LIVIVO - Search results -

Search results

Result 1 - 10 of total 82

Search options

Article ; Online: Correction: CBAP regulates the function of Akt-associated TSC protein complexes to modulate mTORC1 signaling.

Liao, Wei-Ting / Chiang, Yun-Jung / Yang-Yen, Hsin-Fang / Hsu, Li-Chung / Chang, Zee-Fen / Yen, Jeffrey J Y

2024 Volume 300, Issue 2, Page(s) 105686

Language	English
Publishing date	2024-01-29
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2024.105686
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Correction for Kuo and Chang, GATA-1 and Gfi-1B Interplay To Regulate

Kuo, Yuan-Yeh / Chang, Zee-Fen

Molecular and cellular biology

2017 Volume 37, Issue 6

Language	English
Publishing date	2017-03-01
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00008-17
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1666: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A Convenient and Sensitive Method for Deoxynucleoside Triphosphate Quantification by the Combination of Rolling Circle Amplification and Quantitative Polymerase Chain Reaction.

Wang, Hsin-Yen / Hsin, Peng / Huang, Chang-Yu / Chang, Zee-Fen

Analytical chemistry

2021 Volume 93, Issue 42, Page(s) 14247–14255

Abstract: Measurement of four dNTP pools is important for investigating metabolism, genome stability, and drug action. In this report, we developed a two-step method for quantitating dNTPs by the combination of rolling circle amplification (RCA) and quantitative ... ...

Abstract	Measurement of four dNTP pools is important for investigating metabolism, genome stability, and drug action. In this report, we developed a two-step method for quantitating dNTPs by the combination of rolling circle amplification (RCA) and quantitative polymerase chain reaction (qPCR). We used CircLigase to generate a single-strand DNA in circular monomeric configuration, which was then used for the first step of RCA reaction that contained three dNTPs in excess for quantification of one dNTP at limiting levels. The second step is the amplification of RCA products by qPCR, in which one primer was designed to be completely annealed with the polymeric ssDNA product but not the monomeric template DNA. Using 1 amol of the template in the assay, each dNTP from 0.02 to 2.5 pmol gave a linearity with
MeSH term(s)	Biological Assay ; DNA/genetics ; Nucleic Acid Amplification Techniques ; Polymerase Chain Reaction ; Polyphosphates
Chemical Substances	Polyphosphates ; DNA (9007-49-2) ; triphosphoric acid (NU43IAG5BC)
Language	English
Publishing date	2021-10-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.1c03236
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4033: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: NME3 Regulates Mitochondria to Reduce ROS-Mediated Genome Instability

Chih-Wei Chen / Ning Tsao / Wei Zhang / Zee-Fen Chang

International Journal of Molecular Sciences, Vol 21, Iss 5048, p

2020 Volume 5048

Abstract: NME3 is a member of the nucleoside diphosphate kinase (NDPK) family that binds to the mitochondrial outer membrane to stimulate mitochondrial fusion. In this study, we showed that NME3 knockdown delayed DNA repair without reducing the cellular levels of ... ...

Abstract	NME3 is a member of the nucleoside diphosphate kinase (NDPK) family that binds to the mitochondrial outer membrane to stimulate mitochondrial fusion. In this study, we showed that NME3 knockdown delayed DNA repair without reducing the cellular levels of nucleotide triphosphates. Further analyses revealed that NME3 knockdown increased fragmentation of mitochondria, which in turn led to mitochondrial oxidative stress-mediated DNA single-strand breaks (SSBs) in nuclear DNA. Re-expression of wild-type NME3 or inhibition of mitochondrial fission markedly reduced SSBs and facilitated DNA repair in NME3 knockdown cells, while expression of N-terminal deleted mutant defective in mitochondrial binding had no rescue effect. We further showed that disruption of mitochondrial fusion by knockdown of NME4 or MFN1 also caused mitochondrial oxidative stress-mediated genome instability. In conclusion, the contribution of NME3 to redox-regulated genome stability lies in its function in mitochondrial fusion.
Keywords	NME3 ; DNA damage ; mitochondrial morphology ; oxidative stress ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Language	English
Publishing date	2020-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: CBAP regulates the function of Akt-associated TSC protein complexes to modulate mTORC1 signaling.

Liao, Wei-Ting / Chiang, Yun-Jung / Yang-Yen, Hsin-Fang / Hsu, Li-Chung / Chang, Zee-Fen / Yen, Jeffrey J Y

The Journal of biological chemistry

2023 Volume 299, Issue 12, Page(s) 105455

Abstract: The Akt-Rheb-mTORC1 pathway plays a crucial role in regulating cell growth, but the mechanisms underlying the activation of Rheb-mTORC1 by Akt remain unclear. In our previous study, we found that CBAP was highly expressed in human T-ALL cells and primary ...

