Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum - Wikidata - wikimedia - TriplyDB

Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

http://www.wikidata.org/entity/Q24297064

about

The cellular and molecular basis for malaria parasite invasion of the human red blood cell Novel approaches to identify protective malaria vaccine candidates Dangerous liaisons: molecular basis for a syndemic relationship between Kaposi's sarcoma and P. falciparum malaria Plasmodium falciparum erythrocyte invasion: combining function with immune evasion Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies Production of full-length soluble Plasmodium falciparum RH5 protein vaccine using a Drosophila melanogaster Schneider 2 stable cell line system Merozoite surface proteins in red blood cell invasion, immunity and vaccines against malaria Basigin (CD147), a multifunctional transmembrane glycoprotein with various binding partners Fundamentals of protein interaction network mapping The mechanics of malaria parasite invasion of the human erythrocyte - towards a reassessment of the host cell contribution Anti-infective immunoadhesins from plants.The influence of host genetics on erythrocytes and malaria infection: is there therapeutic potential?Malaria and human red blood cells Lactate transport and signaling in the brain: potential therapeutic targets and roles in body-brain interaction Paths to a malaria vaccine illuminated by parasite genomics The role of EMMPRIN in T cell biology and immunological diseases Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans Revealing the sequence and resulting cellular morphology of receptor-ligand interactions during Plasmodium falciparum invasion of erythrocytes Using mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor.Young lives lost as B cells falter: what we are learning about antibody responses in malaria.Antibodies to PfSEA-1 block parasite egress from RBCs and protect against malaria infection Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3-MSP1 complex Semaphorin-7A is an erythrocyte receptor for P. falciparum merozoite-specific TRAP homolog, MTRAP Biochemical analysis of the Plasmodium falciparum erythrocyte-binding antigen-175 (EBA175)-glycophorin-A interaction: implications for vaccine design Multiple pathways for Plasmodium ookinete invasion of the mosquito midgut Binding of Plasmodium falciparum Merozoite Surface Proteins DBLMSP and DBLMSP2 to Human Immunoglobulin M Is Conserved among Broadly Diverged Sequence Variants Recent advances in malaria genomics and epigenomics Malaria Parasites: The Great Escape Malaria vaccine clinical trials: what's on the horizon Biochemical and functional analysis of two Plasmodium falciparum blood-stage 6-cys proteins: P12 and P41 Plasmodium malariae and P. ovale genomes provide insights into malaria parasite evolution Host reticulocytes provide metabolic reservoirs that can be exploited by malaria parasites Plasmodium vivax Reticulocyte Binding Proteins Are Key Targets of Naturally Acquired Immunity in Young Papua New Guinean Children Plasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasion P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5 P-selectin is a host receptor for Plasmodium MSP7 ligands Plasmodium falciparum erythrocyte-binding antigen 175 triggers a biophysical change in the red blood cell that facilitates invasion Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA RH5-Basigin interaction plays a major role in the host tropism of Plasmodium falciparum.

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P2860

Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

http://www.wikidata.org/entity/Q24297064

description

2011 nî lūn-bûn

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2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum

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Michel Theron

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Omar Ndir

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S Josefin Bartholdson

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P2860

Genome-wide detection and characterization of positive selection in human populations

Large-scale screening for novel low-affinity extracellular protein interactions

A map of human genome variation from population-scale sequencing

Genome-wide and fine-resolution association analysis of malaria in West Africa

Crystal structure of HAb18G/CD147: implications for immunoglobulin superfamily homophilic adhesion

The Oka blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues

Methodological challenges of genome-wide association analysis in Africa

Invasion of red blood cells by malaria parasites

Complement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand.

PfRH5: a novel reticulocyte-binding family homolog of plasmodium falciparum that binds to the erythrocyte, and an investigation of its receptor

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10.1038/NATURE10606

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Dominic P. Kwiatkowski

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2011-12-22T00:00:00Z

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