A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion
about
Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasitesComparative Plasmodium gene overexpression reveals distinct perturbation of sporozoite transmission by profilin.Spatial localisation of actin filaments across developmental stages of the malaria parasiteConcerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondiiA cyclic GMP signalling module that regulates gliding motility in a malaria parasiteStructural differences explain diverse functions of Plasmodium actinsStructure and Function of a G-actin Sequestering Protein with a Vital Role in Malaria Oocyst Development inside the Mosquito VectorStructure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNAPlasmodium falciparum dynein light chain 1 interacts with actin/myosin during blood stage developmentA tetracycline-repressible transactivator system to study essential genes in malaria parasitesOrigins and evolution of the formin multigene family that is involved in the formation of actin filamentsThe lasso segment is required for functional dimerization of the Plasmodium formin 1 FH2 domainPlasmodium falciparum coronin organizes arrays of parallel actin filaments potentially guiding directional motility in invasive malaria parasitesPaternal effect of the nuclear formin-like protein MISFIT on Plasmodium development in the mosquito vectorVital role for the Plasmodium actin capping protein (CP) beta-subunit in motility of malaria sporozoitesToxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.Malaria parasite actin polymerization and filament structureActin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondiiToxoplasma gondii myosin F, an essential motor for centrosomes positioning and apicoplast inheritance.An aspartyl protease directs malaria effector proteins to the host cell.Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.How apicomplexan parasites move in and out of cells.Host cell invasion by apicomplexan parasites: the junction conundrumMolecular characterization of Toxoplasma gondii formin 3, an actin nucleator dispensable for tachyzoite growth and motility.Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro.Erythrocyte-binding antigens of Plasmodium falciparum are targets of human inhibitory antibodies and function to evade naturally acquired immunity.Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparumFamily members stick together: multi-protein complexes of malaria parasites.The moving junction of apicomplexan parasites: a key structure for invasion.Holding back the microfilament--structural insights into actin and the actin-monomer-binding proteins of apicomplexan parasites.The apicomplexan glideosome and adhesins - Structures and function.Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Plasma IgG autoantibody against actin-related protein 3 in liver fluke Opisthorchis viverrini infection.The actin-based machinery of Trichomonas vaginalis mediates flagellate-amoeboid transition and migration across host tissue.Geometric constrains for detecting short actin filaments by cryogenic electron tomography.Gliding motility powers invasion and egress in Apicomplexa.Positive diversifying selection on Plasmodium vivax RON2 protein.Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism.Stage-specific depletion of myosin A supports an essential role in motility of malarial ookinetes.
P2860
