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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-4-23
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pubmed:abstractText |
Chaperones are ubiquitous conserved proteins critical in stabilization of new proteins, repair/removal of defective proteins and immunodominant antigens in innate and adaptive immunity. Periodontal disease is a chronic inflammatory infection associated with infection by Porphyromonas gingivalis that culminates in the destruction of the supporting structures of the teeth. We previously reported studies of serum antibodies reactive with the human chaperone Hsp90 in gingivitis, a reversible form of gingival disease confined to the oral soft tissues. In those studies, antibodies were at their highest levels in subjects with the best oral health. We hypothesized that antibodies to the HSP90 homologue of P. gingivalis (HtpG) might be associated with protection/resistance against destructive periodontitis.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-10522229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-10534073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-10576699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-10685367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-10983884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-14296927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-14656896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-14980431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-15008982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-15140573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-15165254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-15597150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-15713605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-16248272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-16409250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-16417949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-16438680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-16513386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-16677293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-17100776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-1718852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-17346315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-17425262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-17615388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-18030332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-2969967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-8182133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18431474-9715365
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HtpG protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e1984
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18431474-Adult,
pubmed-meshheading:18431474-Amino Acid Sequence,
pubmed-meshheading:18431474-Antibodies, Bacterial,
pubmed-meshheading:18431474-Antibody Formation,
pubmed-meshheading:18431474-Antigens, Bacterial,
pubmed-meshheading:18431474-Bacterial Proteins,
pubmed-meshheading:18431474-Cluster Analysis,
pubmed-meshheading:18431474-Colony Count, Microbial,
pubmed-meshheading:18431474-Dental Plaque,
pubmed-meshheading:18431474-Disease Susceptibility,
pubmed-meshheading:18431474-Female,
pubmed-meshheading:18431474-Fusobacterium nucleatum,
pubmed-meshheading:18431474-HSP90 Heat-Shock Proteins,
pubmed-meshheading:18431474-Health,
pubmed-meshheading:18431474-Humans,
pubmed-meshheading:18431474-Immunoglobulin G,
pubmed-meshheading:18431474-Male,
pubmed-meshheading:18431474-Molecular Chaperones,
pubmed-meshheading:18431474-Molecular Sequence Data,
pubmed-meshheading:18431474-Peptides,
pubmed-meshheading:18431474-Periodontitis,
pubmed-meshheading:18431474-Porphyromonas gingivalis,
pubmed-meshheading:18431474-Serum
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pubmed:year |
2008
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pubmed:articleTitle |
Serum antibodies to Porphyromonas gingivalis chaperone HtpG predict health in periodontitis susceptible patients.
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pubmed:affiliation |
Department of Biologic and Materials Sciences, The University of Michigan School of Dentistry, Ann Arbor, Michigan, United States of America. ceshelbu@umich.edu
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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