Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells.
about
Bacterial Sphingomyelinases and Phospholipases as Virulence FactorsNutrient salvaging and metabolism by the intracellular pathogen Legionella pneumophilaCell biology of infection by Legionella pneumophilaVipD of Legionella pneumophila Targets Activated Rab5 and Rab22 to Interfere with Endosomal Trafficking in MacrophagesThe Legionella pneumophila IcmSW complex interacts with multiple Dot/Icm effectors to facilitate type IV translocationStructure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial PhagosomeBiological diversity of prokaryotic type IV secretion systems.Legionella eukaryotic-like type IV substrates interfere with organelle trafficking.LnaB: a Legionella pneumophila activator of NF-kappaB.Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector.Molecular pathogenesis of infections caused by Legionella pneumophilaComprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila.Functional characterization of a phospholipase A(2) homolog from Rickettsia typhi.Structural basis for the recruitment and activation of the Legionella phospholipase VipD by the host GTPase Rab5.The E Block motif is associated with Legionella pneumophila translocated substrates.Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress responseLarge-scale identification and translocation of type IV secretion substrates by Coxiella burnetii.Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesisRickettsia typhi possesses phospholipase A2 enzymes that are involved in infection of host cells.Ubiquitin activates patatin-like phospholipases from multiple bacterial speciesA novel phosphatidylinositol 4,5-bisphosphate binding domain mediates plasma membrane localization of ExoU and other patatin-like phospholipases.A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell deathMinimization of the Legionella pneumophila genome reveals chromosomal regions involved in host range expansion.The Legionella pneumophila effector SidJ is required for efficient recruitment of endoplasmic reticulum proteins to the bacterial phagosome.Which Way In? The RalF Arf-GEF Orchestrates Rickettsia Host Cell InvasionMultiple roles of phospholipase A2 during lung infection and inflammation.Legionella pneumophila EnhC is required for efficient replication in tumour necrosis factor alpha-stimulated macrophagesHost cell processes that influence the intracellular survival of Legionella pneumophila.SigmaS controls multiple pathways associated with intracellular multiplication of Legionella pneumophilaPhosphatidylcholine synthesis is required for optimal function of Legionella pneumophila virulence determinants.The Legionella pneumophila replication vacuole: making a cosy niche inside host cells.VipD is a Rab5-activated phospholipase A1 that protects Legionella pneumophila from endosomal fusion.The professional phagocyte Dictyostelium discoideum as a model host for bacterial pathogensManipulation of host vesicular trafficking and innate immune defence by Legionella Dot/Icm effectors.Formation of a pathogen vacuole according to Legionella pneumophila: how to kill one bird with many stones.Creating a customized intracellular niche: subversion of host cell signaling by Legionella type IV secretion system effectors.The Type II Secretion System of Legionella pneumophila Dampens the MyD88 and Toll-Like Receptor 2 Signaling Pathway in Infected Human Macrophages.Legionella and Coxiella effectors: strength in diversity and activity.Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways.The Legionella pneumophila Dot/Icm-secreted effector PlcC/CegC1 together with PlcA and PlcB promotes virulence and belongs to a novel zinc metallophospholipase C family present in bacteria and fungi.
P2860
Q26745804-41ED5CC9-8965-4231-9FDC-D03094404C4CQ26864957-07CADB04-0822-457D-AC7D-0D140191B50FQ27026901-4D6A4E20-24FA-4D29-BBD9-CCB80D25E045Q27675624-544566EA-2899-43B3-ABD5-70333A5DE1D4Q28471800-C7D73BB7-C123-4C61-8D0B-EDFD1CEC1A8EQ28548314-E80F9F02-E598-49E8-8317-1C4D3DAD1E93Q30927042-01AEA9D9-8CAA-49CD-BCFD-DCA7DE919A82Q33356625-3E363CDB-FC34-4E5D-8E99-13B360424DDFQ33530689-8B6EB01D-A609-4685-BADF-75A8031B587CQ33545239-4B9904B7-8C78-4FCB-909F-52C254E0B118Q33825611-10868549-E4F9-424B-AF1A-EC9381604D10Q33847063-C168427B-580A-4DEC-AD5A-CD70C05FC358Q33964188-0EBF7D53-102A-4440-AA12-BACAF3FC534CQ34120152-C5F9DDE4-8891-43E4-886E-FF4822276482Q34140790-68E60F59-FEE4-4CF2-BA8A-6C432A6D1974Q34257036-BF59EE13-FA6C-4C13-BB2F-4B44B53F81BEQ34411597-4E2FA100-5618-41BC-BD46-81A122B434C5Q34468990-885E8E14-046E-4377-946B-1901805B2B67Q34789261-FF073AB4-F56B-4ED2-87B3-49F9A10558E9Q34853536-8879E91C-ADA1-4247-870D-CED86C0A77CCQ35048920-126416F9-4C4D-4F0C-A249-B187FD81FA91Q35161315-3AC43131-CDCC-4E70-A65E-38617C690458Q35202685-5860E230-92EB-4F39-88D5-F0C6DD77F1C1Q35689306-25050631-8945-493C-B367-9F9F341ED0C7Q35751326-66F4437C-8766-4A43-A2A6-ADD76E897476Q36710691-AC97D067-D09B-47B5-A999-E584173DA47AQ36964166-202A82C1-8212-4121-B9B3-2539F50A3A75Q37118104-679AA42D-3141-4C4D-8ADF-CD8832375583Q37157034-76A0862A-3D90-4F5E-B954-47F0ECF4682AQ37237972-B36865E8-F808-4899-9CB4-495A29AEEFFFQ37326393-F0C4CD05-3F4B-459A-A60D-631AE9EE2618Q37674312-45F6B199-7A97-45CB-B7CB-CAD1AE549AC4Q37848852-9554716F-C285-41E5-B248-1F06708E13D7Q37943396-CD2923BC-768E-48BA-915A-737FD67B86D3Q38436575-B84461A6-F862-4895-A16A-DB42954B8645Q38522634-9E24FBD1-3C33-4F08-B46B-F58A7E125B94Q38718759-0871E1BB-8997-4EF2-8CAF-CB2CDFFAEBC5Q39437877-541583C3-BA9B-495D-95D7-E2E85BE6238EQ39915159-E6129775-1611-43CD-BA68-6F0CAEEA647FQ39959076-82151BED-4B45-44F6-96C6-A086A559F46C
P2860
Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Members of a Legionella pneumo ...... translocated to target cells.
@ast
Members of a Legionella pneumo ...... translocated to target cells.
@en
Members of a Legionella pneumophila family of proteins with ExoU
@nl
type
label
Members of a Legionella pneumo ...... translocated to target cells.
@ast
Members of a Legionella pneumo ...... translocated to target cells.
@en
Members of a Legionella pneumophila family of proteins with ExoU
@nl
prefLabel
Members of a Legionella pneumo ...... translocated to target cells.
@ast
Members of a Legionella pneumo ...... translocated to target cells.
@en
Members of a Legionella pneumophila family of proteins with ExoU
@nl
P2093
P2860
P356
P1476
Members of a Legionella pneumo ...... translocated to target cells.
@en
P2093
Ralph R Isberg
Susan M VanRheenen
Tamara O'Connor
Zhao-Qing Luo
P2860
P304
P356
10.1128/IAI.02060-05
P407
P577
2006-06-01T00:00:00Z