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PDF) The Contribution of Accessory Toxins of Vibrio cholerae O1 El Tor to  the Proinflammatory Response in a Murine Pulmonary Cholera Model
PDF) The Contribution of Accessory Toxins of Vibrio cholerae O1 El Tor to the Proinflammatory Response in a Murine Pulmonary Cholera Model

Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease  domain | The EMBO Journal
Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain | The EMBO Journal

IAI Table of Contents Volume 80, Issue 8
IAI Table of Contents Volume 80, Issue 8

The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly  Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological  Chemistry
The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological Chemistry

The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly  Catalyzes the Covalent Cross-linking of Actin - ScienceDirect
The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly Catalyzes the Covalent Cross-linking of Actin - ScienceDirect

Karla Fullner Satchell : Faculty Profile: Faculty Profiles: Feinberg School  of Medicine: Northwestern University
Karla Fullner Satchell : Faculty Profile: Faculty Profiles: Feinberg School of Medicine: Northwestern University

Structure-Function Analysis of Inositol Hexakisphosphate-induced  Autoprocessing of the Vibrio cholerae Multifunctional Autoprocessing RTX  Toxin - ScienceDirect
Structure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing of the Vibrio cholerae Multifunctional Autoprocessing RTX Toxin - ScienceDirect

Identification of a domain within the multifunctional <italic  toggle='yes'>Vibrio cholerae</italic> RTX toxi
Identification of a domain within the multifunctional <italic toggle='yes'>Vibrio cholerae</italic> RTX toxi

The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly  Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological  Chemistry
The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological Chemistry

Structure-Function Analysis of Inositol Hexakisphosphate-induced  Autoprocessing of the Vibrio cholerae Multifunctional Autoprocessing RTX  Toxin - ScienceDirect
Structure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing of the Vibrio cholerae Multifunctional Autoprocessing RTX Toxin - ScienceDirect

Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease  domain | The EMBO Journal
Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain | The EMBO Journal

Event: PATB Committee Protein Toxins Workshop - HESI - Health and  Environmental Sciences Institute
Event: PATB Committee Protein Toxins Workshop - HESI - Health and Environmental Sciences Institute

Microbes and Infection | Vol 5, Issue 13, Pages 1165-1288 (November 2003) |  ScienceDirect.com by Elsevier
Microbes and Infection | Vol 5, Issue 13, Pages 1165-1288 (November 2003) | ScienceDirect.com by Elsevier

Prolonged Colonization of Mice by Vibrio cholerae El Tor O1 Depends on  Accessory Toxins | Infection and Immunity
Prolonged Colonization of Mice by Vibrio cholerae El Tor O1 Depends on Accessory Toxins | Infection and Immunity

Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease  domain | The EMBO Journal
Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain | The EMBO Journal

The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly  Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological  Chemistry
The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological Chemistry

American Academy of Microbiology Names 16 Women as Fellows : Women In  Academia Report
American Academy of Microbiology Names 16 Women as Fellows : Women In Academia Report

Identification of a domain within the multifunctional Vibrio cholerae RTX  toxin that covalently cross-links actin | PNAS
Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin | PNAS

Neutrophils are essential for containment of Vibrio cholerae to the  intestine during the proinflammatory phase of infection. - Abstract -  Europe PMC
Neutrophils are essential for containment of Vibrio cholerae to the intestine during the proinflammatory phase of infection. - Abstract - Europe PMC

MARTX, Multifunctional Autoprocessing Repeats-in-Toxin Toxins | Infection  and Immunity
MARTX, Multifunctional Autoprocessing Repeats-in-Toxin Toxins | Infection and Immunity

Characterization of the Enzymatic Activity of the Actin Cross-linking  Domain from the Vibrio cholerae MARTXVc Toxin*
Characterization of the Enzymatic Activity of the Actin Cross-linking Domain from the Vibrio cholerae MARTXVc Toxin*

Identification of a domain within the multifunctional Vibrio cholerae RTX  toxin that covalently cross-links actin | PNAS
Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin | PNAS

The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly  Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological  Chemistry
The Actin Cross-linking Domain of the Vibrio cholerae RTX Toxin Directly Catalyzes the Covalent Cross-linking of Actin* - Journal of Biological Chemistry

Structure-Function Analysis of Inositol Hexakisphosphate-induced  Autoprocessing of the Vibrio cholerae Multifunctional Autoprocessing RTX  Toxin - ScienceDirect
Structure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing of the Vibrio cholerae Multifunctional Autoprocessing RTX Toxin - ScienceDirect

Auto-catalytic Cleavage of Clostridium difficile Toxins A and B Depends on  Cysteine Protease Activity* - Journal of Biological Chemistry
Auto-catalytic Cleavage of Clostridium difficile Toxins A and B Depends on Cysteine Protease Activity* - Journal of Biological Chemistry