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ProteomicsRegulation of the HTRA2 protease activity by PDZ domain-binding peptide ligands and the influence on HTRA2-specific protein interaction networks in retinal tissues
For the identification of HTRA2-specific protein interaction partners in retinal tissues of the house swine (Sus scrofa), we performed co-immunoprecipitation experiments with recombinant 6His-tag HTRA2 followed by quantitative LC-MS-based proteomics (see Fig. 2A and File S1). In brief, 2 µg recombin...
ORGANISM(S): Homo sapiens (Human) Sus scrofa domesticus (domestic pig) 
2021-10-11 | PXD024442 | Pride
Htra2  neuroprotection  retina  interaction partners  co-immunoprecipitation  mass spectrometry 
TranscriptomicsTranscription profiling of mouse brain tissue from HtrA2 knockouts
Cellular stress responses can be activated following functional defects in organelles such as mitochondria and the endoplasmic reticulum. Mitochondrial dysfunction caused by loss of the serine protease HtrA2 leads to a progressive movement disorder in mice and has been linked to parkinsonian neurode...
ORGANISM(S): Mus musculus 
2009-01-13 | E-GEOD-13033 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of mouse HtrA2 knockout mice with a movement disorder (possible Parkinsons model) reveals mitochondrial dysfunction by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
Cellular stress responses can be activated following functional defects in organelles such as mitochondria and the endoplasmic reticulum. Mitochondrial dysfunction caused by loss of the serine protease HtrA2 leads to a progressive movement disorder in mice and has been linked to parkinsonian neurode...
ORGANISM(S): Mus musculus 
2008-12-05 | E-GEOD-13035 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of mouse embryonic fibroblasts from HtrA2 knockoutafter rotenone treatment. HtrA2 knockout mice have a movement disorder which may be similar to Parkinsons disease
Cellular stress responses can be activated following functional defects in organelles such as mitochondria and the endoplasmic reticulum. Mitochondrial dysfunction caused by loss of the serine protease HtrA2 leads to a progressive movement disorder in mice and has been linked to parkinsonian neurode...
ORGANISM(S): Mus musculus 
2009-01-13 | E-GEOD-13034 | biostudies-arrayexpress
GenomicsGene expression profiling of HtrA2/Omi S400D mice liver
Gene expression profiling of HtrA2/Omi S400D mice liver
PRJNA924820 | ENA
GenomicsGene expression profiling of HUVECs with different HtrA2/Omi
Gene expression profiling of HUVECs with different HtrA2/Omi
PRJNA832707 | ENA
TranscriptomicsGene expression profiling of HtrA2/Omi S400D mice liver
To study the role of HtrA2/Omi S400 phosphorylation, we generated knock in mice with HtrA2/Omi S400D mutation which mimics constitutive S400 phosphorylation of HtrA2/Omi.
ORGANISM(S): Mus musculus 
2023-01-29 | GSE223095 | GEO
TranscriptomicsGene expression profiling of HUVECs with different HtrA2/Omi
Our previous experiments suggested that HtrA2/Omi could regulate the transcription of certain genes through its PDZ domain. Here, we used an inducible Tet-On system to mimic stress-induced HtrA2/Omi upregulation and RNA sequencing to study its influence.
ORGANISM(S): Homo sapiens 
2022-05-12 | GSE201703 | GEO
UnknownNovel variant Pro143Ala in HTRA2 contributes to Parkinson's disease by inducing hyperphosphorylation of HTRA2 protein in mitochondria.
Not available
S-EPMC3214265 | biostudies-literature
TranscriptomicsDifferentially expressed genes in brain tissue from HtrA2 knockout mice
Cellular stress responses can be activated following functional defects in organelles such as mitochondria and the endoplasmic reticulum. Mitochondrial dysfunction caused by loss of the serine protease HtrA2 leads to a progressive movement disorder in mice and has been linked to parkinsonian neurode...
ORGANISM(S): Mus musculus 
2008-12-01 | GSE13033 | GEO
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