV000086231 | MassIVE
ProteomicsProlyl Hydroxylase Substrate Adenylosuccinate Lyase Is An 2 Oncogenic Driver In Triple Negative Breast Cancer
Protein hydroxylation extensively regulates cellular signaling by affecting protein stability, activity, and interactome, therefore contributing to the pathogenesis of various diseases including cancers. However, because of the transient nature of the hydroxylase-substrate interaction, identifying n...
ORGANISM(S): Homo sapiens (Human) 
2019-11-20 | PXD015790 | Pride
Egln2 prolyl hydroxylase Protein hydroxylation Adenylosuccinate lyase (adsl) 
UnknownControl of cyclin D1 and breast tumorigenesis by the EglN2 prolyl hydroxylase.
Not available
S-EPMC2788761 | biostudies-literature
TranscriptomicsChromophobe and Oncocytoma Renal Cell Carcinomas: gene expression and SNP analysis
Chromosomal abnormalities, such as structural and numerical abnormalities, are a common occurrence in cancer. The close association of homologous chromosomes during interphase, a phenomenon termed somatic chromosome pairing, has been observed in cancerous cells, but the functional consequences of so...
ORGANISM(S): Homo sapiens 
2010-05-25 | E-GEOD-8271 | biostudies-arrayexpress
ProteomicsProlyl Hydroxylase Substrate Adenylosuccinate Lyase Is An Oncogenic Driver In Triple Negative Breast Cancer
Protein hydroxylation extensively regulates cellular signaling by affecting protein stability, protein-protein interaction and protein activity, and its dysregulation contributes to the pathogenesis of various diseases including cancers. However, because of the transient nature of the enzyme-substra...
ORGANISM(S): Homo sapiens (Human) 
2020-10-06 | PXD015773 | Pride
Hydroxylation Ptm Breast cancer 
ProteomicsIdentification of EGLN2 binding partners using AP-MS
Protein binding parnters of EGLN2 were identified in response to DMOG treatment.
ORGANISM(S): Homo sapiens (Human) 
2019-11-20 | PXD015787 | Pride
Proteomics Ap-ms 
GenomicsProlyl Hydroxylase Substrate Adenylosuccinate Lyase Is An Oncogenic Driver In Triple Negative Breast Cancer
Prolyl Hydroxylase Substrate Adenylosuccinate Lyase Is An Oncogenic Driver In Triple Negative Breast Cancer
PRJNA562516 | ENA
TranscriptomicsProlyl Hydroxylase Substrate Adenylosuccinate Lyase Is An Oncogenic Driver In Triple Negative Breast Cancer
Protein hydroxylation extensively regulates cellular signaling by affecting protein stability, activity, and interactome, therefore contributing to the pathogenesis of various diseases including cancers. However, because of the transient nature of the hydroxylase-substrate interaction, identifying n...
ORGANISM(S): Homo sapiens 
2019-10-09 | GSE136414 | GEO
TranscriptomicsTuning the transcriptional response to hypoxia through HIF prolyl- and asparaginyl-hydroxylase inhibition: Microarray data
The hypoxia inducible factor (HIF) system orchestrates cellular responses to hypoxia in animals. HIF is an α/β-heterodimeric transcription factor that regulates the expression of hundreds of genes in a context dependent manner. A hypoxia-sensing component of the HIF system involves oxygen-dependen...
ORGANISM(S): Homo sapiens 
2016-08-31 | E-MTAB-4300 | biostudies-arrayexpress
TranscriptomicsTargeting EGLN2/PHD1 protects motor neurons and normalizes the astrocytic interferon response.
The egl-9 family hypoxia-inducible factor (EGLN) enzymes, also known as prolyl hydroxylase domain (PHD) enzymes, are metabolic sensors regulating inflammatory responses and cellular metabolism. Both neuroinflammation and dysregulated energy metabolism are linked to motor neuron degeneration leading ...
ORGANISM(S): Homo sapiens 
2024-09-05 | GSE260913 | GEO
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