Yersinia adhesin A (YadA) – Beauty & beast-Reference-Cited by-同舟云学术

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Yersinia adhesin A (YadA) – Beauty & beast

Published:2015-02 Issue:2 Volume:305 Page:252-258
ISSN:1438-4221
Container-title:International Journal of Medical Microbiology
language:en
Short-container-title:International Journal of Medical Microbiology

Author:

Mühlenkamp Melanie,Oberhettinger Philipp,Leo Jack C.,Linke Dirk,Schütz Monika S.

Funder

German Research Council

University Hospital Tübingen TÜFF

UKT fortüne

German Center for Infection Research

VISTA

Publisher

Elsevier BV

Subject

Infectious Diseases,Microbiology (medical),General Medicine,Microbiology

Reference80 articles.

1. Killing of dsrA mutants of Haemophilus ducreyi by normal human serum occurs via the classical complement pathway and is initiated by immunoglobulin M binding;Abdullah;Infect. Immun.,2005

2. Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica;Ackermann;J. Bacteriol.,2008

3. Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica;Ackermann;J. Bacteriol.,2008

4. A transition from strong right-handed to canonical left-handed supercoiling in a conserved coiled-coil segment of trimeric autotransporter adhesins;Alvarez;J. Struct. Biol.,2010

5. Characterization of complement factor H binding to Yersinia enterocolitica serotype O:3;Biedzka-Sarek;Infect. Immun.,2008

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3. Yersinia pestis;Molecular Medical Microbiology;2024

4. The Love and Hate Relationship between T5SS and Other Secretion Systems in Bacteria;International Journal of Molecular Sciences;2023-12-24

5. A poly‐proline II helix in YadA from Yersinia enterocolitica serotype O:9 facilitates heparin binding through electrostatic interactions;The FEBS Journal;2023-11-27

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