Search details
1.
An atlas of human vector-borne microbe interactions reveals pathogenicity mechanisms.
Cell
; 2024 Jun 11.
Article
in English
| MEDLINE | ID: mdl-38876107
2.
Selenomonas sputigena Interactions with Gingival Epithelial Cells That Promote Inflammation.
Infect Immun
; 91(2): e0031922, 2023 02 16.
Article
in English
| MEDLINE | ID: mdl-36648232
3.
Orientia tsutsugamushi OtDUB Is Expressed and Interacts with Adaptor Protein Complexes during Infection.
Infect Immun
; 90(12): e0046922, 2022 12 15.
Article
in English
| MEDLINE | ID: mdl-36374099
4.
Functional Characterization of Non-Ankyrin Repeat Domains of Orientia tsutsugamushi Ank Effectors Reveals Their Importance for Molecular Pathogenesis.
Infect Immun
; 90(5): e0062821, 2022 05 19.
Article
in English
| MEDLINE | ID: mdl-35435726
5.
Immunization against Anaplasma phagocytophilum Adhesin Binding Domains Confers Protection against Infection in the Mouse Model.
Infect Immun
; 88(10)2020 09 18.
Article
in English
| MEDLINE | ID: mdl-32661123
6.
Orientia tsutsugamushi uses two Ank effectors to modulate NF-κB p65 nuclear transport and inhibit NF-κB transcriptional activation.
PLoS Pathog
; 14(5): e1007023, 2018 05.
Article
in English
| MEDLINE | ID: mdl-29734393
7.
The Obligate Intracellular Bacterium Orientia tsutsugamushi Targets NLRC5 To Modulate the Major Histocompatibility Complex Class I Pathway.
Infect Immun
; 87(3)2019 03.
Article
in English
| MEDLINE | ID: mdl-30559222
8.
Orientia tsutsugamushi Modulates Endoplasmic Reticulum-Associated Degradation To Benefit Its Growth.
Infect Immun
; 86(1)2018 01.
Article
in English
| MEDLINE | ID: mdl-29109174
9.
The Prostaglandin E2-EP3 Receptor Axis Regulates Anaplasma phagocytophilum-Mediated NLRC4 Inflammasome Activation.
PLoS Pathog
; 12(8): e1005803, 2016 08.
Article
in English
| MEDLINE | ID: mdl-27482714
10.
Orientia tsutsugamushi Ank9 is a multifunctional effector that utilizes a novel GRIP-like Golgi localization domain for Golgi-to-endoplasmic reticulum trafficking and interacts with host COPB2.
Cell Microbiol
; 19(7)2017 07.
Article
in English
| MEDLINE | ID: mdl-28103630
11.
Anaplasma marginale Outer Membrane Protein A Is an Adhesin That Recognizes Sialylated and Fucosylated Glycans and Functionally Depends on an Essential Binding Domain.
Infect Immun
; 85(3)2017 03.
Article
in English
| MEDLINE | ID: mdl-27993973
12.
Intracellular Uropathogenic E. coli Exploits Host Rab35 for Iron Acquisition and Survival within Urinary Bladder Cells.
PLoS Pathog
; 11(8): e1005083, 2015 Aug.
Article
in English
| MEDLINE | ID: mdl-26248231
13.
Essential domains of Anaplasma phagocytophilum invasins utilized to infect mammalian host cells.
PLoS Pathog
; 11(2): e1004669, 2015 Feb.
Article
in English
| MEDLINE | ID: mdl-25658707
14.
Anaplasma phagocytophilum Rab10-dependent parasitism of the trans-Golgi network is critical for completion of the infection cycle.
Cell Microbiol
; 18(2): 260-81, 2016 Feb.
Article
in English
| MEDLINE | ID: mdl-26289115
15.
Chimeric Coupling Proteins Mediate Transfer of Heterologous Type IV Effectors through the Escherichia coli pKM101-Encoded Conjugation Machine.
J Bacteriol
; 198(19): 2701-18, 2016 10 01.
Article
in English
| MEDLINE | ID: mdl-27432829
16.
The Anaplasma phagocytophilum effector AmpA hijacks host cell SUMOylation.
Cell Microbiol
; 17(4): 504-19, 2015 Apr.
Article
in English
| MEDLINE | ID: mdl-25308709
17.
Orientia tsutsugamushi Strain Ikeda Ankyrin Repeat-Containing Proteins Recruit SCF1 Ubiquitin Ligase Machinery via Poxvirus-Like F-Box Motifs.
J Bacteriol
; 197(19): 3097-109, 2015 Oct.
Article
in English
| MEDLINE | ID: mdl-26170417
18.
Anaplasma phagocytophilum surface protein AipA mediates invasion of mammalian host cells.
Cell Microbiol
; 16(8): 1133-45, 2014 Aug.
Article
in English
| MEDLINE | ID: mdl-24612118
19.
Ceramide-1-phosphate is a regulator of Golgi structure and is co-opted by the obligate intracellular bacterial pathogen Anaplasma phagocytophilum.
mBio
; 15(4): e0029924, 2024 Apr 10.
Article
in English
| MEDLINE | ID: mdl-38415594
20.
Anaplasma phagocytophilum Asp14 is an invasin that interacts with mammalian host cells via its C terminus to facilitate infection.
Infect Immun
; 81(1): 65-79, 2013 Jan.
Article
in English
| MEDLINE | ID: mdl-23071137