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Article

Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis.

The EMBO journal - 1 Oct 1996

Hellsten E, Vesa J, Olkkonen V M, Jalanko A, Peltonen L

Abstract excerpt

Palmitoyl protein thioesterase (PPT) is an enzyme that removes palmitate residues from various S-acylated proteins in vitro. We recently identified mutations in the human PPT gene in patients suffering from a neurodegenerative disease in childhood, infantile neuronal ceroid lipofuscinosis (INCL),...

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Biological Transport
COS Cells
Endoplasmic Reticulum
Glycosylation
Molecular Weight
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

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PMID: 8895569
PMCID: PMC452268

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-8895569-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

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Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis.PMID 8895569Read ↗

Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL).Semantic proximity Read ↗

Neuronal trafficking of palmitoyl protein thioesterase provides an excellent model to study the effects of different mutations which cause infantile neuronal ceroid lipofuscinocis.Semantic proximity Read ↗

cDNA and Genomic Cloning of Human Palmitoyl-Protein Thioesterase (PPT), the Enzyme Defective in Infantile Neuronal Ceroid LipofuscinosisSemantic proximity Read ↗

Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1)--distinct characteristics in neurons.Semantic proximity Read ↗

Reversible Cysteine Acylation Regulates the Activity of Human Palmitoyl-Protein Thioesterase 1 (PPT1).Semantic proximity Read ↗

Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

Infantile neuronal ceroid lipofuscinosis: no longer just a 'Finnish' disease.Semantic proximity Read ↗

Detection of eight novel palmitoyl protein thioesterase (PPT) mutations underlying infantile neuronal ceroid lipofuscinosis (INCL;CLN1).Semantic proximity Read ↗

Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S.Semantic proximity Read ↗

Proteomics insights into infantile neuronal ceroid lipofuscinosis (CLN1) point to the involvement of cilia pathology in the disease.Semantic proximity Read ↗

Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2).Semantic proximity Read ↗

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