Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses.
Identifieur interne : 002808 ( PubMed/Checkpoint ); précédent : 002807; suivant : 002809Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses.
Auteurs : Tswen-Kei Tang [Taïwan] ; Mark P-J Wu ; Shui-Tsung Chen ; Ming-Hon Hou ; Ming-Hsiang Hong ; Fu-Ming Pan ; Hui-Ming Yu ; Jenn-Han Chen ; Chen-Wen Yao ; Andrew H-J WangSource :
- Proteomics [ 1615-9853 ] ; 2005.
Descripteurs français
- KwdFr :
- ADN (), ADN complémentaire (métabolisme), ARN (), Acides aminés (), Analyse par réseau de protéines (), Animaux, Anticorps antiviraux (), Antigènes (), Antigènes viraux (), Cadres ouverts de lecture, Cellules Vero, Chromatographie sur gel, Clonage moléculaire, Coronavirus humain 229E (métabolisme), Dichroïsme circulaire, Dimérisation, Données de séquences moléculaires, Humains, Lapins, Liaison aux protéines, Microscopie de fluorescence, Nucléocapside (), Peptides (), Protéines nucléocapside (), Protéomique (), Réactifs réticulants (pharmacologie), Similitude de séquences d'acides aminés, Sites de fixation, Structure tertiaire des protéines, Syndrome respiratoire aigu sévère (diagnostic), Séquence d'acides aminés, Test ELISA, Virus du SRAS (métabolisme), Électrophorèse sur gel de polyacrylamide, Épitopes ().
- MESH :
- diagnostic : Syndrome respiratoire aigu sévère.
- métabolisme : ADN complémentaire, Coronavirus humain 229E, Virus du SRAS.
- pharmacologie : Réactifs réticulants.
- ADN, ARN, Acides aminés, Analyse par réseau de protéines, Animaux, Anticorps antiviraux, Antigènes, Antigènes viraux, Cadres ouverts de lecture, Cellules Vero, Chromatographie sur gel, Clonage moléculaire, Dichroïsme circulaire, Dimérisation, Données de séquences moléculaires, Humains, Lapins, Liaison aux protéines, Microscopie de fluorescence, Nucléocapside, Peptides, Protéines nucléocapside, Protéomique, Similitude de séquences d'acides aminés, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Test ELISA, Électrophorèse sur gel de polyacrylamide, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acids (chemistry), Animals, Antibodies, Viral (chemistry), Antigens (chemistry), Antigens, Viral (chemistry), Binding Sites, Chlorocebus aethiops, Chromatography, Gel, Circular Dichroism, Cloning, Molecular, Coronavirus 229E, Human (metabolism), Cross-Linking Reagents (pharmacology), DNA (chemistry), DNA, Complementary (metabolism), Dimerization, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Epitopes (chemistry), Humans, Microscopy, Fluorescence, Molecular Sequence Data, Nucleocapsid (chemistry), Nucleocapsid Proteins (chemistry), Open Reading Frames, Peptides (chemistry), Protein Array Analysis (methods), Protein Binding, Protein Structure, Tertiary, Proteomics (methods), RNA (chemistry), Rabbits, SARS Virus (metabolism), Sequence Homology, Amino Acid, Severe Acute Respiratory Syndrome (diagnosis), Vero Cells.
- MESH :
- chemical , chemistry : Amino Acids, Antibodies, Viral, Antigens, Antigens, Viral, DNA, Epitopes, Nucleocapsid Proteins, Peptides, RNA.
- chemistry : Nucleocapsid.
- diagnosis : Severe Acute Respiratory Syndrome.
- metabolism : Coronavirus 229E, Human, DNA, Complementary, SARS Virus.
- methods : Protein Array Analysis, Proteomics.
- chemical , pharmacology : Cross-Linking Reagents.
