Associated Papers
A computational approach to analyzing the functional and structural impacts of Tripeptidyl-Peptidase 1 missense mutations in neuronal ceroid lipofuscinosis.
K P et al.
Metabolic Brain Disease, 2024
Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 disease.
Gardner E et al.
Human Mutation, 2019
Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
Pal A et al.
The Journal of Biological Chemistry, 2009
Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Guhaniyogi J et al.
The Journal of Biological Chemistry, 2009
19038967 (PubMed )
Supplement: M806943200_1.pdf
Atypical CLN2 with later onset and prolonged course: a neuropathologic study showing different sensitivity of neuronal subpopulations to TPP1 deficiency.
Elleder M et al.
Acta Neuropathologica, 2008
Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes.
Steinfeld R et al.
Human Molecular Genetics, 2004
Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations.
Lin L et al.
Human Mutation, 2001
Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
Sleat DE et al.
American Journal of Human Genetics, 1999
Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5.
Mole SE et al.
Human Mutation, 1999
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