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rdf:type |
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lifeskim:mentions |
umls-concept:C0004651,
umls-concept:C0021027,
umls-concept:C0023621,
umls-concept:C0036576,
umls-concept:C0205171,
umls-concept:C0242210,
umls-concept:C0332307,
umls-concept:C0567416,
umls-concept:C1413972,
umls-concept:C1514562,
umls-concept:C1706124,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:dateCreated |
2008-9-9
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pubmed:abstractText |
Protein A, protein G and protein L are three well-defined immunoglobulin (Ig)-binding proteins (IBPs), which show affinity for specific sites on Ig of mammalian hosts. Although the precise functions of these molecules are not fully understood, it is thought that they play an important role in pathogenicity of bacteria. The single domains of protein A, protein G and protein L were all demonstrated to have function to bind to Ig. Whether combinations of Ig-binding domains of various IBPs could exhibit useful novel binding is interesting.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-10229674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-10398395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-10678837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-10805799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-11587642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-11955599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-1390743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-1420164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-1460053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-15183931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-15488939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-15769469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-1733930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-1871600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-1909733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-2495325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-2738404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-2938951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-2964447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-3017704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-3745123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-557409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-6319407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-6338496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-7664045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-7743134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-7788293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-7947810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-8413328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-9700502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18700046-9874260
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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 |
1471-2180
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pubmed:author |
pubmed-author:ChenQiu-LiQL,
pubmed-author:JiaJian-AnJA,
pubmed-author:JiangShao-HuaSH,
pubmed-author:KeyD DDD,
pubmed-author:LiLian-QingLQ,
pubmed-author:LiaoWen-TingWT,
pubmed-author:PanXinX,
pubmed-author:QiZhong-TianZT,
pubmed-author:WenZong-MeiZM,
pubmed-author:XuRongR,
pubmed-author:YangHuaH,
pubmed-author:YinP HPH,
pubmed-author:ZhouXiaX
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pubmed:issnType |
Electronic
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
137
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2008
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pubmed:articleTitle |
Evolutional selection of a combinatorial phage library displaying randomly-rearranged various single domains of immunoglobulin (Ig)-binding proteins (IBPs) with four kinds of Ig molecules.
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pubmed:affiliation |
Department of Microbiology, State Key Laboratory of Medical Immunology, Second Military Medical University, Shanghai 200433, PR China. yanghua97065@yahoo.com.cn
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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