Results 101 to 110 of about 2,448 (132)

Tripeptidyl-peptidase 1 in neuronal ceroid lipofuscinoses and other lysosomal storage disorders

European Journal of Paediatric Neurology, 2001
The classic late infantile form of neuronal ceroid lipofuscinosis (CLN2, cLINCL) is associated with mutations in the gene encoding tripeptidyl-peptidase I (TPP-I), a lysosomal aminopeptidase that cleaves off tripeptides from the free N-termini of oligopeptides.
Krystyna E. Wisniewski, Elizabeth Kida, Mariusz Walus, Peter Wujek, Wojciech Kaczmarski, Adam A. Golabek   +5 more
openaire   +1 more source

Intrathecal tripeptidyl-peptidase 1 reduces lysosomal storage in a canine model of late infantile neuronal ceroid lipofuscinosis

Molecular Genetics and Metabolism, 2011
Late infantile neuronal ceroid lipofuscinosis (LINCL) is caused by mutations in the gene encoding tripeptidyl-peptidase 1 (TPP1). LINCL patients accumulate lysosomal storage materials in the CNS accompanied by neurodegeneration, blindness, and functional decline.
Brian R, Vuillemenot, Martin L, Katz, Joan R, Coates, Derek, Kennedy, Pascale, Tiger, Shinichi, Kanazono, Peter, Lobel, Istvan, Sohar, Su, Xu, Rhea, Cahayag, Steve, Keve, Eugen, Koren, Stuart, Bunting, Laurie S, Tsuruda, Charles A, O'Neill   +14 more
openaire   +2 more sources

Validity of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease

Clinica Chimica Acta, 2019
CLN2 disease is a genetic disorder caused by dysfunction of the lysosomal enzyme tripeptidyl peptidase 1 (TPP1) that belongs to the neuronal ceroid lipofuscinoses (NCL) and leads to epilepsy, dementia, and death in young persons. CLN2 disease has recently become treatable by enzyme replacement, which can only be effective when the disease is diagnosed ...
Zoltan Lukacs, Miriam Nickel, Simona Murko, Paulina Nieves Cobos, Angela Schulz, René Santer, Alfried Kohlschütter   +6 more
openaire   +2 more sources

[Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation].

Voprosy meditsinskoi khimii, 2003
The data on biochemical and molecular-genetic diagnostics of a hereditary lisosomal storage disease, late infantile neuronal ceroid lipofuscinosis (CLN2) are presented. The disease is associated with a hereditary deficiency of pepstatin-unsensitive peptidase--tripeptidylpeptidase 1 (TPP1)--caused by mutations in the TPP1-coding gene CLN2.
A M, Bukina, I V, Tsvetkova, A N, Semiachkina, E S, Il'ina   +3 more
openaire   +1 more source

A computational approach to analyzing the functional and structural impacts of Tripeptidyl-Peptidase 1 missense mutations in neuronal ceroid lipofuscinosis

Metabolic Brain Disease
Neuronal ceroid-lipofuscinosis (NCLs) are a group of severe neurodegenerative conditions, most likely present in infantile, late infantile, juvenile, and adult-onset forms. Their phenotypic characteristics comprise eyesight damage, reduced motor activity and cognitive function, and sometimes tend to die in the initial stage.
Priyanka K, Priya N Madhana, Rajalakshmanan Eswaramoorthy, Magesh Ramasamy   +3 more
openaire   +2 more sources

Twelve-year experience with a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease

Molecular Genetics and Metabolism, 2019
CLN2 disease is a lysosomal storage disorder that belongs to the neuronal ceroid lipofuscinoses (NCL) and progressively leads to dementia, blindness and early death. It is caused by a deficiency of the lysosomal enzyme tripeptidyl peptidase 1 (TPP1). The disease has recently gained interest as an enzyme replacement therapy has become available.
Zoltan Lukacs, Miriam Nickel, Simona Murko, Paulina Nieves Cobos, Angela Schulz, René Santer, Alfried Kohlschütter   +6 more
openaire   +1 more source

Tripeptidyl-peptidase II (TPP II) inhibitory activity of ( S )-2,3-dihydro-2-(1 H -imidazol-2-yl)-1 H -indoles, a systematic SAR evaluation. Part 2

Bioorganic & Medicinal Chemistry Letters, 2003
We have systematically explored the structure-activity relationship (SAR) for a series of compounds 2 as inhibitors of tripeptidyl-peptidase II (TPP II), a serine protease responsible for the degradation of cholecystokinin-8 (CCK-8). This SAR evaluation of the core structure 2 suggest a fairly restrictive pharmacophore for such related structures, but ...
Henry J, Breslin, Tamara A, Miskowski, Michael J, Kukla, Hans L, De Winter, Maria V F, Somers, Peter W M, Roevens, Robert W, Kavash   +6 more
openaire   +2 more sources

Design, Synthesis, and Tripeptidyl Peptidase II Inhibitory Activity of a Novel Series of (S)-2,3-Dihydro-2-(4-alkyl-1H-imidazol-2-yl)-1H-indoles

Journal of Medicinal Chemistry, 2002
Butabindide, 1, was previously reported as a potent inhibitor (IC50 = 7 nM) of the serine protease enzyme tripeptidyl peptidase II (TPPII), an endogenous protease that degrades cholecystokinin-8 (CCK-8). We found that 1 has some inherent chemical instability, yielding diketopiperazine 2 fairly readily under mimicked physiological conditions.
Henry J, Breslin, Tamara A, Miskowski, Michael J, Kukla, William H, Leister, Hans L, De Winter, Diane A, Gauthier, Maria V F, Somers, Daniëlle C G, Peeters, Peter W M, Roevens   +8 more
openaire   +2 more sources

Comparison of tripeptidyl peptidase 1 (CLN2) measurement by fluorometry and tandem mass spectrometry

Molecular Genetics and Metabolism, 2020
Zoltan Lukacs, Paulina Nieves Cobos, Petra Oliva, Rene Santer, David Kasper   +4 more
openaire   +1 more source

The gene encoding tripeptidyl peptidase II maps to Chromosome 1 in the mouse

Mammalian Genome, 1996
N A, Bermingham, T, McKay, J, Hoyle, D, Hernandez, J E, Martin, E M, Fisher   +5 more
openaire   +2 more sources