Abstract	The Akt-Rheb-mTORC1 pathway plays a crucial role in regulating cell growth, but the mechanisms underlying the activation of Rheb-mTORC1 by Akt remain unclear. In our previous study, we found that CBAP was highly expressed in human T-ALL cells and primary tumors, and its deficiency led to reduced phosphorylation of TSC2/S6K1 signaling proteins as well as impaired cell proliferation and leukemogenicity. We also demonstrated that CBAP was required for Akt-mediated TSC2 phosphorylation in vitro. In response to insulin, CBAP was also necessary for the phosphorylation of TSC2/S6K1 and the dissociation of TSC2 from the lysosomal membrane. Here we report that CBAP interacts with AKT and TSC2, and knockout of CBAP or serum starvation leads to an increase in TSC1 in the Akt/TSC2 immunoprecipitation complexes. Lysosomal-anchored CBAP was found to override serum starvation and promote S6K1 and 4EBP1 phosphorylation and c-Myc expression in a TSC2-dependent manner. Additionally, recombinant CBAP inhibited the GAP activity of TSC2 complexes in vitro, leading to increased Rheb-GTP loading, likely due to the competition between TSC1 and CBAP for binding to the HBD domain of TSC2. Overexpression of the N26 region of CBAP, which is crucial for binding to TSC2, resulted in a decrease in mTORC1 signaling and an increase in TSC1 association with the TSC2/AKT complex, ultimately leading to increased GAP activity toward Rheb and impaired cell proliferation. Thus, we propose that CBAP can modulate the stability of TSC1-TSC2 as well as promote the translocation of TSC1/TSC2 complexes away from lysosomes to regulate Rheb-mTORC1 signaling.
MeSH term(s)	Humans ; Cell Proliferation ; Guanosine Triphosphate/metabolism ; Immunoprecipitation ; Lysosomes/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Membrane Proteins/deficiency ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-akt/metabolism ; Ras Homolog Enriched in Brain Protein/metabolism ; TOR Serine-Threonine Kinases/metabolism ; Tuberous Sclerosis Complex 1 Protein/metabolism ; Tuberous Sclerosis Complex 2 Protein/metabolism
Chemical Substances	Guanosine Triphosphate (86-01-1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Membrane Proteins ; MYC protein, human ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Ras Homolog Enriched in Brain Protein ; RHEB protein, human ; ribosomal protein S6 kinase, 70kD, polypeptide 1 (EC 2.7.11.1) ; TMEM102 protein, human ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; TSC1 protein, human ; TSC2 protein, human ; Tuberous Sclerosis Complex 1 Protein ; Tuberous Sclerosis Complex 2 Protein
Language	English
Publishing date	2023-11-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105455
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: NME3 Regulates Mitochondria to Reduce ROS-Mediated Genome Instability.

Chen, Chih-Wei / Tsao, Ning / Zhang, Wei / Chang, Zee-Fen

International journal of molecular sciences

2020 Volume 21, Issue 14

Abstract	NME3 is a member of the nucleoside diphosphate kinase (NDPK) family that binds to the mitochondrial outer membrane to stimulate mitochondrial fusion. In this study, we showed that NME3 knockdown delayed DNA repair without reducing the cellular levels of nucleotide triphosphates. Further analyses revealed that NME3 knockdown increased fragmentation of mitochondria, which in turn led to mitochondrial oxidative stress-mediated DNA single-strand breaks (SSBs) in nuclear DNA. Re-expression of wild-type NME3 or inhibition of mitochondrial fission markedly reduced SSBs and facilitated DNA repair in NME3 knockdown cells, while expression of N-terminal deleted mutant defective in mitochondrial binding had no rescue effect. We further showed that disruption of mitochondrial fusion by knockdown of NME4 or MFN1 also caused mitochondrial oxidative stress-mediated genome instability. In conclusion, the contribution of NME3 to redox-regulated genome stability lies in its function in mitochondrial fusion.
MeSH term(s)	DNA Damage ; Gene Knockdown Techniques ; Genomic Instability ; HEK293 Cells ; HeLa Cells ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; NM23 Nucleoside Diphosphate Kinases/genetics ; NM23 Nucleoside Diphosphate Kinases/metabolism ; Oxidative Stress ; Reactive Oxygen Species/metabolism
Chemical Substances	NM23 Nucleoside Diphosphate Kinases ; Reactive Oxygen Species ; NME3 protein, human (EC 2.7.4.6)
Language	English
Publishing date	2020-07-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21145048
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: A Convenient and Sensitive Method for Deoxynucleoside Triphosphate Quantification by the Combination of Rolling Circle Amplification and Quantitative Polymerase Chain Reaction

