Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-9-12
pubmed:abstractText
Fibrinogen (Fg), the major clotting protein in blood plasma, plays key roles in blood coagulation and thrombosis. In addition, this 340 kD glycoprotein is a stress inducible protein; its synthesis is dramatically upregulated during inflammation or under exposure to stress such systemic infections. This regulation of Fg expression indicates that Fg also participates in the host defense system against infections. In fact, a number of reported studies have demonstrated the involvement of both the intrinsic and extrinsic pathways of coagulation; the thrombotic and the fibrinolytic systems in the pathophysiology of infectious diseases. It is, therefore, perhaps not surprising that many pathogenic bacteria can interact with Fg and manipulate its biology. This review focuses on the major Fg-binding proteins (Fgbps) from Gram-positive bacteria with an emphasis on those that are known to have an effect on coagulation and thrombosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ClfA protein, Staphylococcus aureus, http://linkedlifedata.com/resource/pubmed/chemical/Coagulase, http://linkedlifedata.com/resource/pubmed/chemical/Fbe protein, bacteria, http://linkedlifedata.com/resource/pubmed/chemical/FbsA protein, Streptococcus..., http://linkedlifedata.com/resource/pubmed/chemical/Fib protein, Staphylococcus aureus, http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen, http://linkedlifedata.com/resource/pubmed/chemical/MSCRAMM proteins, Staphylococcus, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/fibronectin-binding proteins..., http://linkedlifedata.com/resource/pubmed/chemical/opacity factor, http://linkedlifedata.com/resource/pubmed/chemical/streptococcal M protein
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
503-11
pubmed:dateRevised
2010-10-19
pubmed:meshHeading
pubmed-meshheading:17849038-Adhesins, Bacterial, pubmed-meshheading:17849038-Animals, pubmed-meshheading:17849038-Antigens, Bacterial, pubmed-meshheading:17849038-Bacterial Outer Membrane Proteins, pubmed-meshheading:17849038-Bacterial Proteins, pubmed-meshheading:17849038-Blood Coagulation, pubmed-meshheading:17849038-Carrier Proteins, pubmed-meshheading:17849038-Coagulase, pubmed-meshheading:17849038-Fibrinogen, pubmed-meshheading:17849038-Humans, pubmed-meshheading:17849038-Models, Molecular, pubmed-meshheading:17849038-Peptide Hydrolases, pubmed-meshheading:17849038-Protein Conformation, pubmed-meshheading:17849038-Staphylococcal Infections, pubmed-meshheading:17849038-Staphylococcus, pubmed-meshheading:17849038-Streptococcal Infections, pubmed-meshheading:17849038-Streptococcus, pubmed-meshheading:17849038-Thrombosis
pubmed:year
2007
pubmed:articleTitle
Fibrinogen-binding proteins of Gram-positive bacteria.
pubmed:affiliation
CEMB, Institute of Biosciences and Technology, 2121 W. Holcombe, Houston, Texas 77030, USA. jrivera@ibt.tamhsc.edu
pubmed:publicationType
Journal Article, Review