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In turn, LIMK1 and LIMK2 (show LIMK2 Proteins) are required for MT1-MMP (show MMP14 Proteins)-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
increased BMPR2 (show BMPR2 Proteins) signal transduction is linked to fragile X (show FMR1 Proteins) syndrome (FXS) and that the BMPR2 (show BMPR2 Proteins)-LIMK1 pathway is a putative therapeutic target in patients with FXS and possibly other forms of autism
Report structural basis for noncanonical substrate recognition of cofilin-1/LIMK1 to regulation actin cytoskeleton dynamics.
LIMK1 expression is negatively regulated in granular layers-negative psoriatic epidermis or IL-22 (show IL22 Proteins)/IL-24 (show IL24 Proteins)-treated hyperproliferative reconstituted epidermis. These findings suggest a novel regulatory mechanism and a potent role of LIMK1 in psoriatic epidermis.
Therefore, miR (show MLXIP Proteins)-138/LIMK1/cofilin (show CFL1 Proteins) may be considered a potential therapeutic target for the treatment of non-small cell lung cancer
This study showed that LIMK1 messenger RNA levels was significantly upregulated in subjects with schizophrenia in laminar and cellular samples.
Gene knockdown/rescue experiments reveal that LIMK1 palmitoylation is essential for normal spine actin polymerization, for spine-specific structural plasticity and for long-term spine stability.
LIMK1 is overexpressed in endometrial stromal cells.
Data show that the downregulation of miR (show MLXIP Proteins)-138 induced the upregulation of Limk1 in ovarian cancer (OC) cells suggesting that these 2 genes may play a key role in the migration and invasion of OC cells.
LIMK1 is overexpressed in gastric cancer.
bone morphogenetic protein receptor II (BMPRII (show BMPR2 Proteins)) is a major regulator of LIMK1 in extending RGC axons, as expression of a BMPRII (show BMPR2 Proteins) lacking the LIMK1 binding region caused a dramatic shortening of the axons
High LIMK1 expression is associated with aberrant synaptic development in mouse and Drosophila models of Fragile X (show FMR1 Proteins) syndrome.
we define how ROCK/LIMK pathway regulates mast cell development and functions
LIMK1 negatively regulated neuronal migration by affecting the neuronal cytoskeleton and that its effects were partly mediated by cofilin (show CFL1 Proteins) phosphorylation
Social isolation resulted in up-regulation of Limk-1 mRNA expression in the cerebral cortex.
The data emphasize the importance of the PLCeta2 EF-hand domain and articulation of PLCeta2 with LIMK-1 in regulating neuritogenesis.
Our study indicates that there is a connection between LIMK1 and AD in the mouse model of AD.
Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization.
LIMK1 and Cofilin (show CFL1 Proteins) phosphorylation depends on PKA and is essential for mouse sperm acrosomal exocytosis
These results provide strong evidence that LIMK1 deletion is sufficient to lead to a long-term memory deficit and that this deficit is attributable to CREB (show CREB1 Proteins) hypofunction.
There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. This protein also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
LIM domain kinase 1
, LIM motif-containing protein kinase
, LIM motif-containing protein kinase 1
, LIM-domain containing protein kinase 1
, LIM-domain containing, protein kinase 1