Nuclear import of LASP-1 is regulated by phosphorylation and dynamic protein-protein interactions
about
The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-κBRegulation of matrix metalloproteinases (MMPs) expression and secretion in MDA-MB-231 breast cancer cells by LIM and SH3 protein 1 (LASP1)LASP1, a Newly Identified Melanocytic Protein with a Possible Role in Melanin Release, but Not in Melanoma ProgressionLASP-1: a nuclear hub for the UHRF1-DNMT1-G9a-Snail1 complex.An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker proteinLoss of tumor suppressor mir-203 mediates overexpression of LIM and SH3 Protein 1 (LASP1) in high-risk prostate cancer thereby increasing cell proliferation and migration.LIM and SH3 domain protein 1 (LASP-1) overexpression was associated with aggressive phenotype and poor prognosis in clear cell renal cell cancer.LASP1 is a novel BCR-ABL substrate and a phosphorylation-dependent binding partner of CRKL in chronic myeloid leukemiaPodosomes in adhesion, migration, mechanosensing and matrix remodeling.Molecular characterization of LASP-1 expression reveals vimentin as its new partner in human hepatocellular carcinoma cells.Nuclear import of transcription factor BR-C is mediated by its interaction with RACK1.Integrative Phosphoproteomics Links IL-23R Signaling with Metabolic Adaptation in LymphocytesThe intracellular fate of zonula occludens 2 is regulated by the phosphorylation of SR repeats and the phosphorylation/O-GlcNAcylation of S257.Beyond cell-cell adhesion: Emerging roles of the tight junction scaffold ZO-2.Analyses of PDE-regulated phosphoproteomes reveal unique and specific cAMP-signaling modules in T cells.ZO-2, a tight junction protein involved in gene expression, proliferation, apoptosis, and cell size regulation.Paving the path for invasion: The polyedric role of LASP1 in cancer.SUMOylation regulates the intracellular fate of ZO-2.Lasp1 promotes malignant phenotype of non-small-cell lung cancer via inducing phosphorylation of FAK-AKT pathway.LIM and SH3 protein 1 knockdown suppresses proliferation and metastasis of colorectal carcinoma cells via inhibition of the mitogen-activated protein kinase signaling pathway.New Frontiers for the Cytoskeletal Protein LASP1
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P2860
Nuclear import of LASP-1 is regulated by phosphorylation and dynamic protein-protein interactions
description
2013 nî lūn-bûn
@nan
2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@ast
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en-gb
Nuclear import of LASP-1 is re ...... c protein-protein interactions
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type
label
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@ast
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en-gb
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@nl
prefLabel
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@ast
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en-gb
Nuclear import of LASP-1 is re ...... c protein-protein interactions
@nl
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Nuclear import of LASP-1 is re ...... c protein-protein interactions
@en
P2093
H J Pavenstädt
J Kremerskothen
P Thalheimer
S Gaetzner
S Herterich
U Lewandrowski
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P304
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P356
10.1038/ONC.2012.216
P407
P577
2012-06-04T00:00:00Z
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P6179
1009955406