arginine has been researched along with Neuronal Ceroid-Lipofuscinoses in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 7 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Chan, CH; Pearce, DA; Ramirez-Montealegre, D | 1 |
Chattopadhyay, S; Pearce, DA | 1 |
Kim, Y; Pearce, DA; Ramirez-Montealegre, D | 1 |
Pearce, DA; Ramirez-Montealegre, D | 1 |
Leman, AR; Mole, SE; Pearce, DA; Polochock, S; Rothberg, PG | 1 |
Pearce, DA; Vitiello, SP; Wolfe, DM | 1 |
Lin, L; Lobel, P | 1 |
7 other study(ies) available for arginine and Neuronal Ceroid-Lipofuscinoses
Article | Year |
---|---|
Altered arginine metabolism in the central nervous system (CNS) of the Cln3-/- mouse model of juvenile Batten disease.
Topics: Animals; Arginine; Brain; Cationic Amino Acid Transporter 1; Cells, Cultured; Citrulline; Disease Models, Animal; Female; Gene Expression; Liver; Male; Membrane Glycoproteins; Mice; Mice, Knockout; Molecular Chaperones; Neuronal Ceroid-Lipofuscinoses; Neurons; Nitric Oxide; Nitric Oxide Synthase; Protein Isoforms; RNA, Messenger; Urea | 2009 |
Interaction with Btn2p is required for localization of Rsglp: Btn2p-mediated changes in arginine uptake in Saccharomyces cerevisiae.
Topics: Arginine; Base Sequence; Biological Transport, Active; DNA, Fungal; Humans; Lysosomes; Membrane Glycoproteins; Models, Biological; Molecular Chaperones; Neuronal Ceroid-Lipofuscinoses; Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Vacuoles | 2002 |
A role in vacuolar arginine transport for yeast Btn1p and for human CLN3, the protein defective in Batten disease.
Topics: Arginine; Biological Transport; Cyclins; Gene Deletion; Humans; Kinetics; Membrane Glycoproteins; Molecular Chaperones; Molecular Sequence Data; Neuronal Ceroid-Lipofuscinoses; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Deletion; Vacuoles | 2003 |
Defective lysosomal arginine transport in juvenile Batten disease.
Topics: Adenosine Triphosphate; Adolescent; Adult; Antibodies, Blocking; Arginine; Biological Transport; Cations; Child; Female; Humans; Lymphocytes; Lysosomes; Male; Membrane Glycoproteins; Molecular Chaperones; Mutation; Neuronal Ceroid-Lipofuscinoses; Vacuolar Proton-Translocating ATPases | 2005 |
Homogeneous PCR nucleobase quenching assays to detect four mutations that cause neuronal ceroid lipofuscinosis: T75P and R151X in CLN1, and IVS5-1G>C and R208X in CLN2.
Topics: Aminopeptidases; Arginine; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; DNA Mutational Analysis; Endopeptidases; Family Health; Humans; Membrane Proteins; Mutation; Neuronal Ceroid-Lipofuscinoses; Polymerase Chain Reaction; Proline; Reproducibility of Results; Serine Proteases; Thiolester Hydrolases; Threonine; Tripeptidyl-Peptidase 1 | 2006 |
Absence of Btn1p in the yeast model for juvenile Batten disease may cause arginine to become toxic to yeast cells.
Topics: Amino Acid Transport Systems, Basic; Arginine; Basic-Leucine Zipper Transcription Factors; Biological Transport; Cell Line; Cell Membrane; Child; Cyclins; DNA-Binding Proteins; Gene Expression Regulation, Fungal; Genetic Complementation Test; Humans; Membrane Glycoproteins; Models, Biological; Molecular Chaperones; Mutation; Neuronal Ceroid-Lipofuscinoses; RNA, Messenger; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription Factors; Vacuoles | 2007 |
Production and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosis.
Topics: Aminopeptidases; Animals; Arginine; Biological Transport; Cell Line; CHO Cells; Codon, Terminator; Cricetinae; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; Endocytosis; Endopeptidases; Fibroblasts; Heterozygote; Humans; Infant; Kinetics; Molecular Sequence Data; Neuronal Ceroid-Lipofuscinoses; Peptide Hydrolases; Receptor, IGF Type 2; Recombinant Proteins; Serine Proteases; Transfection; Tripeptidyl-Peptidase 1 | 2001 |