proline and Niemann-Pick Disease

proline has been researched along with Niemann-Pick Disease in 3 studies

Research

Studies (3)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (33.33)	18.2507
2000's	1 (33.33)	29.6817
2010's	1 (33.33)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Edmunds, T; Garman, SC; Metcalf, MC; Qiu, H; Wei, RR; Zhou, YF	1
Millat, G; Vanier, MT	1
Desnick, RJ; Levran, O; Schuchman, EH	1

Reviews

1 review(s) available for proline and Niemann-Pick Disease

Article	Year
Structure and function of the NPC2 protein. Biochimica et biophysica acta, 2004, Oct-11, Volume: 1685, Issue:1-3 Topics: Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins; Cholesterol; Consensus Sequence; Conserved Sequence; Cysteine; Glycoproteins; Glycosylation; Humans; Hydrogen-Ion Concentration; Models, Biological; Molecular Sequence Data; Mutation; Niemann-Pick Diseases; Proline; Protein Binding; Protein Sorting Signals; Sequence Homology, Amino Acid; Vesicular Transport Proteins	2004

Article

Year

Structure and function of the NPC2 protein.

Biochimica et biophysica acta, 2004, Oct-11, Volume: 1685, Issue:1-3

Topics: Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins; Cholesterol; Consensus Sequence; Conserved Sequence; Cysteine; Glycoproteins; Glycosylation; Humans; Hydrogen-Ion Concentration; Models, Biological; Molecular Sequence Data; Mutation; Niemann-Pick Diseases; Proline; Protein Binding; Protein Sorting Signals; Sequence Homology, Amino Acid; Vesicular Transport Proteins

2004

Other Studies

2 other study(ies) available for proline and Niemann-Pick Disease

Article	Year
Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease. Nature communications, 2016, 10-11, Volume: 7 Topics: Amino Acid Sequence; Binding Sites; Catalytic Domain; Crystallography, X-Ray; HEK293 Cells; Humans; Models, Molecular; Mutation; Niemann-Pick Diseases; Phosphorylcholine; Proline; Protein Domains; Saposins; Sphingomyelin Phosphodiesterase; Substrate Specificity; Zinc	2016
Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients. Blood, 1992, Oct-15, Volume: 80, Issue:8 Topics: Base Sequence; Cell Line; Codon; DNA; Gene Expression; Humans; Jews; Leucine; Molecular Sequence Data; Mutation; Niemann-Pick Diseases; Nucleic Acid Hybridization; Pedigree; Polymerase Chain Reaction; Proline; Sphingomyelin Phosphodiesterase; Transfection	1992

Article

Year

Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease.

Nature communications, 2016, 10-11, Volume: 7

Topics: Amino Acid Sequence; Binding Sites; Catalytic Domain; Crystallography, X-Ray; HEK293 Cells; Humans; Models, Molecular; Mutation; Niemann-Pick Diseases; Phosphorylcholine; Proline; Protein Domains; Saposins; Sphingomyelin Phosphodiesterase; Substrate Specificity; Zinc

2016

Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients.

Blood, 1992, Oct-15, Volume: 80, Issue:8

Topics: Base Sequence; Cell Line; Codon; DNA; Gene Expression; Humans; Jews; Leucine; Molecular Sequence Data; Mutation; Niemann-Pick Diseases; Nucleic Acid Hybridization; Pedigree; Polymerase Chain Reaction; Proline; Sphingomyelin Phosphodiesterase; Transfection

1992