Wang, Hsin-Yen / Hsin, Peng / Huang, Chang-Yu / Chang, Zee-Fen

Analytical chemistry. 2021 Oct. 11, v. 93, no. 42

2021

Abstract	Measurement of four dNTP pools is important for investigating metabolism, genome stability, and drug action. In this report, we developed a two-step method for quantitating dNTPs by the combination of rolling circle amplification (RCA) and quantitative polymerase chain reaction (qPCR). We used CircLigase to generate a single-strand DNA in circular monomeric configuration, which was then used for the first step of RCA reaction that contained three dNTPs in excess for quantification of one dNTP at limiting levels. The second step is the amplification of RCA products by qPCR, in which one primer was designed to be completely annealed with the polymeric ssDNA product but not the monomeric template DNA. Using 1 amol of the template in the assay, each dNTP from 0.02 to 2.5 pmol gave a linearity with r² > 0.99, and the quantification was not affected by the presence of rNTPs. We further found that the preparation of biological samples for the RCA reaction required methanol and chloroform extraction. The method was so sensitive that 1 × 10⁴ cells were sufficient for dNTP quantification with the results similar to those determined by a radio-isotope method using 2 × 10⁵ cells. Thus, the RCA/qPCR method is convenient, cost-effective, and highly sensitive for dNTP quantification.
Keywords	analytical chemistry ; chloroform ; cost effectiveness ; genome ; metabolism ; methanol ; polymers ; quantitative polymerase chain reaction ; radionuclides
Language	English
Dates of publication	2021-1011
Size	p. 14247-14255.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.1c03236
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 52/94: Show issues
Z 2.9: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: NME3 is a gatekeeper for DRP1-dependent mitophagy in hypoxia.

Chen, Chih-Wei / Su, Chi / Huang, Chang-Yu / Huang, Xuan-Rong / Cuili, Xiaojing / Chao, Tung / Fan, Chun-Hsiang / Ting, Cheng-Wei / Tsai, Yi-Wei / Yang, Kai-Chien / Yeh, Ti-Yen / Hsieh, Sung-Tsang / Chen, Yi-Ju / Feng, Yuxi / Hunter, Tony / Chang, Zee-Fen

Nature communications

2024 Volume 15, Issue 1, Page(s) 2264

Abstract: NME3 is a member of the nucleoside diphosphate kinase (NDPK) family localized on the mitochondrial outer membrane (MOM). Here, we report a role of NME3 in hypoxia-induced mitophagy dependent on its active site phosphohistidine but not the NDPK function. ... ...

Abstract	NME3 is a member of the nucleoside diphosphate kinase (NDPK) family localized on the mitochondrial outer membrane (MOM). Here, we report a role of NME3 in hypoxia-induced mitophagy dependent on its active site phosphohistidine but not the NDPK function. Mice carrying a knock-in mutation in the Nme3 gene disrupting NME3 active site histidine phosphorylation are vulnerable to ischemia/reperfusion-induced infarction and develop abnormalities in cerebellar function. Our mechanistic analysis reveals that hypoxia-induced phosphatidic acid (PA) on mitochondria is essential for mitophagy and the interaction of DRP1 with NME3. The PA binding function of MOM-localized NME3 is required for hypoxia-induced mitophagy. Further investigation demonstrates that the interaction with active NME3 prevents DRP1 susceptibility to MUL1-mediated ubiquitination, thereby allowing a sufficient amount of active DRP1 to mediate mitophagy. Furthermore, MUL1 overexpression suppresses hypoxia-induced mitophagy, which is reversed by co-expression of ubiquitin-resistant DRP1 mutant or histidine phosphorylatable NME3. Thus, the site-specific interaction with active NME3 provides DRP1 a microenvironment for stabilization to proceed the segregation process in mitophagy.
MeSH term(s)	Animals ; Mice ; Dynamins/genetics ; Dynamins/metabolism ; Histidine/metabolism ; Hypoxia ; Mitophagy/genetics ; Ubiquitination
Chemical Substances	Dynamins (EC 3.6.5.5) ; Histidine (4QD397987E) ; Nme3 protein, mouse (EC 2.7.4.6) ; Dnm1l protein, mouse (EC 3.6.5.5)
Language	English
Publishing date	2024-03-13
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-46385-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: DNMT3b protects centromere integrity by restricting R-loop-mediated DNA damage.

