Literature DB >> 7074096

Isolation, characterization, and synthesis of peptides from human fibrinogen that block the staphylococcal clumping reaction and construction of a synthetic clumping particle.

D D Strong, A P Laudano, J Hawiger, R F Doolittle.   

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Year:  1982        PMID： 7074096     DOI： 10.1021/bi00535a048

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  20 in total

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2.  Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization.

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3.  Specific binding of human fibrinogen fragment D to Aspergillus fumigatus conidia.

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4.  Functional studies of a fibrinogen binding protein from Staphylococcus epidermidis.

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Journal:  Infect Immun       Date:  1999-09       Impact factor: 3.441

5.  A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.

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6.  Use of synthetic peptides to identify an N-terminal epitope on mouse gamma interferon that may be involved in function.

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8.  Specific interaction of Aspergillus fumigatus with fibrinogen and its role in cell adhesion.

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9.  Staphylococcus aureus induces platelet aggregation via a fibrinogen-dependent mechanism which is independent of principal platelet glycoprotein IIb/IIIa fibrinogen-binding domains.

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10.  Genetic evidence that bound coagulase of Staphylococcus aureus is not clumping factor.

Authors:  D McDevitt; P Vaudaux; T J Foster
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