Jung N

References (4)

Title : Comprehensive subspecies identification of 175 nontuberculous mycobacteria species based on 7547 genomic profiles - Matsumoto_2019_Emerg.Microbes.Infect_8_1043
Author(s) : Matsumoto Y , Kinjo T , Motooka D , Nabeya D , Jung N , Uechi K , Horii T , Iida T , Fujita J , Nakamura S
Ref : Emerg Microbes Infect , 8 :1043 , 2019
Abstract : The prevalence of nontuberculous mycobacteria (NTM) pulmonary diseases has been increasing worldwide. NTM consist of approximately 200 species and distinguishing between them at the subspecies level is critical to treatment. In this study, we sequenced 63 NTM genomes, 27 of which were newly determined, by hybrid assembly using sequencers from Illumina and Oxford Nanopore Technologies (ONT). This analysis expanded the available genomic data to 175 NTM species and redefined their subgenus classification. We also developed a novel multi-locus sequence typing (MLST) database based on 184 genes from 7547 assemblies and an identification software, mlstverse, which can also be used for detecting other bacteria given a suitable MLST database. This method showed the highest sensitivity and specificity amongst conventional methods and demonstrated the capacity for rapid detection of NTM, 10 min of sequencing of the ONT MinION being sufficient. Application of this methodology could improve disease epidemiology and increase the cure rates of NTM diseases.
ESTHER : Matsumoto_2019_Emerg.Microbes.Infect_8_1043
PubMedSearch : Matsumoto_2019_Emerg.Microbes.Infect_8_1043
PubMedID: 31287781
Gene_locus related to this paper: 9myco-a0a6n4vdv4

Title : A magnetic nanoprobe technology for detecting molecular interactions in live cells - Won_2005_Science_309_121
Author(s) : Won J , Kim M , Yi YW , Kim YH , Jung N , Kim TK
Ref : Science , 309 :121 , 2005
Abstract : Technologies to assess the molecular targets of biomolecules in living cells are lacking. We have developed a technology called magnetism-based interaction capture (MAGIC) that identifies molecular targets on the basis of induced movement of superparamagnetic nanoparticles inside living cells. Efficient intracellular uptake of superparamagnetic nanoparticles (coated with a small molecule of interest) was mediated by a transducible fusogenic peptide. These nanoprobes captured the small molecule's labeled target protein and were translocated in a direction specified by the magnetic field. Use of MAGIC in genome-wide expression screening identified multiple protein targets of a drug. MAGIC was also used to monitor signal-dependent modification and multiple interactions of proteins.
ESTHER : Won_2005_Science_309_121
PubMedSearch : Won_2005_Science_309_121
PubMedID: 15994554

Title : Characterization of lysosomal acid lipase mutations in the signal peptide and mature polypeptide region causing Wolman disease - Zschenker_2001_J.Lipid.Res_42_1033
Author(s) : Zschenker O , Jung N , Rethmeier J , Trautwein S , Hertel S , Zeigler M , Ameis D
Ref : J Lipid Res , 42 :1033 , 2001
Abstract : Wolman disease results from an inherited deficiency of lysosomal acid lipase (LAL; EC This enzyme is essential for the hydrolysis of cholesteryl esters and triacylglycerols derived from endocytosed lipoproteins. Because of a complete absence of LAL activity, Wolman patients accumulate progressive amounts of cholesteryl esters and triacylglycerols in affected tissues. To investigate the nature of the genetic defects causing this disease, mutations in the LAL gene from three subjects of Moslem-Arab and Russian descent living in Israel were determined. Two homozygotes for a novel 1-bp deletion introducing a premature in-frame termination codon at amino acid position 106 (S106X) were identified. A third subject was a homozygote for a G-5R signal peptide substitution and a G60V missense mutation. The functional significance of these mutations was tested by in vitro expression of single and double mutants in Spodoptera frugiperda cells. Single mutants G60V and S106X and double mutant G-5R/G60V displayed a virtual absence of lipase activity in cell extracts and culture medium. Signal peptide mutant G-5R retained lipase activity in cell extracts and showed a drastically reduced enzyme activity in culture supernatant, indicating that the mutation may affect secretion of active enzyme from cells. These results support the notion that Wolman disease is a genetically heterogeneous disorder of lipid metabolism.
ESTHER : Zschenker_2001_J.Lipid.Res_42_1033
PubMedSearch : Zschenker_2001_J.Lipid.Res_42_1033
PubMedID: 11441129
Gene_locus related to this paper: human-LIPA

Title : Different missense mutations in histidine-108 of lysosomal acid lipase cause cholesteryl ester storage disease in unrelated compound heterozygous and hemizygous individuals - Ries_1998_Hum.Mutat_12_44
Author(s) : Ries S , Buchler C , Schindler G , Aslanidis C , Ameis D , Gasche C , Jung N , Schambach A , Fehringer P , Vanier MT , Belli DC , Greten H , Schmitz G
Ref : Hum Mutat , 12 :44 , 1998
Abstract : Cholesteryl ester storage disease (CESD) and Wolman disease (WD) are both autosomal recessive disorders associated with reduced activity of lysosomal acid lipase (LAL), that leads to the tissue accumulation of cholesteryl esters in endosomes and lysosomes. WD is caused by genetic defects of LAL that leave no residual enzymatic activity, while in CESD patients a residual LAL activity can be identified. We have analyzed the LAL cDNA in three CESD patients from two nonrelated families and identified the mutations responsible for the disease. The associated genetic defects characterized revealed compound heterozygosity for a splice defect leading to skipping of exon 8, due to a G-->A transition at position -1 of the exon 8 splice donor site, and a point mutation leading to a Hisl08Pro change (CAT-->CCT) in two patients (siblings) with mild CESD phenotype. A further CESD patient was hemizygous for a His108-->Arg missense mutation (CAT-->CGT) in combination with a partial deletion of the LAL gene and was affected more severely. Expression of the LAL enzymes with the His108-->Pro and His108-->Arg mutation in insect cells revealed residual enzymatic activities of 4.6% versus 2.7%, respectively, compared with controls. Therefore, His108 seems to play a crucial role in folding or catalytic activity of the lysosomal acid lipase. This is the first description of two different, naturally occurring mutations involving the same amino acid residue in the lysosomal acid lipase in unrelated CESD patients. Moreover, our results demonstrate that the variable manifestation of CESD can be explained by mutation-dependent, variable inactivation of the LAL enzyme.
ESTHER : Ries_1998_Hum.Mutat_12_44
PubMedSearch : Ries_1998_Hum.Mutat_12_44
PubMedID: 9633819
Gene_locus related to this paper: human-LIPA