scholarly journals Nucleocapsid protein-dependent assembly of the RNA packaging signal of Middle East respiratory syndrome coronavirus

2018 ◽  
Vol 25 (1) ◽  
Author(s):  
Wei-Chen Hsin ◽  
Chan-Hua Chang ◽  
Chi-You Chang ◽  
Wei-Hao Peng ◽  
Chung-Liang Chien ◽  
...  
Keyword(s):  
Middle East ◽  
Nucleocapsid Protein ◽  
Middle East Respiratory Syndrome ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Rna Packaging Signal

Stem-loop SL4 of the HIV-1 Ψ RNA packaging signal exhibits weak affinity for the nucleocapsid protein. structural studies and implications for genome recognition

2001 ◽  
Vol 314 (5) ◽  
pp. 961-970 ◽  
Author(s):  
Gaya K. Amarasinghe ◽  
Jing Zhou ◽  
Matthew Miskimon ◽  
Kalola J. Chancellor ◽  
Jasmine A. McDonald ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Structural Studies ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Genome Recognition ◽  
Rna Packaging Signal ◽  
Hiv 1

NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the Ψ-RNA packaging signal. implications for genome recognition 1 1Edited by P. Wright

2000 ◽  
Vol 301 (2) ◽  
pp. 491-511 ◽  
Author(s):  
Gaya K Amarasinghe ◽  
Roberto N De Guzman ◽  
Ryan B Turner ◽  
Kalola J Chancellor ◽  
Zeng Rong Wu ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Nmr Structure ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Genome Recognition ◽  
Rna Packaging Signal ◽  
Hiv 1

scholarly journals The 1H, 15N, and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the Middle East respiratory syndrome coronavirus

2021 ◽  
Author(s):  
Talita Stelling de Araujo ◽  
Glauce Moreno Barbosa ◽  
Karoline Sanches ◽  
Jéssica M. Azevedo ◽  
Katia Maria dos Santos Cabral ◽  
...  
Keyword(s):  
Middle East ◽  
Nucleocapsid Protein ◽  
Resonance Assignments ◽  
Middle East Respiratory Syndrome ◽  
Terminal Domain

scholarly journals Inhibition of Hepadnavirus Reverse Transcriptase-ε RNA Interaction by Porphyrin Compounds

2007 ◽  
Vol 82 (5) ◽  
pp. 2305-2312 ◽  
Author(s):  
Li Lin ◽  
Jianming Hu
Keyword(s):  
Reverse Transcriptase ◽  
Protoporphyrin Ix ◽  
Rna Packaging ◽  
Packaging Signal ◽  
B Virus ◽  
Protein Priming ◽  
Rna Interaction ◽  
Iron Protoporphyrin ◽  
Rna Packaging Signal ◽  
Viral Reverse Transcription

ABSTRACT The hepatitis B virus (HBV) reverse transcriptase (RT) plays a multitude of fundamental roles in the viral life cycle and is the key target in the development of anti-HBV chemotherapy. We report here that the endogenous small molecule iron protoporphyrin IX (hemin) and several related porphyrin compounds potently blocked a critical RT interaction with the viral RNA packaging signal/origin of replication, called ε. As RT-ε interaction is essential for the initiation of viral reverse transcription, which is primed by RT itself (protein priming), the porphyrin compounds dramatically suppressed the protein-priming reaction. Further studies demonstrated that these compounds could target the unique N-terminal domain of the RT protein, the so-called terminal protein. Hemin and related porphyrin compounds thus represent a novel class of agents that can block HBV RT functions through a mechanism and target that are completely distinct from those of existing anti-HBV drugs.

Comparative Structural Effects of HIV-1 Gag and Nucleocapsid Proteins in Binding to and Unwinding of the Viral RNA Packaging Signal

Biochemistry ◽  
2012 ◽  
Vol 51 (15) ◽  
pp. 3162-3169 ◽  
Author(s):  
Neil M. Bell ◽  
Julia C. Kenyon ◽  
Shankar Balasubramanian ◽  
Andrew M. L. Lever
Keyword(s):  
Viral Rna ◽  
Structural Effects ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Nucleocapsid Proteins ◽  
Rna Packaging Signal ◽  
Hiv 1
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