Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. - Wikidata - awgldk - TriplyDB

Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins.

Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins.

http://www.wikidata.org/entity/Q41898316

about

Subversion of Cell-Autonomous Immunity and Cell Migration by Legionella pneumophila Effectors Bacterial pathogens commandeer Rab GTPases to establish intracellular niches Activation of Ran GTPase by a Legionella effector promotes microtubule polymerization, pathogen vacuole motility and infection Catalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detail Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain Structural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidD The Legionella pneumophila GTPase Activating Protein LepB Accelerates Rab1 Deactivation by a Non-canonical Hydrolytic Mechanism Innate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogen The machinery at endoplasmic reticulum-plasma membrane contact sites contributes to spatial regulation of multiple Legionella effector proteins.Identification of novel Coxiella burnetii Icm/Dot effectors and genetic analysis of their involvement in modulating a mitogen-activated protein kinase pathway.Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: an expanded role for Inc proteins.Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesis Post-translational modifications are key players of the Legionella pneumophila infection strategy Toxicity and SidJ-Mediated Suppression of Toxicity Require Distinct Regions in the SidE Family of Legionella pneumophila Effectors Endoplasmic Reticulum Tubule Protein Reticulon 4 Associates with the Legionella pneumophila Vacuole and with Translocated Substrate Ceg9.Beyond Rab GTPases Legionella activates the small GTPase Ran to promote microtubule polymerization, pathogen vacuole motility, and infection Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.Membrane extraction of Rab proteins by GDP dissociation inhibitor characterized using attenuated total reflection infrared spectroscopy Type II Secretion Is Necessary for Optimal Association of the Legionella-Containing Vacuole with Macrophage Rab1B but Enhances Intracellular Replication Mainly by Rab1B-Independent Mechanisms.Spatiotemporal imaging of small GTPases activity in live cells How Bacteria Subvert Animal Cell Structure and Function.AMPylation is critical for Rab1 localization to vacuoles containing Legionella pneumophila.The role of Rab GTPases in the transport of vacuoles containing Legionella pneumophila and Coxiella burnetii.Microbial modulation of host immunity with the small molecule phosphorylcholine.What pathogens have taught us about posttranslational modifications.Exploring adenylylation and phosphocholination as post-translational modifications.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.Structure and function of Fic proteins.Bacterial glycosyltransferase toxins.Rab35 GTPase: A Central Regulator of Phosphoinositides and F-actin in Endocytic Recycling and Beyond.Icm/Dot-dependent inhibition of phagocyte migration by Legionella is antagonized by a translocated Ran GTPase activator.Molecular control of Rab activity by GEFs, GAPs and GDI.Post translational modifications of Rab GTPases.Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.A Novel Fic (Filamentation Induced by cAMP) Protein from Clostridium difficile Reveals an Inhibitory Motif-independent Adenylylation/AMPylation Mechanism.Legionella Effector AnkX Disrupts Host Cell Endocytic Recycling in a Phosphocholination-Dependent Manner.Locking GTPases covalently in their functional states.Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein.

P2860

Q26781334-9C079481-55FC-4335-8372-89229631C6FC Q27026776-6DBFF3FC-385B-4D93-B16E-8D872EE2AA76 Q27333488-9EB57495-EEF5-4A23-8EC5-AC19F5A60796 Q27675470-3ECB2246-25FE-4B2A-8426-8027AD4910B8 Q27675735-0FCB35FC-AC79-442A-A1F3-A762052ADB67 Q27677280-A43E6FDD-5016-45D6-8D1B-3BCA4145B868 Q27678253-458EE3C0-0CDD-497A-8233-AF87C97F5510 Q27678890-7D295F66-2BCD-44B0-ABE4-4BADA15EAAB9 Q28829229-1188D8D1-845F-4807-B8FA-82DBF531728A Q33846189-20DAA1BB-975E-4F79-BC2A-20AB82B8D30B Q34298317-FFE49499-2B80-4AEC-84B5-797D5F7851DE Q34433420-748F6005-6F90-481D-B295-D1F5A13FD1CE Q34468990-835DE65F-510A-4EA9-A459-E0DB90756271 Q35067041-CCC12B61-6046-414D-8DDA-71A1B090AC2A Q35671101-3CE09901-A29B-4D80-93CD-34AD3A4C6283 Q35947390-27DA06F4-6C7F-47AF-8330-1123933EF977 Q36147452-31919505-66F8-4001-89F5-37484A9D755F Q36563109-72895F0B-F060-49AA-B6EB-FBD146829EB8 Q37104002-667EAB8E-83B2-4873-9BAE-8B4849004A13 Q37424957-FF243BB4-16A6-4A7A-80DF-BA14CD0853A6 Q37514902-57E4803A-1867-4277-81B3-3F5DC69C4B5F Q37527203-10BC243A-7709-4365-95BE-42A18EF6A73E Q37631519-EBE48334-8DFF-40A9-BB92-922F28B91FB0 Q38061988-346E97E1-8B57-4359-A352-13FFC0E64A1B Q38066467-7B5B5FFA-C464-4BFF-8A9F-9092643C0032 Q38137411-34DC78AE-35FF-47A0-9F2C-0D84A22344D5 Q38156707-0046D724-7221-40F8-A408-1603A9E7F394 Q38436575-5CFAFC2C-24DC-41C7-89A2-19F1EEE5F79C Q38522634-A5911313-FFA7-4329-B1CE-D2B80A13C424 Q38572149-3E52B246-6516-4E74-A24A-B706D9BB360B Q38601591-932DD9A8-83A6-462A-8B18-DBA728A7A572 Q38872611-3719A021-B9A4-482A-BE57-AB6013B35B79 Q39036824-907BDD74-959A-46D3-AE58-005D7A241E91 Q39068332-BE6C65A1-0058-4E6B-872D-9B563259108B Q39252084-8C41FC7C-3A74-4412-A59E-55CD136333EC Q39385959-3E378C4F-74AB-4E9B-9EEF-7D70D454C2C3 Q40715444-E882CE48-DC5F-4CC9-AD97-F5A5314B4EED Q41699480-75FD74D4-22F7-46F9-BB3A-8E8CC3600E92 Q41817034-A2F99A79-8ABD-46BA-88CD-5D2333435691 Q42058621-FB6E514C-A4A6-45E3-A9A1-4A63B76B7E9E

