Antibody fragment expression and purification.
Identifieur interne : 001950 ( PubMed/Corpus ); précédent : 001949; suivant : 001951Antibody fragment expression and purification.
Auteurs : Dimana Dimitrova ; Vidita Choudhry ; Christopher C. BroderSource :
- Methods in molecular biology (Clifton, N.J.) [ 1064-3745 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Immunoglobulin Fab Fragments, Immunoglobulin Fragments.
- chemical , metabolism : Immunoglobulin Fragments.
- methods : Molecular Biology.
- Bacteriophages, Humans.
Abstract
Interest in the potential of monoclonal antibodies (mAbs) to serve as therapeutic agents has surged in the past decade with a major emphasis on human viral diseases. There has been much attention in this area directed towards the human immunodeficiency virus type-1 (HIV-1) and promising research developments have emerged on the inhibition of HIV-1 infection by mAbs and the identification of several highly conserved neutralizing epitopes. More recently, potent fully-human neutralizing mAbs have been developed against a variety of important human viral disease agents including the paramyxoviruses Hendra virus and Nipah virus, and human or humanized mAbs have been developed against severe acute respiratory syndrome coronavirus (SARS CoV), and West Nile virus, among others. Most of these more recently developed antiviral mAbs have come from the use of antibody phage-display technologies and the implementation of simplified, inexpensive yet efficient methods, for expressing and purifying the initially selected fragment antibodies is of prime importance in further facilitating this area of research.
DOI: 10.1007/978-1-59745-554-1_25
PubMed: 19252844
Links to Exploration step
pubmed:19252844Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antibody fragment expression and purification.</title><author><name sortKey="Dimitrova, Dimana" sort="Dimitrova, Dimana" uniqKey="Dimitrova D" first="Dimana" last="Dimitrova">Dimana Dimitrova</name><affiliation><nlm:affiliation>Uniformed Services University of the Health Sciences, Bethesda, MD, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Choudhry, Vidita" sort="Choudhry, Vidita" uniqKey="Choudhry V" first="Vidita" last="Choudhry">Vidita Choudhry</name></author><author><name sortKey="Broder, Christopher C" sort="Broder, Christopher C" uniqKey="Broder C" first="Christopher C" last="Broder">Christopher C. Broder</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19252844</idno><idno type="pmid">19252844</idno><idno type="doi">10.1007/978-1-59745-554-1_25</idno><idno type="wicri:Area/PubMed/Corpus">001950</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001950</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Antibody fragment expression and purification.</title><author><name sortKey="Dimitrova, Dimana" sort="Dimitrova, Dimana" uniqKey="Dimitrova D" first="Dimana" last="Dimitrova">Dimana Dimitrova</name><affiliation><nlm:affiliation>Uniformed Services University of the Health Sciences, Bethesda, MD, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Choudhry, Vidita" sort="Choudhry, Vidita" uniqKey="Choudhry V" first="Vidita" last="Choudhry">Vidita Choudhry</name></author><author><name sortKey="Broder, Christopher C" sort="Broder, Christopher C" uniqKey="Broder C" first="Christopher C" last="Broder">Christopher C. Broder</name></author></analytic><series><title level="j">Methods in molecular biology (Clifton, N.J.)</title><idno type="ISSN">1064-3745</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophages</term><term>Humans</term><term>Immunoglobulin Fab Fragments (isolation & purification)</term><term>Immunoglobulin Fragments (isolation & purification)</term><term>Immunoglobulin Fragments (metabolism)</term><term>Molecular Biology (methods)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Immunoglobulin Fab Fragments</term><term>Immunoglobulin Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Immunoglobulin Fragments</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Molecular Biology</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Bacteriophages</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Interest in the potential of monoclonal antibodies (mAbs) to serve as therapeutic agents has surged in the past decade with a major emphasis on human viral diseases. There has been much attention in this area directed towards the human immunodeficiency virus type-1 (HIV-1) and promising research developments have emerged on the inhibition of HIV-1 infection by mAbs and the identification of several highly conserved neutralizing epitopes. More recently, potent fully-human neutralizing mAbs have been developed against a variety of important human viral disease agents including the paramyxoviruses Hendra virus and Nipah virus, and human or humanized mAbs have been developed against severe acute respiratory syndrome coronavirus (SARS CoV), and West Nile virus, among others. Most of these more recently developed antiviral mAbs have come from the use of antibody phage-display technologies and the implementation of simplified, inexpensive yet efficient methods, for expressing and purifying the initially selected fragment antibodies is of prime importance in further facilitating this area of research.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19252844</PMID><DateCompleted><Year>2009</Year><Month>04</Month><Day>22</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1064-3745</ISSN><JournalIssue CitedMedium="Print"><Volume>525</Volume><PubDate><Year>2009</Year></PubDate></JournalIssue><Title>Methods in molecular biology (Clifton, N.J.)