Inefficient cleavage of palmitoyl-protein thioesterase (PPT) substrates by aminothiols: Implications for treatment of infantile neuronal ceroid lipofuscinosis

[1]  S. Smaalen,et al.  Crystal Structure of 6,7-Dihydro-5a,7a,13,14-tetraaza-pentaphene-5,8-dione , 2019, X-ray Structure Analysis Online.

[2]  H. Goebel,et al.  Current State of Clinical and Morphological Features in Human NCL , 2004, Brain pathology.

[3]  W. Gahl,et al.  Cystinosis. , 2002, The New England journal of medicine.

[4]  S. Hofmann,et al.  The effects of lysosomotropic agents on normal and INCL cells provide further evidence for the lysosomal nature of palmitoyl-protein thioesterase function. , 2002, Biochimica et biophysica acta.

[5]  E. Chouery,et al.  Adult neuronal ceroid lipofuscinosis with palmitoyl‐protein thioesterase deficiency: First adult‐onset patients of a childhood disease , 2001, Annals of neurology.

[6]  K. Wisniewski,et al.  Lysosomal ceroid depletion by drugs: Therapeutic implications for a hereditary neurodegenerative disease of childhood , 2001, Nature Medicine.

[7]  V. Santini.  Amifostine: chemotherapeutic and radiotherapeutic protective effects , 2001, Expert opinion on pharmacotherapy.

[8]  O. Bizzozero,et al.  Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters. , 2001, Biochimica et biophysica acta.

[9]  J. Widom,et al.  The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[10]  K. Wisniewski,et al.  Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. , 1998, The Journal of clinical investigation.

[11]  J. Suopanki,et al.  Sphingolipid activator proteins (SAPs) in neuronal ceroid lipofuscinoses (NCL). , 1997, Neuropediatrics.

[12]  David Levens,et al.  The Far Upstream Element-binding Proteins Comprise an Ancient Family of Single-strand DNA-binding Transactivators* , 1996, The Journal of Biological Chemistry.

[13]  A. Gilman,et al.  Autoacylation of G Protein α Subunits* , 1996, The Journal of Biological Chemistry.

[14]  S. Hofmann,et al.  Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[15]  L. Peltonen,et al.  Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis , 1995, Nature.

[16]  C. Slaughter,et al.  Molecular cloning and expression of palmitoyl-protein thioesterase. , 1994, The Journal of biological chemistry.

[17]  S. Hofmann,et al.  Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras. , 1993, The Journal of biological chemistry.

[18]  M. Baumann,et al.  Storage of saposins A and D in infantile neuronal ceroid‐lipofuscinosis , 1993, FEBS letters.

[19]  R. O. Oude Elferink,et al.  The intralysosomal pH in cultured human skin fibroblasts in relation to cystine accumulation in patients with cystinosis. , 1983, Biochemical and biophysical research communications.

[20]  J. Rapola,et al.  Infantile type of so-called neuronal ceroid-lipofuscinosis , 1973, Acta Neuropathologica.

[21]  J. Rapola,et al.  Infantile type of so-called neuronal ceroid-lipofuscinosis. 2. Morphological and biochemical studies. , 1973, Journal of the neurological sciences.

[22]  J. Rapola,et al.  Infantile Type of So‐called Neuronal Ceroid‐lipofuscinosis , 1973, Journal of the neurological sciences.

[23]  S. Mole.  Neuronal ceroid lipofuscinoses. , 1999, European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society.