LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
about
Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organizationEpstein-Barr virus latent genesEpstein-barr virus latent membrane protein 2B (LMP2B) modulates LMP2A activity.Cholesterol is critical for Epstein-Barr virus latent membrane protein 2A trafficking and protein stabilityViral modulation of T-cell receptor signalingRecycling of MUC1 is dependent on its palmitoylation.
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LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on October 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
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LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
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type
label
LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
@en
LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
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prefLabel
LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
@en
LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
@nl
P2860
P1433
P1476
LMP2A does not require palmitoylation to localize to buoyant complexes or for function.
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P2093
Rebecca B Katzman
Richard Longnecker
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P304
10878-10887
P356
10.1128/JVI.78.20.10878-10887.2004
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P577
2004-10-01T00:00:00Z