N-terminal palmitoylation within the appropriate amino acid environment conveys on NOS2 the ability to progress along the intracellular sorting pathways
about
Molecular Basis for the Protein Recognition Specificity of the Dynein Light Chain DYNLT1/Tctex1: CHARACTERIZATION OF THE INTERACTION WITH ACTIVIN RECEPTOR IIB.Insights into the C-terminal Peptide Binding Specificity of the PDZ Domain of Neuronal Nitric-oxide Synthase: CHARACTERIZATION OF THE INTERACTION WITH THE TIGHT JUNCTION PROTEIN CLAUDIN-3.DYNLT (Tctex-1) forms a tripartite complex with dynein intermediate chain and RagA, hence linking this small GTPase to the dynein motor.Binding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesis.Prediction of palmitoylation sites using the composition of k-spaced amino acid pairs.Protein kinase D activity controls endothelial nitric oxide synthesis.
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N-terminal palmitoylation within the appropriate amino acid environment conveys on NOS2 the ability to progress along the intracellular sorting pathways
description
im März 2006 veröffentlichter wissenschaftlicher Artikel
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scientific article published on 28 March 2006
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wetenschappelijk artikel
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наукова стаття, опублікована в березні 2006
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name
N-terminal palmitoylation with ...... intracellular sorting pathways
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N-terminal palmitoylation with ...... intracellular sorting pathways
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type
label
N-terminal palmitoylation with ...... intracellular sorting pathways
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N-terminal palmitoylation with ...... intracellular sorting pathways
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prefLabel
N-terminal palmitoylation with ...... intracellular sorting pathways
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N-terminal palmitoylation with ...... intracellular sorting pathways
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P2860
P356
P1476
N-terminal palmitoylation with ...... intracellular sorting pathways
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Inmaculada Navarro-Lérida
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P304
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10.1242/JCS.02878
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P577
2006-03-28T00:00:00Z