Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) (Q27656805)

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English	Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)	scientific article

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scholarly article

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Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) (English)

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porcine reproductive and respiratory syndrome

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porcine reproductive and respiratory syndrome virus

object named as

Porcine Reproductive and Respiratory Syndrome Virus

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based on heuristic

inferred from title

7

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Rolf Hilgenfeld

10

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9

object named as

Jinghua Yan

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2

object named as

Guangwen Lu

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author name string

Xinsheng Tian

1

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Feng Gao

3

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Hao Peng

4

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Youjun Feng

5

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Guangpeng Ma

6

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Kegong Tian

8

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George F Gao

11

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language of work or name

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publication date

2 October 2009

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Journal of Molecular Biology

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392

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4

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977-93

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The CCP4 suite: programs for protein crystallography

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Complete genome comparison of porcine reproductive and respiratory syndrome virus parental and attenuated strains

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Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole

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Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors

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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain

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General overview of PRRSV: a perspective from the United States

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Full-length sequence of a Canadian porcine reproductive and respiratory syndrome virus (PRRSV) isolate

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Variable oligomerization modes in coronavirus non-structural protein 9

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Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations

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Expression, purification, and in vitro activity of an arterivirus main proteinase

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Processing and evolution of the N-terminal region of the arterivirus replicase ORF1a protein: identification of two papainlike cysteine proteases

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Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and Is essential for virus replication.

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Emergence of fatal PRRSV variants: unparalleled outbreaks of atypical PRRS in China and molecular dissection of the unique hallmark

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The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition

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Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease.

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The "colorful" epidemiology of PRRS.

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ESPript: analysis of multiple sequence alignments in PostScript

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Generation of an infectious clone of VR-2332, a highly virulent North American-type isolate of porcine reproductive and respiratory syndrome virus

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The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases

1 reference

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Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease

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Prediction of proteinase cleavage sites in polyproteins of coronaviruses and its applications in analyzing SARS-CoV genomes.

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Maximum-likelihood density modification

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'Blue ear' disease of pigs.

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The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain

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Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzyme

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Hepatitis A virus 3C proteinase substrate specificity

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Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease.

1 reference

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Porcine reproductive and respiratory syndrome (PRRS or blue-eared pig disease)

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Subtilisin. Stereochemical mechanism involving transition-state stabilization

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Turkey coronavirus non-structure protein NSP15--an endoribonuclease

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SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant

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Automated MAD and MIR structure solution

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Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes

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1 reference

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Identifiers

10.1016/J.JMB.2009.07.062

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