- Amino Acid Sequence, Animals, Binding Sites, Chlorocebus aethiops, Chromatography, Gel, Circular Dichroism, Cloning, Molecular, Dimerization, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Humans, Microscopy, Fluorescence, Molecular Sequence Data, Open Reading Frames, Protein Binding, Protein Structure, Tertiary, Rabbits, Sequence Homology, Amino Acid, Vero Cells.
Abstract
Severe acute respiratory syndrome (SARS) is a serious health threat and its early diagnosis is important for infection control and potential treatment of the disease. Diagnostic tools require rapid and accurate methods, of which a capture ELISA method may be useful. Toward this goal, we have prepared and characterized soluble full-length nucleocapsid proteins (N protein) from SARS and 229E human coronaviruses. N proteins form oligomers, mostly as dimers at low concentration. These two N proteins degrade rapidly upon storage and the major degraded N protein is the C-terminal fragment of amino acid (aa) 169-422. Taken together with other data, we suggest that N protein is a two-domain protein, with the N-terminal aa 50-150 as the RNA-binding domain and the C-terminal aa 169-422 as the dimerization domain. Polyclonal antibodies against the SARS N protein have been produced and the strong binding sites of the anti-nucleocapsid protein (NP) antibodies produced were mapped to aa 1-20, aa 150-170 and aa 390-410. These sites are generally consistent with those mapped by sera obtained from SARS patients. The SARS anti-NP antibody was able to clearly detect SARS virus grown in Vero E6 cells and did not cross-react with the NP from the human coronavirus 229E. We have predicted several antigenic sites (15-20 amino acids) of S, M and N proteins and produced antibodies against those peptides, some of which could be recognized by sera obtained from SARS patients. Antibodies against the NP peptides could detect the cognate N protein clearly. Further refinement of these antibodies, particularly large-scale production of monoclonal antibodies, could lead to the development of useful diagnostic kits for diseases associated with SARS and other human coronaviruses.
DOI: 10.1002/pmic.200401204
PubMed: 15759315
Affiliations:
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pubmed:15759315Le document en format XML
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Gel</term><term>Circular Dichroism</term><term>Cloning, Molecular</term><term>Coronavirus 229E, Human (metabolism)</term><term>Cross-Linking Reagents (pharmacology)</term><term>DNA (chemistry)</term><term>DNA, Complementary (metabolism)</term><term>Dimerization</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitopes (chemistry)</term><term>Humans</term><term>Microscopy, Fluorescence</term><term>Molecular Sequence Data</term><term>Nucleocapsid (chemistry)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Open Reading Frames</term><term>Peptides (chemistry)</term><term>Protein Array Analysis (methods)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Proteomics (methods)</term><term>RNA (chemistry)</term><term>Rabbits</term><term>SARS Virus (metabolism)</term><term>Sequence Homology, Amino Acid</term><term>Severe Acute Respiratory Syndrome (diagnosis)</term><term>Vero Cells</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN ()</term><term>ADN complémentaire (métabolisme)</term><term>ARN ()</term><term>Acides aminés ()</term><term>Analyse par réseau de protéines ()</term><term>Animaux</term><term>Anticorps antiviraux ()</term><term>Antigènes ()</term><term>Antigènes viraux ()</term><term>Cadres ouverts de lecture</term><term>Cellules Vero</term><term>Chromatographie sur gel</term><term>Clonage moléculaire</term><term>Coronavirus humain 229E (métabolisme)</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Lapins</term><term>Liaison aux protéines</term><term>Microscopie de fluorescence</term><term>Nucléocapside ()</term><term>Peptides ()</term><term>Protéines nucléocapside ()</term><term>Protéomique ()</term><term>Réactifs réticulants (pharmacologie)</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Syndrome respiratoire aigu sévère (diagnostic)</term><term>Séquence d'acides aminés</term><term>Test ELISA</term><term>Virus du SRAS (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide</term><term>Épitopes ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Antibodies, Viral</term><term>Antigens</term><term>Antigens, Viral</term><term>DNA</term><term>Epitopes</term><term>Nucleocapsid Proteins</term><term>Peptides</term><term>RNA</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid</term></keywords><keywords scheme="MESH" qualifier="diagnosis" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="diagnostic" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus 