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The protein encoded by PPT1 is a small glycoprotein involved in the catabolism of lipid-modified proteins during lysosomal degradation. Additionally we are shipping PPT1 Antibodies (106) and PPT1 Proteins (14) and many more products for this protein.
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Targeting PPT1 blocks mTOR (show FRAP1 ELISA Kits) signaling in a manner distinct from catalytic inhibitors, while concurrently inhibiting autophagy, thereby providing a new strategy for cancer therapy.
the combination of elevated glycolysis and deficient MRPL13 activity was closely linked to CLN1-mediated tumor activity in human hepatoma cells
Proteomics analysis on isolated cilia revealed 660 proteins, which differed in their abundance levels between wild type and Ppt1 knock out.
we reveal the existence of a positive feedback loop, where palmitoylation of PPT1 results in decreased activity and subsequent elevation in the amount of palmitoylated proteins.
analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells
Data (including data from knockout mice) suggest that deficiency of PPT1 leads to accumulation of granular osmiophilic deposits in many cell types, especially in astrocytes. [review-like article]
Data suggest that human monocytes and macrophages express PPT1; PPT1 appears to contribute 32-40% of 2-arachidonylglycerol hydrolysis activity in THP1 monocyte cell line.
This neuroimaging finding in PPT1-related neuronal ceroid lipofuscinosis was not previously reported.
Stop codon read-through with PTC124 induces palmitoyl-protein thioesterase-1 activity, reduces thioester load and suppresses apoptosis in cultured cells from Infantile neuronal ceroid lipofuscinosis patients.
Results describe the correlation between the three-dimensional structural changes in mutant palmitoyl protein thioesterase 1 and biochemical phenotypes.
Our results indicate that PPT1 deficiency causes alterations in the mitochondrial respiratory chain.
In the novel Cln1(R151X) mouse model of INCL.
Parkinson-like motor/sensorimotor deficits in Cln1-/- mice are not mediated by dopamine deficiency.
Data show that Cln1 mutations disrupt the maturation of cathepsin D (show CTSD ELISA Kits) in lysosome contributing to neuropathology of infantile neuronal ceroid lipofuscinoses and suggest cathepsin D (show CTSD ELISA Kits) deficiency to be common link between infantile and congenital form.
The authors have generated a Cln1 R151X point mutation mouse model that recapitulates the molecular, neuropathological and behavioral phenotypes of neuronal ceroid lipofuscinoses.
Data (including data from knockout mice) suggest that deficiency of Ppt1 leads to accumulation of granular osmiophilic deposits in many cell types, especially in astrocytes. [review-like article]
Data suggest that mouse macrophages express PPT1; PPT1 appears to contribute to 2-arachidonylglycerol hydrolysis activity in peritoneal macrophages in culture.
The simultaneous loss of both Cln1 and Cln5 genes might enhance the typical pathological phenotypes of these mice by disrupting or downregulating shared or convergent pathogenic pathways.
These results uncover a previously unknown phenotype associated with PPT1 deficiency, that of altered thermoregulation, which is associated with impaired lipolysis and neurotransmitter release to brown adipose tissue during cold exposure.
The protein encoded by this gene is a small glycoprotein involved in the catabolism of lipid-modified proteins during lysosomal degradation. The encoded enzyme removes thioester-linked fatty acyl groups such as palmitate from cysteine residues. Defects in this gene are a cause of infantile neuronal ceroid lipofuscinosis 1 (CLN1, or INCL) and neuronal ceroid lipofuscinosis 4 (CLN4). Two transcript variants encoding different isoforms have been found for this gene.
ceroid-palmitoyl-palmitoyl-protein thioesterase 1
, palmitoyl-protein hydrolase 1
, palmitoyl-protein thioesterase 1
, palmitoyl-protein thioesterase 1 (ceroid-lipofuscinosis, neuronal 1, infantile)
, palmitoyl protein thioesterase
, Palmitoyl-protein hydrolase 1
, palmitoyl-protein thioesterase 1 L homeolog