PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2
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Summary
Using the yeast two-hybrid system, two proteins are identified that interact and colocalize with the presenilin-interacting proteins and it is hypothesized that these proteins possess a metal-dependent enzymatic, possibly protease activity.
- Type
- article
- Published
- 2001-05-14
- Cited by
- 70
- References
- 53
- OpenAlex
- https://openalex.org/W39540931
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:2685606
Keywords
Presenilin, Proteases, Biology, Membrane protein, Cell biology
References
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Cited by
- Phosphorylation and cleavage of presenilin-associated rhomboid-like protein (PARL) promotes changes in mitochondrial morphology
- Mitochondrial Fusion Proteins and Human Diseases
- The mitochondrial pathways of apoptosis.
- Functional investigation of rhomboid proteases and their substrates in Toxoplasma gondii
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- Identification and characterization of innate immune receptor substrates of γ-secretase enzyme complex
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- Protein Degradation within Mitochondria: Versatile Activities of AAA Proteases and Other Peptidases
- Transcriptional profiling of Alzheimer blood mononuclear cells by microarray.
- Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling.
- Normal mitochondrial dynamics requires rhomboid-7 and affects Drosophila lifespan and neuronal function.
- Expression in mammalian cell cultures reveals interdependent, but distinct, functions for Star and Rhomboid proteins in the processing of the Drosophila transforming-growth-factor-alpha homologue Spitz.
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- The Metabolic Theory of Pulmonary Arterial Hypertension
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- The mitochondrial rhomboid protease PSARL is a new candidate gene for type 2 diabetes
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- Presenilin: RIP and Beyond
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