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
Haploidentical haematopoietic stem cell transplantation combined with post-transplant cyclophosphamide in neuronal ceroid lipofuscinosis: Experience in eight patients.
Song Z et al.
Medicina Clinica, 2024
Deep phenotyping and whole-exome sequencing improved the diagnostic yield for nuclear pedigrees with neurodevelopmental disorders.
Wang Q et al.
Molecular Genetics & Genomic Medicine, 2022
Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 disease.
Gardner E et al.
Human Mutation, 2019
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 2019
31345222 (PubMed )
Supplement: 12920_2019_543_MOESM6_ESM.xlsx › S5C
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
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
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