Q56561498-441538FF-E5F0-4E6E-8C2F-C177B1DC9282Q56579218-AF960632-7961-46C1-BEE0-DA39F50BA82FQ56735836-162BD2C7-D395-4ABF-8204-00EF35423942Q59760481-0C1AF028-5E6E-4703-813D-0E882AF37D3AQ59893247-E607B031-3BEE-4C19-9B96-14E73260C09EQ59919635-5E2BEF2E-FF08-43E8-B092-1FD10858BDA8Q59923343-B6899800-A92A-4B0E-AA02-4C36C91CFD81Q59974348-5ADF6762-8416-4050-84CE-9E4DA66D77ABQ59993456-8268DDFE-C382-4C00-80E0-26072DEB6AD3Q60005076-C0944E5D-5FB5-4B50-B152-74A6557670A1Q60005883-5F3F72A4-F2AB-4077-BDC0-875F52711C06Q60006141-4C31B5BD-D6F5-4FCB-BCF5-3D48FD910230Q60013145-36543403-2E8F-49A6-82D4-020BB27F3E6CQ60018091-B43DD6AE-0606-4623-ADD1-C0459D25FA2FQ61621725-85F2A72B-111B-4F0E-AB79-EFD45598A6B8
P1343
Q21559403-B8B2A387-2B7D-4EAB-A27C-06628289FF5CQ27304918-C6B10FC4-7040-461B-B50E-6232E347D2D2Q27308691-10667148-3ECC-431B-9730-D1062EEF90ADQ27313299-1CD7753F-60DE-4016-9A0F-C240CF79DA3CQ27316208-8258B5C8-F465-4476-8D0C-DED75CAB2ED1Q27327176-FDD3A761-6C95-483F-9387-8DC5D2D5FD35Q27659030-EEE7F7F9-C0A4-41F3-B233-CB337ED7BCA6Q27664562-BBCA9629-80C6-4CDF-A83C-4D5F84CF2826Q27677137-8051F004-598B-41F4-978B-659C2623AD9EQ27972565-6A3C521C-58CD-460E-8920-17B40E37E816Q27972939-F55C71AB-57B0-47F8-9A03-F23BB62AC1D3Q28296265-765DD22D-8C92-4652-93AB-FA736F64BEA6Q28731339-759C1974-38F9-4EBD-BC44-4E3CBC39F98DQ30046205-27575AB4-C90D-4B56-9FC6-55544C99F3CCQ30046670-ADA559A2-7824-4BEC-BAE9-5E0A1E9CD4E2Q30048444-D27428EF-3634-4DEE-B4A5-1243B45C5BFEQ30493280-14880AA7-65C1-479E-BC1C-95782B9E7E5EQ30497350-01144A63-E336-4155-B7D5-17C370F6C112Q30499678-EC069418-7686-48C9-B8D1-505D0A18572AQ30540599-6C8880AE-77D7-47E8-AAA3-8536F3B10013Q33639304-555DF614-3270-4D18-8A5A-01CEBD5F433BQ33653471-BE8F8A70-9106-470B-BF38-2D88EE23ECC4Q34122826-37790F90-51B2-4C17-9E91-54E71F5047EFQ35260670-C0ACD8EC-EA0F-4001-AE59-93C053835117Q35804698-F0F6012C-F838-4A89-BC66-8DC29C95AF81Q35871134-A2874B09-35EE-4FB7-9355-E28BF11D3E22Q37202344-575822EE-1A5D-48EE-9D12-835CABE4F3D1Q37414548-68AFDDB5-2DF6-48E8-B139-A964E9E76F02Q37737126-25B00721-2295-407D-8455-03401C2C7B66Q37871026-464B098F-D1B3-40F1-943A-5ABE09C14074Q37997736-E11E148B-CB2D-4185-994C-D10B7A167B7BQ38375594-6B7612B4-E8AA-481F-8A21-77EDECC5E849Q38461991-C5D97FA6-56C2-4E91-A618-8668487080B7Q38895133-0295452A-9EB3-4253-B9D1-FB3D4FA8A188Q39175377-6C4D88C0-7FBB-4AFA-BEDF-5B1895F5F6B9Q39766742-97440352-ED6B-4B85-AB0A-314DDC616F88Q40068658-FA391590-AEF8-4FCC-B5A3-AE5209197388Q42635681-CDCC448A-555B-4C58-B681-F00651D671E4Q42703528-E5117759-0718-46A6-A837-CF325CF4DC6FQ44160058-BBDB35AE-185A-4715-8178-DC29091963F8
P2860
A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion
description
2008 nî lūn-bûn
@nan
2008 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մարտին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A malaria parasite formin regu ...... oving junction during invasion
@ast
A malaria parasite formin regu ...... oving junction during invasion
@en
A malaria parasite formin regu ...... oving junction during invasion
@nl
type
label
A malaria parasite formin regu ...... oving junction during invasion
@ast
A malaria parasite formin regu ...... oving junction during invasion
@en
A malaria parasite formin regu ...... oving junction during invasion
@nl
prefLabel
A malaria parasite formin regu ...... oving junction during invasion
@ast
A malaria parasite formin regu ...... oving junction during invasion
@en
A malaria parasite formin regu ...... oving junction during invasion
@nl
P2093
P50
P921
P3181
P1433
P1476
A malaria parasite formin regu ...... oving junction during invasion
@en
P2093
Aditya S Paul
Christopher J Tonkin
Dave Richard
Melanie Rug
P304
P3181
P356
10.1016/J.CHOM.2008.02.006
P407
P577
2008-03-13T00:00:00Z