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N-terminal processing of proteins exported by malaria parasites

N-terminal processing of proteins exported by malaria parasites

http://www.wikidata.org/entity/Q28282814

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Functional analysis of Hyaloperonospora arabidopsidis RXLR effectors Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte Structure of the Plasmodium falciparum circumsporozoite protein, a leading malaria vaccine candidate A newly discovered protein export machine in malaria parasites Plasmodium falciparum Secretome in Erythrocyte and Beyond Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface Plasmodium Rab5b is secreted to the cytoplasmic face of the tubovesicular network in infected red blood cells together with N-acylated adenylate kinase 2.The exported protein PbCP1 localises to cleft-like structures in the rodent malaria parasite Plasmodium berghei Picomolar Inhibition of Plasmepsin V, an Essential Malaria Protease, Achieved Exploiting the Prime Region Structure of a Plasmodium falciparum PfEMP1 rosetting domain reveals a role for the N-terminal segment in heparin-mediated rosette inhibition Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytes Trafficking of the exported P. falciparum chaperone PfHsp70x The Plasmodium falciparum exportome contains non-canonical PEXEL/HT proteins A conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytes New Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC Inhibition of Plasmepsin V activity demonstrates its essential role in protein export, PfEMP1 display, and survival of malaria parasites Plasmodium falciparum transfected with ultra bright NanoLuc luciferase offers high sensitivity detection for the screening of growth and cellular trafficking inhibitors The biological functions of Naa10 - From amino-terminal acetylation to human disease Identification of a Plasmodium falciparum phospholipid transfer protein Functional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytes Protein export marks the early phase of gametocytogenesis of the human malaria parasite Plasmodium falciparum The longin domain regulates the steady-state dynamics of Sec22 in Plasmodium falciparum Identification of a role for the PfEMP1 semi-conserved head structure in protein trafficking to the surface of Plasmodium falciparum infected red blood cells.The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.Revisiting the Plasmodium falciparum RIFIN family: from comparative genomics to 3D-model prediction.Functional evaluation of Plasmodium export signals in Plasmodium berghei suggests multiple modes of protein export An aspartyl protease directs malaria effector proteins to the host cell.Plasmodium falciparum erythrocyte membrane protein 1 diversity in seven genomes--divide and conquer.The host targeting motif in exported Plasmodium proteins is cleaved in the parasite endoplasmic reticulum.Phylogenomic analyses of malaria parasites and evolution of their exported proteins Profile of Michael A. Marletta.Maurer's clefts, the enigma of Plasmodium falciparum.Forward targeting of Toxoplasma gondii proproteins to the micronemes involves conserved aliphatic amino acids.Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin V Host-targeting protein 1 (SpHtp1) from the oomycete Saprolegnia parasitica translocates specifically into fish cells in a tyrosine-O-sulphate-dependent manner.Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding.An aspartyl protease defines a novel pathway for export of Toxoplasma proteins into the host cell.Proteomic analysis of Plasmodium falciparum parasites from patients with cerebral and uncomplicated malaria

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N-terminal processing of proteins exported by malaria parasites

http://www.wikidata.org/entity/Q28282814

description

2008 nî lūn-bûn

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2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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type

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N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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N-terminal processing of proteins exported by malaria parasites

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J.MOLBIOPARA.2008.04.011

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Molecular and Biochemical Parasitology

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N-terminal processing of proteins exported by malaria parasites

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Arnold M Falick

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

Henry H Chang

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John W Sedat

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

Joseph L DeRisi

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Michael A Marletta

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Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma

Crystal structure of the Aequorea victoria green fluorescent protein

The molecular structure of green fluorescent protein

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

Molecules on the surface of the Plasmodium falciparum infected erythrocyte and their role in malaria pathogenesis and immune evasion

Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites.

Human malaria parasites in continuous culture

Synchronization of Plasmodium falciparum erythrocytic stages in culture

The pathogenic basis of malaria

Patterns of amino acids near signal-sequence cleavage sites

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10.1016/J.MOLBIOPARA.2008.04.011

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2

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Peter Mark Carlton

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