Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: Interaction of the extracellular enzyme with human plasminogen and fibrinogen

Author:

Egea L.,Aguilera L.,Giménez R.,Sorolla M.A.,Aguilar J.,Badía J.,Baldoma L.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry

Reference40 articles.

1. Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K-12;Baldoma;Journal of Biological Chemistry,1987

2. Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli;Balsalobre;Molecular Microbiology,2006

3. Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasilensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells;Barbosa;Infection & Immunity,2006

4. The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration;Bergmann;Thrombosis and Haemostasis,2005

5. Structures of gram-negative cell walls and their derived membrane vesicles;Beveridge;Journal of Bacteriology,1999

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