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anti-Human PITRM1 Antibodies:
anti-Mouse (Murine) PITRM1 Antibodies:
anti-Rat (Rattus) PITRM1 Antibodies:
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Redox control of hPreP in the mitochondrial matrix and the protective role of the conserved methionine 206 residue as an internal antioxidant.
The authors identified two siblings carrying a homozygous PITRM1 missense mutation (c.548G>A, p.Arg183Gln) associated with an autosomal recessive, slowly progressive syndrome characterised by mental retardation, spinocerebellar ataxia, cognitive decline and psychosis.
Data show that the hPreP presequence only targets GFP to the matrix of mammalian and yeast mitochondria.
This study demonstrated decreased proteolytic activity of the mitochondrial amyloid-beta degrading enzyme, PreP peptidasome, in Alzheimer's disease brain mitochondria.
our data suggest that genetic variation in the hPreP gene PITRM1 may potentially contribute to mitochondrial dysfunctions
The substrate specificity of the mitochondrial metallopeptidase proteinase 1 (MP1) was investigated and its mitochondrial targeting signal identified.
Data revealed that six polymorphisms of F10 (show F10 Antibodies), PITRM1, PCSK2 (show PCSK2 Antibodies), JPH3 (show JPH3 Antibodies), MYO7B (show MYO7B Antibodies), and AKAP12 (show AKAP12 Antibodies) were related (P<0.05) to the prevalence of chronic kidney disease.
results suggest that pitrilysin regulates islet amyloid polypeptide (show IAPP Antibodies) in beta cells and suggest the presence of an intramitochondrial pool of islet amyloid polypeptide (show IAPP Antibodies) involved in beta-cell apoptosis.
Pitrm1 is expressed in Pax3 (show PAX3 Antibodies)-expressing myoblast progenitors in the limb, the dermomyotome, and developing muscles of the face and torso.
ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.
, metalloprotease 1 (pitrilysin family)
, pitrilysin metalloproteinase 1
, presequence protease, mitochondrial
, nuclear transplantation upregulated protein 1
, pitrilysin metalloprotease 1
, pitrilysin metallepetidase 1
, Pitrilysin metalloproteinase 1
, metalloprotease 1