Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane.
about
The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sitesRab6 and Rab11 regulate Chlamydia trachomatis development and golgin-84-dependent Golgi fragmentationA chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actinThe Rab6 effector Bicaudal D1 associates with Chlamydia trachomatis inclusions in a biovar-specific mannerCaveolin-2 associates with intracellular chlamydial inclusions independently of caveolin-1Host Organelle Hijackers: a similar modus operandi for Toxoplasma gondii and Chlamydia trachomatis: co-infection model as a tool to investigate pathogenesisChlamydiae interaction with the endoplasmic reticulum: contact, function and consequencesInnate immune responses to Chlamydia pneumoniae infection: role of TLRs, NLRs, and the inflammasomePolarized Cell Division of Chlamydia trachomatisA C. trachomatis cloning vector and the generation of C. trachomatis strains expressing fluorescent proteins under the control of a C. trachomatis promoterAnaplasma phagocytophilum Rab10-dependent parasitism of the trans-Golgi network is critical for completion of the infection cycleDifferential Translocation of Host Cellular Materials into the Chlamydia trachomatis Inclusion Lumen during Chemical FixationChlamydia trachomatis intercepts Golgi-derived sphingolipids through a Rab14-mediated transport required for bacterial development and replicationA cell-based screen reveals that the albendazole metabolite, albendazole sulfone, targets WolbachiaPhosphorylation of Golgi Peripheral Membrane Protein Grasp65 Is an Integral Step in the Formation of the Human Cytomegalovirus Cytoplasmic Assembly CompartmentChlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular developmentContrasting Lifestyles Within the Host CellRottlerin-mediated inhibition of Chlamydia trachomatis growth and uptake of sphingolipids is independent of p38-regulated/activated protein kinase (PRAK)Bioinformatic and biochemical evidence for the identification of the type III secretion system needle protein of Chlamydia trachomatisIntegrating chemical mutagenesis and whole-genome sequencing as a platform for forward and reverse genetic analysis of Chlamydia.Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin.The SPI-2 type III secretion system restricts motility of Salmonella-containing vacuoles.Cytoplasmic lipid droplets are translocated into the lumen of the Chlamydia trachomatis parasitophorous vacuole.Kinematics of intracellular chlamydiae provide evidence for contact-dependent developmentA novel co-infection model with Toxoplasma and Chlamydia trachomatis highlights the importance of host cell manipulation for nutrient scavengingChlamydia trachomatis vacuole maturation in infected macrophagesUptake and intra-inclusion accumulation of exogenous immunoglobulin by Chlamydia-infected cells.Inclusion biogenesis and reactivation of persistent Chlamydia trachomatis requires host cell sphingolipid biosynthesisCharacterization of hypothetical proteins Cpn0146, 0147, 0284 & 0285 that are predicted to be in the Chlamydia pneumoniae inclusion membrane.RNAi screen in Drosophila cells reveals the involvement of the Tom complex in Chlamydia infection.Host chemokine and cytokine response in the endocervix within the first developmental cycle of Chlamydia muridarum.Amino acid transport into cultured McCoy cells infected with Chlamydia trachomatis.Chlamydia Hijacks ARF GTPases To Coordinate Microtubule Posttranslational Modifications and Golgi Complex PositioningManipulation of Host Cholesterol by Obligate Intracellular Bacteria.Lack of cell wall peptidoglycan versus penicillin sensitivity: new insights into the chlamydial anomaly.Fusion of Chlamydia trachomatis-containing inclusions is inhibited at low temperatures and requires bacterial protein synthesis.Brucella abortus transits through the autophagic pathway and replicates in the endoplasmic reticulum of nonprofessional phagocytes.The broad-spectrum antiviral compound ST-669 restricts chlamydial inclusion development and bacterial growth and localizes to host cell lipid droplets within treated cells.Bacterial subversion of the host secretory pathway.Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion.
