Henry Thomas | Researchain

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Featured researches published by Henry Thomas.

PLOS Pathogens | 2016

IglG is secreted in a T6SS-dependent manner and is required for secretion of the Hcp homologue, IglC.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

The four cysteines conserved in PAAR-like proteins are required for IglG secretion and function.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

IglG is a metal-binding PAAR-like protein.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

IglG is required for SCHU S4 virulence in vivo but is dispensable for in vitro replication and cytopathogenicity.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

The first 39 residues of the N-terminal extension of IglG are dispensable for IglG secretion but required for IglG function in virulence.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

The conserved cysteines and the first 39 residues of the N-terminal extension of IglG are required for IglG function in LVS.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

A subset of PAAR-like proteins is extended by T6SS effector domains.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

IglG interacts with IglF in an N-terminal extension (AA 1–39)-dependent manner.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

IglG, a DUF4280-containing protein, is a structural homologue of PAAR proteins with four conserved cysteines potentially implicated in metal ion binding.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

PLOS Pathogens | 2016

Putative model for the Francisella T6SS.

Rigard Mélanie; E. Bröms Jeanette; Mosnier Amandine; Hologne Maggy; Martin Amandine; Lindgren Lena; Punginelli Claire; Lays Claire; Walker Olivier; Charbit Alain; Telouk Philippe; Conlan Wayne; Terradot Laurent; Sjöstedt Anders; Henry Thomas

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Archive Network Publication Hotspot Collaboration

Network

Latest external collaboration on country level. Dive into details by clicking on the dots.

Hotspot

Dive into the research topics where Henry Thomas is active.

Publication

Featured researches published by Henry Thomas.

IglG is secreted in a T6SS-dependent manner and is required for secretion of the Hcp homologue, IglC.

The four cysteines conserved in PAAR-like proteins are required for IglG secretion and function.

IglG is a metal-binding PAAR-like protein.

IglG is required for SCHU S4 virulence in vivo but is dispensable for in vitro replication and cytopathogenicity.

The first 39 residues of the N-terminal extension of IglG are dispensable for IglG secretion but required for IglG function in virulence.

The conserved cysteines and the first 39 residues of the N-terminal extension of IglG are required for IglG function in LVS.

A subset of PAAR-like proteins is extended by T6SS effector domains.

IglG interacts with IglF in an N-terminal extension (AA 1–39)-dependent manner.

IglG, a DUF4280-containing protein, is a structural homologue of PAAR proteins with four conserved cysteines potentially implicated in metal ion binding.

Putative model for the Francisella T6SS.

Collaboration

Dive into the Henry Thomas's collaboration.