229E, Human</term><term>DNA, Complementary</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Array Analysis</term><term>Proteomics</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN complémentaire</term><term>Coronavirus humain 229E</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Réactifs réticulants</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cross-Linking Reagents</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Chlorocebus aethiops</term><term>Chromatography, Gel</term><term>Circular Dichroism</term><term>Cloning, Molecular</term><term>Dimerization</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Humans</term><term>Microscopy, Fluorescence</term><term>Molecular Sequence Data</term><term>Open Reading Frames</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Rabbits</term><term>Sequence Homology, Amino Acid</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN</term><term>ARN</term><term>Acides aminés</term><term>Analyse par réseau de protéines</term><term>Animaux</term><term>Anticorps antiviraux</term><term>Antigènes</term><term>Antigènes viraux</term><term>Cadres ouverts de lecture</term><term>Cellules Vero</term><term>Chromatographie sur gel</term><term>Clonage moléculaire</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Lapins</term><term>Liaison aux protéines</term><term>Microscopie de fluorescence</term><term>Nucléocapside</term><term>Peptides</term><term>Protéines nucléocapside</term><term>Protéomique</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Test ELISA</term><term>Électrophorèse sur gel de polyacrylamide</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is a serious health threat and its early diagnosis is important for infection control and potential treatment of the disease. Diagnostic tools require rapid and accurate methods, of which a capture ELISA method may be useful. Toward this goal, we have prepared and characterized soluble full-length nucleocapsid proteins (N protein) from SARS and 229E human coronaviruses. N proteins form oligomers, mostly as dimers at low concentration. These two N proteins degrade rapidly upon storage and the major degraded N protein is the C-terminal fragment of amino acid (aa) 169-422. Taken together with other data, we suggest that N protein is a two-domain protein, with the N-terminal aa 50-150 as the RNA-binding domain and the C-terminal aa 169-422 as the dimerization domain. Polyclonal antibodies against the SARS N protein have been produced and the strong binding sites of the anti-nucleocapsid protein (NP) antibodies produced were mapped to aa 1-20, aa 150-170 and aa 390-410. These sites are generally consistent with those mapped by sera obtained from SARS patients. The SARS anti-NP antibody was able to clearly detect SARS virus grown in Vero E6 cells and did not cross-react with the NP from the human coronavirus 229E. We have predicted several antigenic sites (15-20 amino acids) of S, M and N proteins and produced antibodies against those peptides, some of which could be recognized by sera obtained from SARS patients. Antibodies against the NP peptides could detect the cognate N protein clearly. Further refinement of these antibodies, particularly large-scale production of monoclonal antibodies, could lead to the development of useful diagnostic kits for diseases associated with SARS and other human coronaviruses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15759315</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1615-9853</ISSN><JournalIssue CitedMedium="Print"><Volume>5</Volume><Issue>4</Issue><PubDate><Year>2005</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Proteomics</Title><ISOAbbreviation>Proteomics</ISOAbbreviation></Journal><ArticleTitle>Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses.</ArticleTitle><Pagination><MedlinePgn>925-37</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is a serious health threat and its early diagnosis is important for infection control and potential treatment of the disease. Diagnostic tools require rapid and accurate methods, of which a capture ELISA method may be useful. Toward this goal, we have prepared and characterized soluble full-length nucleocapsid proteins (N protein) from SARS and 229E human coronaviruses. N proteins form oligomers, mostly as dimers at low concentration. These two N proteins degrade rapidly upon storage and the major degraded N protein is the C-terminal fragment of amino acid (aa) 169-422. Taken together with other data, we suggest that N protein is a two-domain protein, with the N-terminal aa 50-150 as the RNA-binding domain and the C-terminal aa 169-422 as the dimerization