CLPP
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TFAM
Gene Ontology Biological Process
- DNA-dependent DNA replication [TAS]
- chromatin remodeling [IBA]
- gene expression [TAS]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- regulation of transcription from RNA polymerase I promoter [TAS]
- transcription from mitochondrial promoter [IMP, TAS]
- transcription initiation from mitochondrial promoter [IDA, TAS]
Gene Ontology Molecular Function- DNA binding, bending [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IC]
- chromatin binding [IDA]
- mitochondrial light strand promoter sense binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [IMP]
- DNA binding, bending [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IC]
- chromatin binding [IDA]
- mitochondrial light strand promoter sense binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [IMP]
Gene Ontology Cellular Component
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Mitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality.
The mitochondrial caseinolytic protease P (ClpP) plays a central role in mitochondrial protein quality control by degrading misfolded proteins. Using genetic and chemical approaches, we showed that hyperactivation of the protease selectively kills cancer cells, independently of p53 status, by selective degradation of its respiratory chain protein substrates and disrupts mitochondrial structure and function, while it does not affect non-malignant cells. We identified ... [more]
Throughput
- High Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
CLPP TFAM | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | - | |
CLPP TFAM | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 3382608 |
Curated By
- BioGRID