Yong Lin
Kanazawa University
12 Papers
260 Citations
Yong Lin is an academic researcher from Kanazawa University. The author has contributed to research in topics: RNA polymerase II & HBx. The author has an hindex of 9, co-authored 12 publications.
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Papers
•Journal Article
The Transactivation and p53-interacting Functions of Hepatitis B Virus X Protein Are Mutually Interfering but Distinct
TL;DR: The results indicate that the HBx-binding sites are located within the oligomerization and specific DNA-binding domains of p53 and that the p53-binding site was confined to a small region in theHBx transactivation domain.
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Mutational analysis of the structure and functions of hepatitis C virus RNA-dependent RNA polymerase.
TL;DR: The hepatitis C virus (HCV) nonstructural protein 5B (NS5B) is an RNA-dependent RNA polymerase (RdRP), a central catalytic enzyme for HCV replication.
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The Hepatitis B Virus X Protein Is a Co-activator of Activated Transcription That Modulates the Transcription Machinery and Distal Binding Activators
Yong Lin,Hong Tang,Takahiro Nomura,Dorjbal Dorjsuren,Naoyuki Hayashi,Wenxiang Wei,Tsutomu Ohta,Robert G. Roeder,Seishi Murakami +8 more
TL;DR: It is implied that HBx acts as a co-activator that modulates transcriptional machinery and distal-binding activators, which may explain one of the mechanisms of transactivation by HBx when localized in nuclei.
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Direct Interaction between the Subunit RAP30 of Transcription Factor IIF (TFIIF) and RNA Polymerase Subunit 5, Which Contributes to the Association between TFIIF and RNA Polymerase II
Wenxiang Wei,Dorjbal Dorjsuren,Yong Lin,Weiping Qin,Takahiro Nomura,Naoyuki Hayashi,Seishi Murakami +6 more
TL;DR: Interestingly, coexpression of the central region of RPB5 and wild type RAP30 inhibited recovery of endogenous pol II to the FLAG-RAP74-bound M2 resin, strongly suggesting that the RAP 30-binding region ofRPB5 inhibited the association of TFIIF and pol II.
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Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)
Wenxiang Wei,Wenxiang Wei,Jun Xia Gu,Cui Qing Zhu,Feng Yan Sun,Dorjbal Dorjsuren,Yong Lin,Seishi Murakami +7 more
TL;DR: The result of luciferase assay showed that overexpression of RMP, but not the mutant RMP lacking D5 region, suppressed the transcription activated by Gal-VP16, suggesting that interaction with TFIIF is required for RMP to suppress the activated transcription.