Related ArticlesAn NMR-based approach reveals the core structure of the functional domain of SINEUP lncRNAs.
Nucleic Acids Res. 2020 09 18;48(16):9346-9360
Authors: Ohyama T, Takahashi H, Sharma H, Yamazaki T, Gustincich S, Ishii Y, Carninci P
Abstract
Long non-coding RNAs (lncRNAs) are attracting widespread attention for their emerging regulatory, transcriptional, epigenetic, structural and various other functions. Comprehensive transcriptome analysis has revealed that retrotransposon elements (REs) are transcribed and enriched in lncRNA sequences. However, the functions of lncRNAs and the molecular roles of the embedded REs are largely unknown. The secondary and tertiary structures of lncRNAs and their embedded REs are likely to have essential functional roles, but experimental determination and reliable computational prediction of large RNA structures have been extremely challenging. We report here the nuclear magnetic resonance (NMR)-based secondary structure determination of the 167-nt inverted short interspersed nuclear element (SINE) B2, which is embedded in antisense Uchl1 lncRNA and upregulates the translation of sense Uchl1 mRNAs. By using NMR 'fingerprints' as a sensitive probe in the domain survey, we successfully divided the full-length inverted SINE B2 into minimal units made of two discrete structured domains and one dynamic domain without altering their original structures after careful boundary adjustments. This approach allowed us to identify a structured domain in nucleotides 31-119 of the inverted SINE B2. This approach will be applicable to determining the structures of other regulatory lncRNAs.
[NMR paper] 1H-NMR-based metabolomics approach reveals metabolic mechanism of (-)-5-hydroxy-equol against hepatocellular carcinoma cells in vitro.
1H-NMR-based metabolomics approach reveals metabolic mechanism of (-)-5-hydroxy-equol against hepatocellular carcinoma cells in vitro.
1H-NMR-based metabolomics approach reveals metabolic mechanism of (-)-5-hydroxy-equol against hepatocellular carcinoma cells in vitro.
J Proteome Res. 2018 Mar 28;:
Authors: Gao L, Wang KX, Zhang NN, Li JQ, Qin XM, Wang XL
Abstract
1H-NMR-based metabolomics can rapidly detect metabolic shift under various stimulus, thus it facilitated the dissection of the therapeutic mechanisms of compounds....
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[NMR paper] Structure-based drug design: NMR-based approach for ligand-protein interactions.
Structure-based drug design: NMR-based approach for ligand-protein interactions.
Related Articles Structure-based drug design: NMR-based approach for ligand-protein interactions.
Drug Discov Today Technol. 2006;3(3):241-5
Authors: Zhang X, Tang H, Ye C, Liu M
Abstract
The realization of the powerfulness in analyzing ligand-protein interactions at the atomic resolution has made NMR techniques increasingly attractive in drug discovery and development. With some significant new method developments during the past few years,...
[NMR paper] NMR structure determination and structure-based functional characterization of conser
NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.
Related Articles NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.
J Struct Funct Genomics. 2000;1(1):15-25
Authors: Cort JR, Yee A, Edwards AM, Arrowsmith CH, Kennedy MA
The solution structure of MTH1175, a 124-residue protein from the archaeon Methanobacterium...
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11-18-2010 09:15 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
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[NMR paper] NMR structure and functional studies of the Mu repressor DNA-binding domain.
NMR structure and functional studies of the Mu repressor DNA-binding domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure and functional studies of the Mu repressor DNA-binding domain.
Biochemistry. 1999 Jun 29;38(26):8367-76
Authors: Ilangovan U, Wojciak JM, Connolly KM, Clubb RT
The repressor protein of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. It interacts with several repeated DNA...
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08-21-2010 04:03 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Content Type Journal Article
DOI 10.1007/s10858-010-9426-8
Authors
Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA
An NMR-based approach reveals the core structure of the functional domain of SINEUP lncRNAs.
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