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The reports the crystal structure of the N-terminal domain of TIN2 (zeige TINF2 Proteine) in complex with TIN2 (zeige TINF2 Proteine)-binding motifs from TPP1 and TRF2 (zeige TERF2 Proteine), revealing how TIN2 (zeige TINF2 Proteine) interacts cooperatively with TPP1 and TRF2 (zeige TERF2 Proteine).
TPP1 cleaves and destabilizes fibrillar amyloid-beta at multiple sites in a time- and pH-dependent manner.
To confirm clinical suspicion of CLN2 disease, the recommended gold standard for laboratory diagnosis is demonstration of deficient TPP1 enzyme activity (in leukocytes, fibroblasts, or dried blood spots) and the identification of causative mutations in each allele of the TPP1/CLN2 gene.
These studies indicate that optimal treatment outcomes for CLN2 disease may require delivery of TPP1 systemically as well as directly to the central nervous system.
TPP1 is overexpressed in hepatocellular carcinoma tissues and significantly correlated with poor prognosis of hepatocellular carcinoma patients.RFX5 acts as a direct positive transcriptional regulator of TPP1 in hepatocellular carcinoma.
TPP1(CLN2) mutation is associated with neuronal ceroid lipofuscinosis (zeige CLN6 Proteine).
To our knowledge, our results bring the first evidence of a mechanism that links TPP-1 deficiency and oxidative stress-induced (zeige SQSTM1 Proteine) changes in mitochondrial morphology.
hypothesize that loss of function variants abolishing TPP1 enzyme activity lead to CLN2 disease, whereas variants that diminish TPP1 enzyme activity lead to SCAR7
This study demonistrated that the CLN2 gene 4 mutation in late infantile neuronal ceroid lipofuscinosis (zeige CLN6 Proteine).
TPP1 mutants utilize the advantages of a zebrafish model for understanding the pathogenesis of late infantile (or classic late infantile neuronal ceroid lipofuscinosis (zeige CLN6 Proteine)) disease.
telomeres are protected from hyper-resection through the repression of the ATM (zeige ATM Proteine) and ATR kinases by TRF2 (zeige TERF2 Proteine) and TPP1-bound POT1a (zeige POT1 Proteine)/b, respectively.
Rssults suggested that CLN2, CLN3 (zeige CLN3 Proteine) and CLN5 (zeige CLN5 Proteine) genes may play an important role in early embryonal neurogenesis.
demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 (zeige TINF2 Proteine) phenocopy the POT1a (zeige POT1 Proteine),b knockout setting without showing additional phenotypes
Gemfibrozil and fenofibrate, Food and Drug Administration-approved lipid-lowering drugs, up-regulate tripeptidyl-peptidase 1 in brain cells via peroxisome proliferator-activated receptor alpha (zeige PPARA Proteine) and may have implications in late infantile Batten disease therapy
TPPI activity becomes crucial for the neuronal functions later in development.
Telomere protection by TPP1/POT1 (zeige POT1 Proteine) requires tethering to TIN2 (zeige TINF2 Proteine).
TPP1 protects telomere integrity and regulates telomerase recruitment to telomeres, thereby preventing early occurrence of degenerative skin pathologies.
TPP1 deletion resulted in the release of POT1a (zeige POT1 Proteine) and POT1b from chromatin and loss of these proteins from telomeres, indicating that TPP1 is required for the telomere association of POT1a (zeige POT1 Proteine) and POT1b but not for their stability.
Lysosomal degradation of cholecystokinin (zeige CCK Proteine)-(29-33)-amide in mouse brain is dependent on this enzyme: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis (zeige CLN6 Proteine) (tripeptidyl peptidase-I)
TPP-I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B
This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.
ceroid-lipofuscinosis, neuronal 2
, tripeptidyl-peptidase 1
, cell growth-inhibiting gene 1 protein
, growth-inhibiting protein 1
, lysosomal pepstatin insensitive protease
, tripeptidyl aminopeptidase
, lysosomal pepstatin-insensitive protease
, tripeptidyl peptidase 1
, tripeptidyl-peptidase I
, tripeptidyl peptidase-I