Expression and characterisation of plasmepsin I from Plasmodium falciparum.
about
P1343
Recombinant Plasmepsin 1 from the Human Malaria Parasite Plasmodium falciparum : Enzymatic Characterization, Active Site Inhibitor Design, and Structural AnalysisCrystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparumStructural Insights into the Activation and Inhibition of Histo-Aspartic Protease from Plasmodium falciparumEvidence for a Central Role for PfCRT in Conferring Plasmodium falciparum Resistance to Diverse Antimalarial AgentsDisulfide linkages in Plasmodium falciparum plasmepsin-i are essential elements for its processing activity and multi-milligram recombinant production yieldEnzymatic Characterization of Recombinant Food Vacuole Plasmepsin 4 from the Rodent Malaria Parasite Plasmodium bergheiFour plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine.Active site contribution to specificity of the aspartic proteases plasmepsins I and II.Antimalarial synergy of cysteine and aspartic protease inhibitors.Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursorsComputational perspectives into plasmepsins structure-function relationship: implications to inhibitors design.New class of small nonpeptidyl compounds blocks Plasmodium falciparum development in vitro by inhibiting plasmepsinsStructural studies of vacuolar plasmepsinsAntimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin.Inhibitory effects of pepstatin A and mefloquine on the growth of Babesia parasitesMolecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani.Proteases of malaria parasites: new targets for chemotherapy.The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum.Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum.A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum.New directions for protease inhibitors directed drug discovery.Heme binding contributes to antimalarial activity of bis-quaternary ammoniums.Exploring the subsite specificity of Schistosoma mansoni aspartyl hemoglobinase through comparative molecular modelling.Central role of hemoglobin degradation in mechanisms of action of 4-aminoquinolines, quinoline methanols, and phenanthrene methanols.Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors.Cellular uptake of chloroquine is dependent on binding to ferriprotoporphyrin IX and is independent of NHE activity in Plasmodium falciparumA common mechanism for blockade of heme polymerization by antimalarial quinolines.Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum.Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte.
P2860
Q27654043-20B314E2-B4B5-410F-9FA6-EEC3558B2B07Q27667575-7F961623-7B94-4BA3-96AB-88222F7C142DQ27674185-7307414D-893D-4364-99AB-E9CAFADC7DB1Q27861958-C707C5AD-455D-45C3-ABAD-D0E4190925FEQ28540029-D179A2C6-AD41-4F05-BEBA-63890DC09FB9Q28550537-D2CB2549-4CB7-4D85-93B5-1EE6E42103FCQ30042887-28547E53-087A-41CD-9039-DBF3670261F9Q33184160-9DD92BBA-4202-467E-84E3-15CB6CA4A03AQ33696222-B5C8F0AB-DDBD-4BE0-837B-9FD2419AEA92Q33740132-8750596B-F6D4-4C9B-8680-A6300B20CA24Q33961367-970B54AC-1927-45F4-A7E5-ED1F7ED0E0ADQ33982942-1C700393-D366-4429-87B3-B49A2B831FC5Q35159276-6BBB167B-963E-4CE4-AD12-EE82AEC2FE85Q35660425-8A1244C9-7CAA-40C1-BCB7-3264724E6AB5Q36450822-A226B79E-822A-43B5-B6C8-94D7CB8331EEQ36868301-555ABA1D-1198-4ACE-A5AA-0C455A95E538Q37064248-D599D747-EA14-4294-AFEF-B59656929F23Q38526967-F958E312-1272-49BC-8EBD-2F1476E42AFAQ38527649-102ACDD2-02DE-4E81-B4C9-FD51C1E7AB95Q38527989-DEE249A3-2BB6-4566-93F4-C1DBF33B4C88Q38638651-8392FE18-9216-4692-B406-5F90E32DEBD7Q38908351-B2B47C43-B103-4A88-9A54-A7B7B08C5B1BQ39462950-65CDE07A-F0CE-4C26-929B-8DFFC54E5F6EQ39559476-5B51236D-7E16-4E07-962A-FAAA5D6DA9FCQ39947285-2E28599D-E338-4C8B-9161-4DAA30C15C7EQ41819350-C010A0E9-1F40-4913-B672-F76D3D6AFF13Q41925197-470A34AA-A577-409D-ABAF-E760BBFBE14AQ43923777-969FFD6E-4A66-45E5-8906-D4DCD400152DQ44511093-ECEB1C61-4942-4BC3-9295-F9AC5DD9C0DE
P2860
Expression and characterisation of plasmepsin I from Plasmodium falciparum.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Expression and characterisation of plasmepsin I from Plasmodium falciparum.
@en
type
label
Expression and characterisation of plasmepsin I from Plasmodium falciparum.
@en
prefLabel
Expression and characterisation of plasmepsin I from Plasmodium falciparum.
@en
P2093
P2860
P921
P1433
P1476
Expression and characterisation of plasmepsin I from Plasmodium falciparum.
@en
P2093
F Grueninger-Leitch
H Loetscher
P2860
P304
P356
10.1111/J.1432-1033.1997.00552.X
P407
P577
1997-03-01T00:00:00Z