Myristoylation and membrane binding regulate c-Src stability and kinase activity
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Role of N-Terminal Myristylation in the Structure and Regulation of cAMP-Dependent Protein KinaseDesign and Synthesis of High Affinity Inhibitors of Plasmodium falciparum and Plasmodium vivax N -Myristoyltransferases Directed by Ligand Efficiency Dependent Lipophilicity (LELP)Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.Intramolecular dynamics within the N-Cap-SH3-SH2 regulatory unit of the c-Abl tyrosine kinase reveal targeting to the cellular membranec-Src links a RANK/αvβ3 integrin complex to the osteoclast cytoskeleton.The regulation of N-methyl-D-aspartate receptors by Src kinase.Role of Src kinases in mobilization of glycosylphosphatidylinositol-anchored decay-accelerating factor by Dr fimbria-positive adhering bacteria.Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Fatty acylation of proteins: The long and the short of it.Expression of a phosphorylated substrate domain of p130Cas promotes PyMT-induced c-Src-dependent murine breast cancer progression.Myristoylation exerts direct and allosteric effects on Gα conformation and dynamics in solution.Targeting protein lipidation in diseaseEffects of HIV-1 Nef on human N-myristoyltransferase 1.A dominant gain-of-function mutation in universal tyrosine kinase SRC causes thrombocytopenia, myelofibrosis, bleeding, and bone pathologies.Activation of c-Src: a hub for exogenous pro-oxidant-mediated activation of Toll-like receptor 4 signalingC-Src and c-Yes are two unlikely partners of spermatogenesis and their roles in blood-testis barrier dynamics.Allosteric inhibition enhances the efficacy of ABL kinase inhibitors to target unmutated BCR-ABL and BCR-ABL-T315IAn N-myristoylated globin with a redox-sensing function that regulates the defecation cycle in Caenorhabditis elegans.Structural requirements for cub domain containing protein 1 (CDCP1) and Src dependent cell transformationDifferential transformation capacity of Src family kinases during the initiation of prostate cancer.Modulation of tumor fatty acids, through overexpression or loss of thyroid hormone responsive protein spot 14 is associated with altered growth and metastasis.Activation pathway of Src kinase reveals intermediate states as targets for drug designSaturated fatty acids induce c-Src clustering within membrane subdomains, leading to JNK activation.EGFR inhibition evokes innate drug resistance in lung cancer cells by preventing Akt activity and thus inactivating Ets-1 functionNMT1 (N-myristoyltransferase 1).Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA.A truncated fragment of Src protein kinase generated by calpain-mediated cleavage is a mediator of neuronal death in excitotoxicityGPS-Lipid: a robust tool for the prediction of multiple lipid modification sites.The residue at position 5 of the N-terminal region of Src and Fyn modulates their myristoylation, palmitoylation, and membrane interactions.Activation of oncogenic tyrosine kinase signaling promotes insulin receptor-mediated cone photoreceptor survival.Src signaling pathways in prostate cancer.MUC1-mediated motility in breast cancer: a review highlighting the role of the MUC1/ICAM-1/Src signaling triad.Functions of intrinsic disorder in transmembrane proteins.N-Myristoyltransferase Inhibition Induces ER-Stress, Cell Cycle Arrest, and Apoptosis in Cancer Cells.EGFR-activated Src family kinases maintain GAB1-SHP2 complexes distal from EGFR.Molecular requirements for T cell recognition of N-myristoylated peptides derived from the simian immunodeficiency virus Nef protein.Computational study of the W260A activating mutant of Src tyrosine kinase.Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling.Long-lived states in an intrinsically disordered protein domain.A myristoyl/phosphoserine switch controls cAMP-dependent protein kinase association to membranes.
P2860
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P2860
Myristoylation and membrane binding regulate c-Src stability and kinase activity
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@ast
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@en
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@nl
type
label
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@ast
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@en
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@nl
prefLabel
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@ast
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@en
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@nl
P2860
P356
P1476
Myristoylation and membrane binding regulate c-Src stability and kinase activity
@en
P2093
Marilyn D Resh
Parag Patwardhan
P2860
P304
P356
10.1128/MCB.00246-10
P407
P577
2010-06-28T00:00:00Z