Yong Lin

发表

Expression of the circular RNAs in astaxanthin promotes cholesterol efflux from THP-1 cells based on RNA-seq

Peiwen Zhang, T. Zou, Zhexiao Zhang, 2021, Genes & nutrition.

Probing the RNA binding surface of the HIV-1 nucleocapsid protein by site-directed mutagenesis.

P. Borer, W. Ouyang, Yong Lin, 2013, Biochemistry.

Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)

S. Murakami, D. Dorjsuren, Wenxiang Wei, 2003, Cell Research.

Hepatitis B Virus X Protein Is a Transcriptional Modulator That Communicates with Transcription Factor IIB and the RNA Polymerase II Subunit 5*

J. Cheong, S. Murakami, T. Nomura, 1997, The Journal of Biological Chemistry.

RMP, a Novel RNA Polymerase II Subunit 5-Interacting Protein, Counteracts Transactivation by Hepatitis B Virus X Protein

T. Yamashita, S. Murakami, T. Nomura, 1998, Molecular and Cellular Biology.

Proteinby Hepatitis B Virus X 5-Interacting Protein, Counteracts RMP, a Novel RNA Polymerase II Subunit

S. Murakami, T. Nomura, Wenxiang Wei, 2013 .

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*

W. Qin, S. Murakami, T. Nomura, 2001, The Journal of Biological Chemistry.

Human hepatitis B virus X protein augments the DNA binding of nuclear factor for IL‐6 through its basic‐leucine zipper domain

Kenichi Kobayashi, S. Murakami, S. Kaneko, 1999, Journal of medical virology.

The Hepatitis B Virus X Protein Is a Co-activator of Activated Transcription That Modulates the Transcription Machinery and Distal Binding Activators*

R. Roeder, S. Murakami, T. Ohta, 1998, The Journal of Biological Chemistry.

Disruption of Hsp90 Function Results in Degradation of the Death Domain Kinase, Receptor-interacting Protein (RIP), and Blockage of Tumor Necrosis Factor-induced Nuclear Factor-κB Activation*

L. Neckers, A. Devin, Abigail L Miller, 2000, The Journal of Biological Chemistry.

The Death Domain Kinase RIP Is Essential for TRAIL (Apo2L)-Induced Activation of IκB Kinase and c-Jun N-Terminal Kinase

M. Kelliher, S. Lipkowitz, M. Keane, 2000, Molecular and Cellular Biology.

Mutational analysis of the structure and functions of hepatitis C virus RNA–dependent RNA polymerase

Y. Shirota, W. Qin, T. Yamashita, 2001, Hepatology.

The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation.

M. Kelliher, Y. Lin, Z. Liu, 2000, Immunity.

Human hepatitis B virus X protein is detectable in nuclei of transfected cells, and is active for transactivation.

T. Yamashita, S. Murakami, T. Nomura, 1999, Biochimica et biophysica acta.

Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis.

Y. Lin, Z. Liu, A. Devin, 1999, Genes & development.

Proton NMR and structural features of a 24-nucleotide RNA hairpin.

Philip N. Borer, O. Uhlenbeck, P. Borer, 1995, Biochemistry.

Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation.

J. Cheong, S. Murakami, M. Yi, 1995, The EMBO journal.