Plasmodium falciparum histidine-rich protein II binds to actin, phosphatidylinositol 4,5-bisphosphate and erythrocyte ghosts in a pH-dependent manner and undergoes coil-to-helix transitions in anionic micelles.
about
Endophytic life strategies decoded by genome and transcriptome analyses of the mutualistic root symbiont Piriformospora indicaAn erythrocyte cytoskeleton-binding motif in exported Plasmodium falciparum proteinsThere is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeletonCooperative domains define a unique host cell-targeting signal in Plasmodium falciparum-infected erythrocytes.A General Synthetic Approach for Designing Epitope Targeted Macrocyclic Peptide LigandsProtein export from Plasmodium parasites.Heterologous expression of plasmodial proteins for structural studies and functional annotation.Plasmodium falciparum Histidine-Rich Protein II Compromises Brain Endothelial Barriers and May Promote Cerebral Malaria Pathogenesis.Potential biomarkers and their applications for rapid and reliable detection of malaria.Red blood cell membrane fluctuations and shape controlled by ATP-induced cytoskeletal defects.Global sequence variation in the histidine-rich proteins 2 and 3 of Plasmodium falciparum: implications for the performance of malaria rapid diagnostic tests.The Staphylococcus aureus extracellular matrix protein (Emp) has a fibrous structure and binds to different extracellular matrices.
P2860
Q21131407-AA46ACD8-678E-4694-AF69-A0578D444D27Q27973520-3F69178F-5FE4-462E-A214-E6890F73D06EQ28394155-549E3AF6-B6E3-4F44-88F4-85FFBF850A45Q30481036-1A6B0151-3920-468B-A893-F60822073F75Q35777956-0E6121BE-49E5-42A3-8AE5-DBFC663FAF6DQ36708385-824F755C-DFAC-4ACA-A6DD-0D114CD2F27FQ36938795-0C6D384E-537C-43E4-9E12-66F203691EFBQ37123466-ECED8AC3-5575-4B21-97F5-EEB4C76641C1Q37718844-D253BC57-8EA7-465E-A01C-24417D3E6DD6Q40320266-37DEEB60-E793-4486-B5AC-AE5E8CDD6571Q41504973-114063AA-5AD3-4D7A-A06B-C0FA54B02DDFQ42653081-4AD2F448-7613-48FC-82FA-345C92429ED5
P2860
Plasmodium falciparum histidine-rich protein II binds to actin, phosphatidylinositol 4,5-bisphosphate and erythrocyte ghosts in a pH-dependent manner and undergoes coil-to-helix transitions in anionic micelles.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@en
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@nl
type
label
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@en
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@nl
prefLabel
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@en
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@nl
P2093
P1476
Plasmodium falciparum histidin ...... ansitions in anionic micelles.
@en
P2093
Alberto Spisni
Jörg Kobarg
Osmar Norberto de Souza
Reynaldo Mascagni Gatti
Rogério Meneghini
Thelma Aguiar Pertinhez
P304
P356
10.1016/S0166-6851(03)00057-4
P577
2003-05-01T00:00:00Z