The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery - Test2 - elhamkhani - TriplyDB

The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

http://www.wikidata.org/entity/Q24657476

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Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5 Regulation of the Plasmodium Motor Complex: PHOSPHORYLATION OF MYOSIN A TAIL-INTERACTING PROTEIN (MTIP) LOOSENS ITS GRIP ON MyoA Structural characterization and inhibition of the Plasmodium Atg8–Atg3 interaction Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain Evolution and architecture of the inner membrane complex in asexual and sexual stages of the malaria parasite A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity Identification of T. gondii myosin light chain-1 as a direct target of TachypleginA-2, a small-molecule inhibitor of parasite motility and invasion The bactofilin cytoskeleton protein BacM of Myxococcus xanthus forms an extended β-sheet structure likely mediated by hydrophobic interactions Plasmodium falciparum coronin organizes arrays of parallel actin filaments potentially guiding directional motility in invasive malaria parasites Myosin B of Plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP.Calcium-dependent phosphorylation alters class XIVa myosin function in the protozoan parasite Toxoplasma gondii A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex Structure-based design of novel small-molecule inhibitors of Plasmodium falciparum.Rapid discovery of inhibitors of Toxoplasma gondii using hybrid structure-based computational approach.How apicomplexan parasites move in and out of cells.The motor complex of Plasmodium falciparum: phosphorylation by a calcium-dependent protein kinase Myosin light chains: Teaching old dogs new tricks The compact conformation of the Plasmodium knowlesi myosin tail interacting protein MTIP in complex with the C-terminal helix of myosin A.From crystal to compound: structure-based antimalarial drug discovery.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?Gliding motility powers invasion and egress in Apicomplexa.Targeting a dynamic protein-protein interaction: fragment screening against the malaria myosin A motor complex.Development of a multifunctional tool for drug screening against plasmodial protein-protein interactions via surface plasmon resonance.Unusual anchor of a motor complex (MyoD-MLC2) to the plasma membrane of Toxoplasma gondii.Reconstitution of the core of the malaria parasite glideosome with recombinant Plasmodium class XIV myosin A and Plasmodium actin.

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P2860

The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

http://www.wikidata.org/entity/Q24657476

description

2007 nî lūn-bûn

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2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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type

label

The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The Closed MTIP-Myosin A-Tail Complex from the Malaria Parasite Invasion Machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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J.JMB.2007.06.016

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Journal of Molecular Biology

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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

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Claudia M Roach

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

Jürgen Bosch

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

Lawrence W Bergman

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

Stewart Turley

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

Thomas M Daly

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

Wim G J Hol

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

P2860

Three myosin V structures delineate essential features of chemo-mechanical transduction

The global distribution of clinical episodes of Plasmodium falciparum malaria

Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite

Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.

Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications

A structural state of the myosin V motor without bound nucleotide

Crystal structure of scallop Myosin s1 in the pre-power stroke state to 2.6 a resolution: flexibility and function in the head

From The Cover: Automated protein crystal structure determination using ELVES

Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features

Structure of the regulatory domain of scallop myosin at 2.8 A resolution

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