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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2009-2-11
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pubmed:abstractText |
SARS coronavirus main proteinase (SARS CoVMpro) is an important enzyme for the replication of Severe Acute Respiratory Syndrome virus. The active site region of SARS CoVMpro is divided into 8 subsites. Understanding the binding mode of SARS CoVMpro with a specific substrate is useful and contributes to structural-based drug design. The purpose of this research is to investigate the binding mode between the SARS CoVMpro and two octapeptides, especially in the region of the S3 subsite, through a molecular docking and molecular dynamics (MD) simulation approach.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-11842254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12671061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12682352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12730500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12730501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12746549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12890493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12917313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-12917450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-14585926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-15078103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-15214807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-15226499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-15691506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-15752746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19208150-16331324
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1471-2105
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10 Suppl 1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S48
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19208150-Binding Sites,
pubmed-meshheading:19208150-Catalytic Domain,
pubmed-meshheading:19208150-Computational Biology,
pubmed-meshheading:19208150-Cysteine Endopeptidases,
pubmed-meshheading:19208150-Cysteine Proteinase Inhibitors,
pubmed-meshheading:19208150-Hydrogen Bonding,
pubmed-meshheading:19208150-Models, Molecular,
pubmed-meshheading:19208150-Oligopeptides,
pubmed-meshheading:19208150-Protein Conformation,
pubmed-meshheading:19208150-SARS Virus,
pubmed-meshheading:19208150-Structure-Activity Relationship,
pubmed-meshheading:19208150-Substrate Specificity,
pubmed-meshheading:19208150-Viral Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
A computational analysis of SARS cysteine proteinase-octapeptide substrate interaction: implication for structure and active site binding mechanism.
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pubmed:affiliation |
Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkok, Thailand. s7500802@st.kmutt.ac.th
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pubmed:publicationType |
Journal Article
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