P2860

Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins.

http://www.wikidata.org/entity/Q41898316

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Reversible phosphocholination ...... pneumophila effector proteins.

@en

type

label

Reversible phosphocholination ...... pneumophila effector proteins.

@en

prefLabel

Reversible phosphocholination ...... pneumophila effector proteins.

@en

P1433

Q41898316-83B9266E-211D-4799-AEC1-9F6FC42EFCF5

P1476

Q41898316-589E3622-BF59-4D32-8F77-E58313AB393D

P2093

Q41898316-097F31EE-31ED-4987-881E-8D5AB43A0CD2

Q41898316-0E5D4A2C-1785-4E8E-A42E-92B917E88E30

Q41898316-387F49BA-7C4D-4744-B508-1F1518D40496

P2860

Q41898316-0709409F-590E-47B0-BDF3-FEC9D6D58FFB

Q41898316-0ADCF90E-92D6-44B3-B74D-1291F2705CB4

Q41898316-1BC843A9-D1F8-4DD3-BB52-3F7FA7DBE5FC

Q41898316-24CEC5D3-C2AF-4956-A88E-56BC8620EB44

Q41898316-37A33321-ABA7-4018-BED9-13EE950B072D

Q41898316-3AF2152D-42FA-4C21-ACF5-7C33A4513B90

Q41898316-3E416469-A540-47FB-875A-68E30FDC002D

Q41898316-46FD6D4E-51C4-46F0-B7A9-B1B262E63C70

Q41898316-500840ED-AB75-4BB2-949D-68B4A78197D3

Q41898316-538F28E8-B739-4784-B5F7-C57079DD730E

P304

Q41898316-94EC28B4-9D57-4D67-BAB9-856FCC0B8A3E

P31

Q41898316-C3C52326-CB07-4720-A4F2-7DBDC1F2FDA9

P356

Q41898316-9D996C50-DDF5-47ED-AD4D-2A71B3D96D74

P407

Q41898316-B748FC76-B6D6-4A01-917D-9308DE825297

P433

Q41898316-331C5ADB-28E5-452B-AE08-84BD75AD4CB7

P478

Q41898316-B766E42D-E52B-4259-A191-9A8C4E814F6B

P50

Q41898316-0A260E2D-11DF-40B0-90C2-0C27BFD5D9E8

Q41898316-7072948A-A015-424E-9EF7-D8BD5D64998E

Q41898316-A21EA12D-280E-4DDF-81EB-1F84A9E985E5

P577

Q41898316-1F88D1A6-661D-4116-ADE2-7F1A5DF2A090

P5875

Q41898316-B871EEBA-A29F-401D-ACEA-C7B3578A4B79

P698

Q41898316-1D417DD5-28F3-4C06-8203-90BC4BBBA846

P932

Q41898316-2E20FC76-A654-43BB-9CF2-1B8EF7D45281

P356

P1433

The EMBO Journal

P1476

Reversible phosphocholination ...... pneumophila effector proteins.

@en

P2093

Katharina Heller

http://www.w3.org/2001/XMLSchema#string

Lena K Oesterlin

http://www.w3.org/2001/XMLSchema#string

Philip R Goody

http://www.w3.org/2001/XMLSchema#string

P2860

The fic domain: regulation of cell signaling by adenylylation

AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling

Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors

Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity

The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b

Protein LidA from Legionella is a Rab GTPase supereffector

Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination

De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila

Modulation of Rab GTPase function by a protein phosphocholine transferase

P304

1774-1784

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/EMBOJ.2012.16

http://www.w3.org/2001/XMLSchema#string

P407

P433

7

http://www.w3.org/2001/XMLSchema#string

P478

31

http://www.w3.org/2001/XMLSchema#string

P50

Matthias P Müller

P577

2012-02-03T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

221807647

http://www.w3.org/2001/XMLSchema#string

P698

22307087

http://www.w3.org/2001/XMLSchema#string

P932

3321196

http://www.w3.org/2001/XMLSchema#string