Characterization of the lipid-binding domain of the Plasmodium falciparum CTP:phosphocholine cytidylyltransferase through synthetic-peptide studies.
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Molecular Mechanism for the Thermo-Sensitive Phenotype of CHO-MT58 Cell Line Harbouring a Mutant CTP:Phosphocholine CytidylyltransferaseA 22-mer segment in the structurally pliable regulatory domain of metazoan CTP: phosphocholine cytidylyltransferase facilitates both silencing and activating functions.Gelsolin binds to polyphosphoinositide-free lipid vesicles and simultaneously to actin microfilaments.Heterologous expression of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum rescues Chinese Hamster Ovary cells deficient in the Kennedy phosphatidylcholine biosynthesis pathway.
P2860
Characterization of the lipid-binding domain of the Plasmodium falciparum CTP:phosphocholine cytidylyltransferase through synthetic-peptide studies.
description
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name
Characterization of the lipid- ...... ugh synthetic-peptide studies.
@en
Characterization of the lipid- ...... ugh synthetic-peptide studies.
@nl
type
label
Characterization of the lipid- ...... ugh synthetic-peptide studies.
@en
Characterization of the lipid- ...... ugh synthetic-peptide studies.
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Characterization of the lipid- ...... ugh synthetic-peptide studies.
@en
Characterization of the lipid- ...... ugh synthetic-peptide studies.
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P2093
P2860
P356
P1433
P1476
Characterization of the lipid- ...... ough synthetic-peptide studies
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P2093
Catherine Gumila
Claude Roustan
Henri Vial
Luc Maurin
Marie-Pierre Larvor
Patrick Seta
P2860
P304
P356
10.1042/BJ20031011
P407
P577
2003-11-01T00:00:00Z