Characterization of membrane proteins exported from Plasmodium falciparum into the host erythrocyte.
about
A newly discovered protein export machine in malaria parasitesBiosynthesis, localization, and macromolecular arrangement of the Plasmodium falciparum translocon of exported proteins (PTEX)The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growthProteomic analysis identifies novel proteins of the Maurer's clefts, a secretory compartment delivering Plasmodium falciparum proteins to the surface of its host cellInvolvement of Plasmodium falciparum protein kinase CK2 in the chromatin assembly pathwayHost cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytesMAHRP-1, a novel Plasmodium falciparum histidine-rich protein, binds ferriprotoporphyrin IX and localizes to the Maurer's cleftsComplete Plasmodium falciparum liver-stage development in liver-chimeric mice.The Plasmodium berghei translocon of exported proteins reveals spatiotemporal dynamics of tubular extensions.Protein and lipid trafficking induced in erythrocytes infected by malaria parasites.Characterization of Plasmodium vivax Early Transcribed Membrane Protein 11.2 and Exported Protein 1Contrasting Inducible Knockdown of the Auxiliary PTEX Component PTEX88 in P. falciparum and P. berghei Unmasks a Role in Parasite Virulence.Antimalarial activities of dermaseptin S4 derivatives.Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes.The apicomplexan parasite Babesia divergens internalizes band 3, glycophorin A and spectrin during invasion of human red blood cells.Exploitation of a newly-identified entry pathway into the malaria parasite-infected erythrocyte to inhibit parasite egress.Blocking effect of a biotinylated protease inhibitor on the egress of Plasmodium falciparum merozoites from infected red blood cells.Cationic detergents enable the separation of membrane proteins of Plasmodium falciparum-infected erythrocytes by 2D gel electrophoresis.EXP2 is a nutrient-permeable channel in the vacuolar membrane of Plasmodium and is essential for protein export via PTEX
P2860
Q24653443-80604E96-6A1F-4250-9801-2A2B8D17F016Q27972588-C6CA7095-9737-416E-B0E8-62D24A49BC79Q27973421-AD337872-3D3F-43C3-9CE3-4B0FB81166CCQ27973506-AA6F9FBE-DD4C-419E-BCA0-6418259C38C0Q27973592-9D8F335C-C072-4695-A907-FA9D9DBB77ADQ28072465-6008D872-5E6C-4433-9B5E-CA7D4BC20BFFQ30042160-F7989012-F558-4693-96B8-5D850D3103A6Q30525395-4667EA40-71C6-445E-A77B-367A5A2C5CCFQ30659332-DAB71E51-CE4E-4792-8156-A6B5A3463C9AQ34725818-AF9689B1-C1C6-4229-83CE-CE903CEEA91DQ35642087-96FA1A56-E2FE-48E4-8D9C-C18DFBD10AC8Q35926127-5B1617E9-8405-4FFB-9A35-66FDD02667FBQ39474943-2B513458-FC29-455A-BB15-7FC08DAE58F5Q40539958-05B2E91C-C6A0-4A60-80D9-A5C9891CF95AQ41518116-75172079-1DB8-4823-B062-07C1C96DAFE8Q41994264-638E320C-5FF3-4817-BDC0-41F675CC0EDAQ46520625-FE6FB30A-A3CE-4BA3-89F0-6FE968973063Q48008146-4AC815DB-2324-4708-BA3D-89C4C4F350B6Q56305756-6098E379-1FF8-4BB6-BE5F-42032D51EC1E
P2860
Characterization of membrane proteins exported from Plasmodium falciparum into the host erythrocyte.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Characterization of membrane p ...... rum into the host erythrocyte.
@en
Characterization of membrane p ...... rum into the host erythrocyte.
@nl
type
label
Characterization of membrane p ...... rum into the host erythrocyte.
@en
Characterization of membrane p ...... rum into the host erythrocyte.
@nl
prefLabel
Characterization of membrane p ...... rum into the host erythrocyte.
@en
Characterization of membrane p ...... rum into the host erythrocyte.
@nl
P2093
P2860
P1433
P1476
Characterization of membrane p ...... rum into the host erythrocyte.
@en
P2093
Bannister L
Lingelbach K
P2860
P356
10.1017/S0031182000077696
P478
109 ( Pt 1)
P577
1994-07-01T00:00:00Z