P2860
Q21131416-7083BC56-4C5D-44F7-9C3F-C684EB73F172Q21131572-640377AB-F9D2-428C-B03A-CE851A694085Q24564460-F433990F-BF6C-4918-976F-BDC2880DE632Q24678714-F1EA5BDE-1EB7-426A-9E9B-18658DC6526EQ24795726-2D6577A6-D6C5-4C0A-9809-1F321B8CB388Q26825487-CA84A123-1237-4786-AB3C-EEB2B38B25D4Q27014662-F4188E90-CAEA-4A26-A400-9F472C931BA5Q27027451-FC7E9EF1-0157-4FC2-B99F-D36698C527EAQ27312247-93AC1509-479D-4A3D-A8BD-91622C4A245AQ27313656-0983E19B-CA94-40B7-AB33-E3CAEBF4D84DQ27313937-6C389671-D5CE-4B52-AE85-B7DE1E47F827Q27316181-725638CF-8203-4BB3-AE46-F59ABA2CD8D1Q27316389-37ED1C7B-8CE2-4DB2-9EC9-ADE75E1B331DQ27342384-7F8C292C-D4C3-4A69-BAE0-B8722C111ADAQ27343029-94AC2DE7-D1A4-4F8B-A93A-7BF505CCBD03Q27349136-A8A0A6B7-3AD9-41F0-88AD-ABCB2E3FFE67Q28078686-E6FE6116-1636-4AA0-8F6F-A780E7E9459FQ28483639-4CE5DCF5-FECB-4957-AC45-0DB0FD1C6C44Q28484742-FB31A86C-6EA8-41A9-8CA9-DBA2CB2EDA4DQ28791052-0CE95266-9826-4BAA-87E5-7D34B6A75823Q30452836-AD2D7653-DC3A-4BBB-A83D-2D5081C18AD0Q30480339-4EA84193-4659-45A1-AC7B-44623E185226Q30482674-1BCB9432-7968-441C-BF1A-81566496C7C5Q30489992-D12FBDF4-F44D-4B15-BFF6-D18717EDD17EQ30538838-F0F2B2CA-99DA-4B76-AAAE-3534A0496D57Q30580283-CBF4260F-5B13-48DA-B2A3-DAD8337949A5Q30854907-AAF474C0-D428-4164-989A-9792E328D903Q30912299-6BACC268-C40F-444C-B12D-F3D9AB166213Q33284727-BDC6270A-94EA-4953-98B8-575804F1BF3BQ33304217-7371A847-90F3-4ECC-82F6-C87364A4363EQ33557924-DE2A3382-602D-4F11-B028-B25DF0EC5A42Q33600559-17BA6D38-E7BC-4C2F-A8B8-834EA0A5024CQ33629138-0BC1E255-97BE-46B7-BC27-09372BD6A06DQ33639053-3BF3ED75-B939-4F8A-9CA9-76E0B2973917Q33744588-6E3AE050-5184-4BF3-884D-4C284DC0EFECQ33767745-1FF72160-D278-4020-8C21-CD80DBE30D9CQ33768425-58C568F9-7CCC-47AA-A291-A64CE567C11DQ33798572-C3E3B894-58C4-46AB-A4EB-A5882E63E2BDQ33819320-BE72BE6D-9428-4206-947C-6DE9F5A02B16Q33825984-655B48EB-FC83-41B1-83D6-F1B390D3299D
P2860
Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Chlamydia trachomatis interrup ...... aratus to the plasma membrane.
@en
Chlamydia trachomatis interrup ...... aratus to the plasma membrane.
@nl
type
label
Chlamydia trachomatis interrup ...... aratus to the plasma membrane.
@en
Chlamydia trachomatis interrup ...... aratus to the plasma membrane.
@nl
prefLabel
Chlamydia trachomatis interrup ...... aratus to the plasma membrane.
@en
Chlamydia trachomatis interrup ...... aratus to the plasma membrane.
@nl
P2093
P2860
P1433
P1476
Chlamydia trachomatis interrup ...... paratus to the plasma membrane
@en
P2093
Hackstadt T
Heinzen RA
Scidmore MA
P2860
P304
P356
10.1002/J.1460-2075.1996.TB00433.X
P407
P577
1996-03-01T00:00:00Z