Acidocalcisomes and a vacuolar H+-pyrophosphatase in malaria parasites
about
Evolution of vacuolar proton pyrophosphatase domains and volutin granules: clues into the early evolutionary origin of the acidocalcisomeHaemoproteus syrnii in Strix aluco from France: morphology, stages of sporogony in a hippoboscid fly, molecular characterization and discussion on the identification of Haemoproteus speciesAcidocalcisomes as calcium- and polyphosphate-storage compartments during embryogenesis of the insect Rhodnius prolixus StahlDeciphering the relationship among phosphate dynamics, electron-dense body and lipid accumulation in the green alga Parachlorella kessleriRole of calcium signaling in the transcriptional regulation of the apicoplast genome of Plasmodium falciparumNew insights into roles of acidocalcisomes and contractile vacuole complex in osmoregulation in protistsIdentification and characterization of an ecto-pyrophosphatase activity in intact epimastigotes of Trypanosoma rangeliThe diamidine DB75 targets the nucleus of Plasmodium falciparumThe role of acidocalcisomes in parasitic protists.Evolution of acidocalcisomes and their role in polyphosphate storage and osmoregulation in eukaryotic microbesUnlike the synchronous Plasmodium falciparum and P. chabaudi infection, the P. berghei and P. yoelii asynchronous infections are not affected by melatonin.A vacuolar-H(+) -pyrophosphatase (TgVP1) is required for microneme secretion, host cell invasion, and extracellular survival of Toxoplasma gondiiAcidocalcisomes - conserved from bacteria to man.Proteomic analysis of the acidocalcisome, an organelle conserved from bacteria to human cells.Plasmodium falciparum chloroquine resistance transporter is a H+-coupled polyspecific nutrient and drug exporter.Generation and Identification of Peptide-Based Monoclonal Antibodies Against Vacuolar Proton Pyrophosphatase of Toxoplasma gondii.Extracellular ATP triggers proteolysis and cytosolic Ca²⁺ rise in Plasmodium berghei and Plasmodium yoelii malaria parasites.Volutin granules of Eimeria parasites are acidic compartments and have physiological and structural characteristics similar to acidocalcisomesCalcium signaling in a low calcium environment: how the intracellular malaria parasite solves the problem.Ca(2+) monitoring in Plasmodium falciparum using the yellow cameleon-Nano biosensor.Protein trafficking inside Toxoplasma gondii.Molecular machinery of signal transduction and cell cycle regulation in PlasmodiumImmunolocalization and challenge studies using a recombinant Vibrio cholerae ghost expressing Trypanosoma brucei Ca(2+) ATPase (TBCA2) antigen.Insights into the mechanism of membrane pyrophosphatases by combining experiment and computer simulation.Membrane transport in the malaria parasite and its host erythrocyte.A yeast expression system for functional and pharmacological studies of the malaria parasite Ca²⁺/H⁺ antiporter.Human CD1 dimeric proteins as indispensable tools for research on CD1-binding lipids and CD1-restricted T cells.Polyphosphate content and fine structure of acidocalcisomes of Plasmodium falciparum.NAADP induces pH changes in the lumen of acidic Ca2+ stores.Vacuolar proton pyrophosphatase activity and pyrophosphate (PPi) in Toxoplasma gondii as possible chemotherapeutic targetsCyclic AMP and calcium interplay as second messengers in melatonin-dependent regulation of Plasmodium falciparum cell cycle.In vivo uptake of a haem analogue Zn protoporphyrin IX by the human malaria parasite P. falciparum-infected red blood cells.The polyphosphate bodies of Chlamydomonas reinhardtii possess a proton-pumping pyrophosphatase and are similar to acidocalcisomes.Acidocalcisomes are functionally linked to the contractile vacuole of Dictyostelium discoideum.Presence of a plant-like proton-translocating pyrophosphatase in a scuticociliate parasite and its role as a possible drug target.Quantitative calcium measurements in subcellular compartments of Plasmodium falciparum-infected erythrocytes.Products of tryptophan catabolism induce Ca2+ release and modulate the cell cycle of Plasmodium falciparum malaria parasites.Human malarial parasite, Plasmodium falciparum, displays capacitative calcium entry: 2-aminoethyl diphenylborinate blocks the signal transduction pathway of melatonin action on the P. falciparum cell cycle.Acidification of the malaria parasite's digestive vacuole by a H+-ATPase and a H+-pyrophosphatase.