domain. Polyclonal antibodies against the SARS N protein have been produced and the strong binding sites of the anti-nucleocapsid protein (NP) antibodies produced were mapped to aa 1-20, aa 150-170 and aa 390-410. These sites are generally consistent with those mapped by sera obtained from SARS patients. The SARS anti-NP antibody was able to clearly detect SARS virus grown in Vero E6 cells and did not cross-react with the NP from the human coronavirus 229E. We have predicted several antigenic sites (15-20 amino acids) of S, M and N proteins and produced antibodies against those peptides, some of which could be recognized by sera obtained from SARS patients. Antibodies against the NP peptides could detect the cognate N protein clearly. Further refinement of these antibodies, particularly large-scale production of monoclonal antibodies, could lead to the development of useful diagnostic kits for diseases associated with SARS and other human coronaviruses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tang</LastName><ForeName>Tswen-Kei</ForeName><Initials>TK</Initials><AffiliationInfo><Affiliation>Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Mark P-J</ForeName><Initials>MP</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Shui-Tsung</ForeName><Initials>ST</Initials></Author><Author ValidYN="Y"><LastName>Hou</LastName><ForeName>Ming-Hon</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Hong</LastName><ForeName>Ming-Hsiang</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Pan</LastName><ForeName>Fu-Ming</ForeName><Initials>FM</Initials></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Hui-Ming</ForeName><Initials>HM</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Jenn-Han</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Yao</LastName><ForeName>Chen-Wen</ForeName><Initials>CW</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Andrew H-J</ForeName><Initials>AH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Proteomics</MedlineTA><NlmUniqueID>101092707</NlmUniqueID><ISSNLinking>1615-9853</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000941">Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000956">Antigens, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003432">Cross-Linking Reagents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-49-2</RegistryNumber><NameOfSubstance UI="D004247">DNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000737" 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MajorTopicYN="N">Coronavirus 229E, Human</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003432" MajorTopicYN="N">Cross-Linking Reagents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004247" MajorTopicYN="N">DNA</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019251" MajorTopicYN="N">Nucleocapsid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040081" MajorTopicYN="N">Protein Array Analysis</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011817" MajorTopicYN="N">Rabbits</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000175" MajorTopicYN="N">diagnosis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>3</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>9</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>3</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15759315</ArticleId><ArticleId IdType="doi">10.1002/pmic.200401204</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Chen, Jenn Han" sort="Chen, Jenn Han" uniqKey="Chen J" first="Jenn-Han" last="Chen">Jenn-Han Chen</name><name sortKey="Chen, Shui Tsung" sort="Chen, Shui Tsung" uniqKey="Chen S" first="Shui-Tsung" last="Chen">Shui-Tsung Chen</name><name sortKey="Hong, Ming Hsiang" sort="Hong, Ming Hsiang" uniqKey="Hong M" first="Ming-Hsiang" last="Hong">Ming-Hsiang Hong</name><name sortKey="Hou, Ming Hon" sort="Hou, Ming Hon" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name><name sortKey="Pan, Fu Ming" sort="Pan, Fu Ming" uniqKey="Pan F" first="Fu-Ming" last="Pan">Fu-Ming Pan</name><name sortKey="Wang, Andrew H J" sort="Wang, Andrew H J" uniqKey="Wang A" first="Andrew H-J" last="Wang">Andrew H-J Wang</name><name sortKey="Wu, Mark P J" sort="Wu, Mark P J" uniqKey="Wu M" first="Mark P-J" last="Wu">Mark P-J Wu</name><name sortKey="Yao, Chen Wen" sort="Yao, Chen Wen" uniqKey="Yao C" first="Chen-Wen" last="Yao">Chen-Wen Yao</name><name sortKey="Yu, Hui Ming" sort="Yu, Hui Ming" uniqKey="Yu H" first="Hui-Ming" last="Yu">Hui-Ming Yu</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Tang, Tswen Kei" sort="Tang, Tswen Kei" uniqKey="Tang T" first="Tswen-Kei" last="Tang">Tswen-Kei Tang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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