Results 111 to 120 of about 2,889 (188)

Progressively reduced synaptic vesicle pool size in cultured neurons derived from neuronal ceroid lipofuscinosis-1 knockout mice

open access: yesNeurobiology of Disease, 2005
The neuronal ceroid lipofuscinoses are a newly-recognized group of lysosomal storage disorders in which neurodegeneration predominates. The pathophysiological basis for this is unknown.
Tuhin Virmani   +4 more
doaj   +1 more source

Mice with Ppt1Δex4 mutation replicate the INCL phenotype and show an inflammation-associated loss of interneurons

open access: yesNeurobiology of Disease, 2005
Infantile Neuronal Ceroid Lipofuscinosis (INCL) results from mutations in the palmitoyl protein thioesterase (PPT1, CLN1) gene and is characterized by dramatic death of cortical neurons.
Anu Jalanko   +10 more
doaj   +1 more source

Gene expression profiling in a mouse model of infantile neuronal ceroid lipofuscinosis reveals upregulation of immediate early genes and mediators of the inflammatory response

open access: yesBMC Neuroscience, 2007
Background The infantile form of neuronal ceroid lipofuscinosis (also known as infantile Batten disease) is caused by hereditary deficiency of a lysosomal enzyme, palmitoyl-protein thioesterase-1 (PPT1), and is characterized by severe cortical ...
Hofmann Sandra L   +2 more
doaj   +1 more source

Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) – distinct characteristics in neurons-7

open access: yes, 2011
Copyright information:Taken from "Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) – distinct characteristics in neurons"http://www.biomedcentral.com/1471-2121/8/22BMC Cell Biology 2007;8():22-22.Published online
Carina von Schantz (45483)   +7 more
core   +1 more source

The sfp-type 4'-phosphopantetheinyl transferase Ppt1 of Cochliobolus miyabeanus controls development and pathogenicity [PDF]

open access: yes, 2016
In filamentous fungi, the sfp-type 4’-phosphopantetheinyl transferase Ppt1 is required for activation of some of the enzymes for lysine biosynthesis, and peptide/polyketide secondary metabolites.
Mohd Zainudin, Nur Ain Izzati   +1 more
core   +1 more source

Table_1_The Interactome of Palmitoyl-Protein Thioesterase 1 (PPT1) Affects Neuronal Morphology and Function.docx

open access: yes, 2019
Palmitoyl-protein thioesterase 1 (PPT1) is a depalmitoylation enzyme that is mutated in cases of neuronal ceroid lipofuscinosis (NCL). The hallmarks of the disease include progressive neurodegeneration and blindness, as well as seizures.
Orly Reiner (20376)   +6 more
core   +1 more source

Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) – distinct characteristics in neurons-4

open access: yes, 2011
Copyright information:Taken from "Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) – distinct characteristics in neurons"http://www.biomedcentral.com/1471-2121/8/22BMC Cell Biology 2007;8():22-22.Published online
Carina von Schantz (45483)   +7 more
core   +1 more source

Publication Only

open access: yes
HemaSphere, Volume 10, Issue S1, June 2026.
wiley   +1 more source

Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) – distinct characteristics in neurons-10

open access: yes, 2011
Copyright information:Taken from "Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) – distinct characteristics in neurons"http://www.biomedcentral.com/1471-2121/8/22BMC Cell Biology 2007;8():22-22.Published online
Carina von Schantz (45483)   +7 more
core   +1 more source

Examining potential roles of protein phosphatase 5 by identification of protein binding partners and characterization of its yeast homologue, PPT1

open access: yes, 2002
Protein phosphatase 5 (PP5) contains a C-terminal catalytic domain that is structurally related to the catalytic subunits of members of PPP serine/threonine phosphatase family and a unique N-terminal domain consisting of three tetratricopeptide repeats ...
Jeong, Jee-Yeong
core   +1 more source

Home - About - Disclaimer - Privacy