Shih, Hsueh-Tzu / Chen, Wei-Yi / Wang, Hsin-Yen / Chao, Tung / Huang, Hsien-Da / Chou, Chih-Hung / Chang, Zee-Fen

Cell death & disease

2022 Volume 13, Issue 6, Page(s) 546

Abstract: This study used DNA methyltransferase 3b (DNMT3b) knockout cells and the functional loss of DNMT3b mutation in immunodeficiency-centromeric instability-facial anomalies syndrome (ICF) cells to understand how DNMT3b dysfunction causes genome instability. ... ...

Abstract	This study used DNA methyltransferase 3b (DNMT3b) knockout cells and the functional loss of DNMT3b mutation in immunodeficiency-centromeric instability-facial anomalies syndrome (ICF) cells to understand how DNMT3b dysfunction causes genome instability. We demonstrated that R-loops contribute to DNA damages in DNMT3b knockout and ICF cells. More prominent DNA damage signal in DNMT3b knockout cells was due to the loss of DNMT3b expression and the acquirement of p53 mutation. Genome-wide ChIP-sequencing mapped DNA damage sites at satellite repetitive DNA sequences including (peri-)centromere regions. However, the steady-state levels of (peri-)centromeric R-loops were reduced in DNMT3b knockout and ICF cells. Our analysis indicates that XPG and XPF endonucleases-mediated cleavages remove (peri-)centromeric R-loops to generate DNA beaks, causing chromosome instability. DNMT3b dysfunctions clearly increase R-loops susceptibility to the cleavage process. Finally, we showed that DNA double-strand breaks (DSBs) in centromere are probably repaired by error-prone end-joining pathway in ICF cells. Thus, DNMT3 dysfunctions undermine the integrity of centromere by R-loop-mediated DNA damages and repair.
MeSH term(s)	Animals ; Centromere/genetics ; Centromere/metabolism ; DNA/metabolism ; DNA (Cytosine-5-)-Methyltransferases/genetics ; DNA (Cytosine-5-)-Methyltransferases/metabolism ; DNA Damage/genetics ; DNA Methylation ; Immunologic Deficiency Syndromes/genetics ; Immunologic Deficiency Syndromes/metabolism ; Mutation ; R-Loop Structures ; DNA Methyltransferase 3B
Chemical Substances	DNA (9007-49-2) ; DNA (Cytosine-5-)-Methyltransferases (EC 2.1.1.37)
Language	English
Publishing date	2022-06-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-022-04989-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Quantitation of deoxynucleoside triphosphates by click reactions

Chang-Yu Huang / Miriam Yagüe-Capilla / Dolores González-Pacanowska / Zee-Fen Chang

Scientific Reports, Vol 10, Iss 1, Pp 1-

2020 Volume 10

Abstract: Abstract The levels of the four deoxynucleoside triphosphates (dNTPs) are under strict control in the cell, as improper or imbalanced dNTP pools may lead to growth defects and oncogenesis. Upon treatment of cancer cells with therapeutic agents, changes ... ...

Abstract	Abstract The levels of the four deoxynucleoside triphosphates (dNTPs) are under strict control in the cell, as improper or imbalanced dNTP pools may lead to growth defects and oncogenesis. Upon treatment of cancer cells with therapeutic agents, changes in the canonical dNTPs levels may provide critical information for evaluating drug response and mode of action. The radioisotope-labeling enzymatic assay has been commonly used for quantitation of cellular dNTP levels. However, the disadvantage of this method is the handling of biohazard materials. Here, we described the use of click chemistry to replace radioisotope-labeling in template-dependent DNA polymerization for quantitation of the four canonical dNTPs. Specific oligomers were designed for dCTP, dTTP, dATP and dGTP measurement, and the incorporation of 5-ethynyl-dUTP or C8-alkyne-dCTP during the polymerization reaction allowed for fluorophore conjugation on immobilized oligonucleotides. The four reactions gave a linear correlation coefficient >0.99 in the range of the concentration of dNTPs present in 106 cells, with little interference of cellular rNTPs. We present evidence indicating that data generated by this methodology is comparable to radioisotope-labeling data. Furthermore, the design and utilization of a robust microplate assay based on this technology evidenced the modulation of dNTPs in response to different chemotherapeutic agents in cancer cells.
Keywords	Medicine ; R ; Science ; Q
Subject code	500
Language	English
Publishing date	2020-01-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED