The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. (Q37094749)

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scholarly article

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English	The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.	scholarly article

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scholarly article

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25 December 2019

The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world (English)

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Europe PubMed Central

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25 December 2019

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structural biology

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inferred from title

non-structural protein 9 [SARS-Cov]

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1 reference

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Valérie Campanacci

3

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25 December 2019

François Ferron

2

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25 December 2019

Corinne Rancurel

5

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25 December 2019

Helene Dutartre

6

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25 December 2019

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25 December 2019

Alexander E. Gorbalenya

8

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25 December 2019

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25 December 2019

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Sonia Longhi

4

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Christian Cambillau

9

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Christian Cambillau

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25 December 2019

Marie-Pierre Egloff

1

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Marie-Pierre Egloff

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25 December 2019

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8 March 2004

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25 December 2019

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5

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Proceedings of the National Academy of Sciences of the United States of America

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25 December 2019

101

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25 December 2019

11

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25 December 2019

3792-3796

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25 December 2019

Raster3D: photorealistic molecular graphics

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29 September 2017

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21 January 2018

Refinement of macromolecular structures by the maximum-likelihood method

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29 September 2017

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29 September 2017

Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage

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Mechanisms and enzymes involved in SARS coronavirus genome expression

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Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB

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29 September 2017

The Genome sequence of the SARS-associated coronavirus

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Characterization of a novel coronavirus associated with severe acute respiratory syndrome

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29 September 2017

Coronavirus as a possible cause of severe acute respiratory syndrome

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29 September 2017

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29 September 2017

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OB-fold domains: a snapshot of the evolution of sequence, structure and function

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Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA

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29 September 2017

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The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity

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Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly.

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The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding

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Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein

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10.1073/PNAS.0307877101

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Europe PubMed Central

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25 December 2019

2004PNAS..101.3792E

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25 December 2019

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25 December 2019

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