</Title><ISOAbbreviation>Methods Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Antibody fragment expression and purification.</ArticleTitle><Pagination><MedlinePgn>491-8, xiii</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/978-1-59745-554-1_25</ELocationID><Abstract><AbstractText>Interest in the potential of monoclonal antibodies (mAbs) to serve as therapeutic agents has surged in the past decade with a major emphasis on human viral diseases. There has been much attention in this area directed towards the human immunodeficiency virus type-1 (HIV-1) and promising research developments have emerged on the inhibition of HIV-1 infection by mAbs and the identification of several highly conserved neutralizing epitopes. More recently, potent fully-human neutralizing mAbs have been developed against a variety of important human viral disease agents including the paramyxoviruses Hendra virus and Nipah virus, and human or humanized mAbs have been developed against severe acute respiratory syndrome coronavirus (SARS CoV), and West Nile virus, among others. Most of these more recently developed antiviral mAbs have come from the use of antibody phage-display technologies and the implementation of simplified, inexpensive yet efficient methods, for expressing and purifying the initially selected fragment antibodies is of prime importance in further facilitating this area of research.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dimitrova</LastName><ForeName>Dimana</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Uniformed Services University of the Health Sciences, Bethesda, MD, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Choudhry</LastName><ForeName>Vidita</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Broder</LastName><ForeName>Christopher C</ForeName><Initials>CC</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>AI054715</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 AI057168-010002</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI054715</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI057168</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI054715-03</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 AI057168</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI054715-02</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Methods Mol Biol</MedlineTA><NlmUniqueID>9214969</NlmUniqueID><ISSNLinking>1064-3745</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007140">Immunoglobulin Fab Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007128">Immunoglobulin Fragments</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001435" MajorTopicYN="N">Bacteriophages</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007140" MajorTopicYN="N">Immunoglobulin Fab Fragments</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007128" MajorTopicYN="N">Immunoglobulin Fragments</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008967" MajorTopicYN="N">Molecular Biology</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>3</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>3</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>4</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19252844</ArticleId><ArticleId IdType="doi">10.1007/978-1-59745-554-1_25</ArticleId><ArticleId IdType="pmc">PMC2858623</ArticleId><ArticleId IdType="mid">NIHMS189626</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Curr Opin Biotechnol. 1997 Aug;8(4):503-8</Citation><ArticleIdList><ArticleId IdType="pubmed">9265732</ArticleId></ArticleIdList></Reference><Reference><Citation>J Infect Dis. 1997 Nov;176(5):1215-24</Citation><ArticleIdList><ArticleId IdType="pubmed">9359721</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Immunol. 1997 Apr;9(2):201-12</Citation><ArticleIdList><ArticleId IdType="pubmed">9099794</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Chem. 2005 May;51(5):830-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15718486</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Med. 2005 May;11(5):522-30</Citation><ArticleIdList><ArticleId IdType="pubmed">15852016</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Cancer. 2007 Sep;7(9):701-6</Citation><ArticleIdList><ArticleId IdType="pubmed">17721434</ArticleId></ArticleIdList></Reference><Reference><Citation>Expert Rev Anti Infect Ther. 2006 Feb;4(1):57-66</Citation><ArticleIdList><ArticleId IdType="pubmed">16441209</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 2006 Jul;72(7):4589-95</Citation><ArticleIdList><ArticleId IdType="pubmed">16820448</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2007 Jun 20;363(1):79-90</Citation><ArticleIdList><ArticleId IdType="pubmed">17306322</ArticleId></ArticleIdList></Reference><Reference><Citation>Oncogene. 2007 May 28;26(25):3714-33</Citation><ArticleIdList><ArticleId IdType="pubmed">17530025</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):12123-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17620608</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Jan;80(2):891-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16378991</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001950 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 001950 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:19252844
|texte= Antibody fragment expression and purification.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:19252844" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |