ADP-ribose-1"-phosphatase activities of the human coronavirus 229E and SARS coronavirus X domains (Q79231395)

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20 December 2019

title

ADP-ribose-1"-phosphatase activities of the human coronavirus 229E and SARS coronavirus X domains (English)

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20 December 2019

1 reference

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human coronavirus

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inferred from title

Human coronavirus 229E

object named as

human coronavirus 229E

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3

Witold Filipowicz

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20 December 2019

author name string

Akos Putics

1

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20 December 2019

Jutta Slaby

2

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20 December 2019

Alexander E Gorbalenya

4

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20 December 2019

John Ziebuhr

5

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20 December 2019

publication date

1 January 2006

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Advances in Experimental Medicine and Biology

20 December 2019

published in

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20 December 2019

volume

581

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20 December 2019

page(s)

93-96

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A biochemical genomics approach for identifying genes by the activity of their products.

20 December 2019

cites work

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12 December 2020

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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12 December 2020

A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae

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12 December 2020

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12 December 2020

The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A

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12 December 2020

Mechanisms and enzymes involved in SARS coronavirus genome expression

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12 December 2020

Cloning and characterization of the Arabidopsis cyclic phosphodiesterase which hydrolyzes ADP-ribose 1'',2''-cyclic phosphate and nucleoside 2',3'-cyclic phosphates

1 reference

12 December 2020

Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses

1 reference

12 December 2020

Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular processing enzyme

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12 December 2020

The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond.

1 reference

12 December 2020