P2860
Q21203752-0DAC3C8A-2195-4768-A527-268C26DD86AEQ24624271-2B62A180-4521-40A2-BAD2-B0A78B217215Q27313446-5A6FF2C6-DC41-4906-B1E4-447D3353AE08Q27316246-8BB05ECF-392C-41A7-9576-791FB2397819Q27974339-CD499E53-3B2C-4896-85C5-7EA6692AD767Q28295380-EC4E443A-13BE-42F3-AF9A-8E6A1B7461DBQ28542885-6EA04484-7A7F-40B6-BDA3-E1F2B29EBBCAQ30487931-AC0D1472-AF9C-40F0-A37C-3085324CD3C2Q33573949-9F184C6D-C4C6-4E31-9385-7A578B466F5DQ33632851-7AAFB000-BBE6-4EBE-9CCD-AAF6D037681EQ33735095-D97B9524-7B9D-4820-BD51-3E7A12F81E69Q34157987-BAAAEE32-88C4-4C82-ACDC-EF4B36C30882Q34398973-EB0162CC-5E80-4FE7-8955-0CD9D643629FQ34682192-76258656-5607-4AE9-8D17-C1DE755C10C3Q35212623-BDF7B8E5-990F-477C-BE44-906B2389BD38Q35822193-0C33DFD2-63E1-40AB-AF1B-05A0673B05AAQ35980267-BE64496A-1B2D-46C0-A0E1-F4A2BE32FF80Q36237611-EF3EF693-8006-4091-AEA7-7C898424C57FQ36323422-D9B37443-F5EB-493D-945C-CAD6D4E87F92Q36719348-AA1BDA36-A03F-4B6E-A98D-3E58AB829B85Q37106600-038FD6A0-D325-4B07-91CD-3658C5543C19Q37235092-8330773B-3B2D-47BF-8D81-2C37F953CDB6Q37450423-1983D911-0C6C-4178-8593-BF35A4FD6CB8Q37679967-576B88FB-88FC-4398-994B-B09527379D2DQ38170172-960FA488-892C-4B63-8E5F-B5E40AE7BB86Q39424138-004D87DA-3F12-4287-8E41-D6C9A66B4282Q39859712-D94711EB-9527-44B6-84A3-7129990D2640Q41913211-E5C1337B-B054-440A-B624-60FFC9586222Q42076235-A3BAFCF4-E2F0-459D-860D-9C012D0DAC44Q42238346-EBEDA376-295C-4DF2-BEF4-22FC08539923Q42914575-78895B9B-6985-4559-9335-DC105155DCC6Q43057331-0C5ED797-E85E-419F-96BB-63B750E43612Q43752265-9DB12E55-3DF2-4413-A8D0-B7CD5C2B59A0Q43826805-470EA32F-581D-4C4E-809A-B755EF4DE7AAQ44860400-86CDD857-1158-4063-AC21-E0D41D0443D9Q46520708-18981FE6-F6EB-4C83-8EB8-3A1622887DA9Q46692851-AF6A8489-7AF4-40F6-9DA4-B3F0C526D320Q46970996-FF651753-7221-45DB-B814-09D5C5515991Q47917641-58D38B67-14A7-45A2-850B-2790E864775C
P2860
Acidocalcisomes and a vacuolar H+-pyrophosphatase in malaria parasites
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Acidocalcisomes and a vacuolar H+-pyrophosphatase in malaria parasites
@en
type
label
Acidocalcisomes and a vacuolar H+-pyrophosphatase in malaria parasites
@en
prefLabel
Acidocalcisomes and a vacuolar H+-pyrophosphatase in malaria parasites
@en
P2093
P2860
P1433
P1476
Acidocalcisomes and a vacuolar H+-pyrophosphatase in malaria parasites
@en
P2093
P2860
P304
P356
10.1042/0264-6021:3470243
P407
P478
P577
2000-04-01T00:00:00Z