The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases. (Q40568559)

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6 November 2019

title

The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases (English)

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6 November 2019

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6 November 2019

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6 November 2019

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6 November 2019

J S Malik Peiris

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6 November 2019

Leo L M Poon

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6 November 2019

Rory M Watt

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6 November 2019

Lin-Yu Lu

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6 November 2019

Marie C Lin

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6 November 2019

Hsiang-Fu Kung

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6 November 2019

language of work or name

English

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publication date

13 August 2003

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Journal of Biological Chemistry

6 November 2019

published in

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6 November 2019

volume

278

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6 November 2019

issue

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6 November 2019

page(s)

39578-39582

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Coronavirus as a possible cause of severe acute respiratory syndrome

6 November 2019

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The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis.

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Herpes simplex virus helicase-primase inhibitors are active in animal models of human disease

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Nucleotide triphosphatase/helicase of hepatitis C virus as a target for antiviral therapy

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Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein

21 January 2018

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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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Helicase structure and mechanism

21 January 2018

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Structure of the hepatitis C virus RNA helicase domain

21 January 2018

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Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases

21 January 2018

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Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus

21 January 2018

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RNA helicase activity of the plant virus movement proteins encoded by the first gene of the triple gene block

21 January 2018

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Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

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The helicase-like domain of plant potexvirus replicase participates in formation of RNA 5' cap structure by exhibiting RNA 5'-triphosphatase activity

21 January 2018

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Purification and Characterization of West Nile Virus Nucleoside Triphosphatase (NTPase)/Helicase: Evidence for Dissociation of the NTPase and Helicase Activities of the Enzyme

21 January 2018

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21 January 2018

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Mechanisms and enzymes involved in SARS coronavirus genome expression

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.C300328200

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6 November 2019

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