scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M112.409276 |
P953 | full work available at URL | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3481285 |
P932 | PMC publication ID | 3481285 |
P698 | PubMed publication ID | 22989878 |
P50 | author | Niraj H Tolia | Q55175593 |
P2093 | author name string | Daniel H Lin | |
Joseph D Batchelor | |||
Brian M Malpede | |||
P2860 | cites work | DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering | Q39388340 |
Differential antibody responses to Plasmodium falciparum invasion ligand proteins in individuals living in malaria-endemic areas in Brazil and Cameroon. | Q46298357 | ||
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A malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(alpha 2-3)Gal- sequences of glycophorin A | Q24643787 | ||
A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes | Q27230006 | ||
The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL. | Q27230097 | ||
Dimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARC | Q27670749 | ||
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Invasion of red blood cells by malaria parasites | Q29618806 | ||
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Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl) | Q30042536 | ||
A family of erythrocyte binding proteins of malaria parasites | Q33198214 | ||
Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations | Q34163026 | ||
A family affair: var genes, PfEMP1 binding, and malaria disease | Q34543611 | ||
Reticulocyte and erythrocyte binding-like proteins function cooperatively in invasion of human erythrocytes by malaria parasites | Q34739631 | ||
Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1 | Q37146848 | ||
Invasion profiles of Brazilian field isolates of Plasmodium falciparum: phenotypic and genotypic analyses | Q37524172 | ||
P433 | issue | 44 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | cell biology | Q7141 |
Plasmodium falciparum | Q311383 | ||
red blood cell | Q37187 | ||
erythrocyte binding antigen-140 | Q56582827 | ||
erythrocyte invasion | Q122665572 | ||
P304 | page(s) | 36830-6 | |
P577 | publication date | 2012-10-26 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Crystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte Invasion | |
P478 | volume | 287 |
Q37632441 | A quantitative assay for binding and inhibition of Plasmodium falciparum Erythrocyte Binding Antigen 175 reveals high affinity binding depends on both DBL domains |
Q36978206 | Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein |
Q34237880 | Critical glycosylated residues in exon three of erythrocyte glycophorin A engage Plasmodium falciparum EBA-175 and define receptor specificity. |
Q92993772 | Erythrocyte glycophorins as receptors for Plasmodium merozoites |
Q38650817 | Genetic evidence for erythrocyte receptor glycophorin B expression levels defining a dominant Plasmodium falciparum invasion pathway into human erythrocytes |
Q33701044 | Host-Parasite Interactions in Human Malaria: Clinical Implications of Basic Research |
Q37124750 | Inhibitory humoral responses to the Plasmodium falciparum vaccine candidate EBA-175 are independent of the erythrocyte invasion pathway |
Q37728315 | Malaria adhesins: structure and function |
Q37462647 | Malaria parasite CelTOS targets the inner leaflet of cell membranes for pore-dependent disruption |
Q47396685 | Mechanisms of naturally acquired immunity to P. falciparum and approaches to identify merozoite antigen targets |
Q27676877 | Molecular Basis for Sialic Acid-dependent Receptor Recognition by the Plasmodium falciparum Invasion Protein Erythrocyte-binding Antigen-140/BAEBL |
Q35190960 | Multimeric assembly of host-pathogen adhesion complexes involved in apicomplexan invasion |
Q30042563 | Plasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasion |
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Q21131367 | Red blood cell invasion by Plasmodium vivax: structural basis for DBP engagement of DARC |
Q38696399 | Red cell receptors as access points for malaria infection |
Q38180023 | Sequence variation and structural conservation allows development of novel function and immune evasion in parasite surface protein families |
Q60301624 | Shed EBA-175 mediates red blood cell clustering that enhances malaria parasite growth and enables immune evasion |
Q28544738 | Structural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine design |
Q27678372 | Structural and Functional Basis for Inhibition of Erythrocyte Invasion by Antibodies that Target Plasmodium falciparum EBA-175 |
Q92325722 | Structural basis for neutralization of Plasmodium vivax by naturally acquired human antibodies that target DBP |
Q34452432 | Structural conservation despite huge sequence diversity allows EPCR binding by the PfEMP1 family implicated in severe childhood malaria |
Q36723862 | Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand |
Q38375594 | The apicomplexan glideosome and adhesins - Structures and function |
Q35542746 | The baculovirus-expressed binding region of Plasmodium falciparum EBA-140 ligand and its glycophorin C binding specificity |
Q34606720 | The epitope of monoclonal antibodies blocking erythrocyte invasion by Plasmodium falciparum map to the dimerization and receptor glycan binding sites of EBA-175. |
Q38301947 | The structures of glycophorin C N-glycans, a putative component of the GPC receptor site for Plasmodium falciparum EBA-140 ligand |
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