The Rickettsia conorii Adr1 Interacts with the C-Terminus of Human Vitronectin in a Salt-Sensitive Manner. - Wikidata - wikimedia - TriplyDB

The Rickettsia conorii Adr1 Interacts with the C-Terminus of Human Vitronectin in a Salt-Sensitive Manner.

The Rickettsia conorii Adr1 Interacts with the C-Terminus of Human Vitronectin in a Salt-Sensitive Manner.

http://www.wikidata.org/entity/Q37672403

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Expression of Rickettsia Adr2 protein in E. coli is sufficient to promote resistance to complement-mediated killing, but not adherence to mammalian cells Immunity against the obligate intracellular bacterial pathogen Rickettsia australis requires functional complement system.

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The Rickettsia conorii Adr1 Interacts with the C-Terminus of Human Vitronectin in a Salt-Sensitive Manner.

http://www.wikidata.org/entity/Q37672403

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on March 2017

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

The Rickettsia conorii Adr1 In ...... in in a Salt-Sensitive Manner.

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The Rickettsia conorii Adr1 In ...... in in a Salt-Sensitive Manner.

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type

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The Rickettsia conorii Adr1 In ...... in in a Salt-Sensitive Manner.

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The Rickettsia conorii Adr1 In ...... in in a Salt-Sensitive Manner.

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FCIMB.2017.00061

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Frontiers in cellular and infection microbiology

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The Rickettsia conorii Adr1 In ...... in in a Salt-Sensitive Manner.

@en

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Abigail I Fish

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Juan J Martinez

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P2860

The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence

Haemophilus influenzae protein E recognizes the C-terminal domain of vitronectin and modulates the membrane attack complex

Haemophilus influenzae acquires vitronectin via the ubiquitous Protein F to subvert host innate immunity

Vitronectin in bacterial pathogenesis: a host protein used in complement escape and cellular invasion

Localization of the domains of the Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin

Characteristics of a new meningococcal serogroup B vaccine, bivalent rLP2086 (MenB-FHbp; Trumenba®).

Neisseria meningitidis Opc invasin binds to the sulphated tyrosines of activated vitronectin to attach to and invade human brain endothelial cells.

Pathogenic Rickettsia species acquire vitronectin from human serum to promote resistance to complement-mediated killing

Multimeric vitronectin. Identification and characterization of conformation-dependent self-association of the adhesive protein.

The hemopexin-type repeats of human vitronectin are recognized by Streptococcus pyogenes.

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61

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scholarly article

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10.3389/FCIMB.2017.00061

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7

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Kristian Riesbeck

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2017-03-01T00:00:00Z

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28299286

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5331051

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