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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

SLIT-ROBO Rho GTPase activating protein 1

Top mentioned proteins: Rhodopsin, Cdc42, ACID, RhoGAP, CAN
Papers on SRGAP1
Recombinant Slit2 attenuates neuroinflammation after surgical brain injury by inhibiting peripheral immune cell infiltration via Robo1-srGAP1 pathway in a rat model.
Zhang et al., Loma Linda, United States. In Neurobiol Dis, Jan 2016
This study evaluated the effect of recombinant Slit2 and the role of its receptor roundabout1 (Robo1) and its downstream mediator Slit-Robo GTPase activating protein 1 (srGAP1)-Cdc42 on peripheral immune cell infiltration after SBI in a rat model.
Mutations of the SLIT2-ROBO2 pathway genes SLIT2 and SRGAP1 confer risk for congenital anomalies of the kidney and urinary tract.
Hildebrandt et al., Boston, United States. In Hum Genet, Aug 2015
We identified two heterozygous mutations in SRGAP1 in 2 unrelated families.
MicroRNA-145 Promotes the Phenotype of Human Glioblastoma Cells Selected for Invasion.
Toussaint et al., Bryan, United States. In Anticancer Res, Jun 2015
Herein, we investigated the correlation between miR-145 and srGAP1 (SLIT-ROBO Rho GTPase-activating protein1) that is purported to be a target of miR-145 and involved in migration and invasion.
Identification of a novel germline FOXE1 variant in patients with familial non-medullary thyroid carcinoma (FNMTC).
Cavaco et al., Lisbon, Portugal. In Endocrine, May 2015
Nine FNMTC susceptibility loci have been mapped; however, only the DICER1 and SRGAP1 susceptibility genes have been identified.
Rho GEFs and GAPs: emerging integrators of extracellular matrix signaling.
Yamada et al., In Small Gtpases, 2014
We discovered that the Rho GEF βPix has a unique function during cell migration in fibrillar collagen environments by restraining RhoA signaling through a conserved signaling axis involving Cdc42 and the Rho GAP srGAP1.
An extracellular-matrix-specific GEF-GAP interaction regulates Rho GTPase crosstalk for 3D collagen migration.
Yamada et al., Bethesda, United States. In Nat Cell Biol, 2014
Mechanistically, collagen phospho-regulates βPix, leading to its association with srGAP1, a GTPase-activating protein (GAP), needed to suppress RhoA activity.
Genome-wide association study identifies new susceptibility loci for epithelial ovarian cancer in Han Chinese women.
Wei et al., Tianjin, China. In Nat Commun, 2013
(rs1192691 near ANKRD30A, P(meta) = 2.62 × 10(-8)), and two consistently replicated loci at 12q14.2 (rs11175194 in SRGAP1, P(meta) = 1.14 × 10(-7)) and 9q34.2 (rs633862 near ABO and SURF6, P(meta) = 8.57 × 10(-7)) (P<0.05 in all three stages).
srGAP1 regulates lamellipodial dynamics and cell migratory behavior by modulating Rac1 activity.
Takenawa et al., Suita, Japan. In Mol Biol Cell, 2013
Here we show that Slit-Robo GAP 1 (srGAP1) is a modulator of Rac activity in locomotive cells.
SRGAP1 is a candidate gene for papillary thyroid carcinoma susceptibility.
de la Chapelle et al., Columbus, United States. In J Clin Endocrinol Metab, 2013
RESULTS: Linkage analysis and association studies identified the Slit-Robo Rho GTPase activating protein 1 gene (SRGAP1) in the linkage peak as a candidate gene.
The inverse F-BAR domain protein srGAP2 acts through srGAP3 to modulate neuronal differentiation and neurite outgrowth of mouse neuroblastoma cells.
Jin et al., Shanghai, China. In Plos One, 2012
The inverse F-BAR (IF-BAR) domain proteins srGAP1, srGAP2 and srGAP3 are implicated in neuronal development and may be linked to mental retardation, schizophrenia and seizure.
The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently.
Polleux et al., Chapel Hill, United States. In J Cell Sci, 2012
Here, we demonstrate that the F-BAR domains of two closely related family members, srGAP1 and srGAP3 [designated F-BAR(1) and F-BAR(3), respectively] display significantly different membrane deformation properties in non-neuronal COS7 cells and in cortical neurons.
Slit-Robo GTPase-activating proteins are differentially expressed in murine dorsal root ganglia: modulation by peripheral nerve injury.
Yi et al., Haikou, China. In Anat Rec (hoboken), 2012
srGAP1 and srGAP3 are largely expressed in subpopulations of dorsal root ganglion neurons following sciatic nerve lesion.
The corticofugal neuron-associated genes ROBO1, SRGAP1, and CTIP2 exhibit an anterior to posterior gradient of expression in early fetal human neocortex development.
Clowry et al., Newcastle upon Tyne, United Kingdom. In Cereb Cortex, 2011
This study proposed that the expression of SRGAP1 in the anterior neocortex may mark the early location of the human motor cortex, including its corticospinal projection neurons, allowing further study of their early differentiation.
Slit2 regulates attractive eosinophil and repulsive neutrophil chemotaxis through differential srGAP1 expression during lung inflammation.
Geng et al., Shanghai, China. In J Immunol, 2010
Compared to neutrophils, eosinophils exhibited a significantly lower level of Slit-Robo GTPase-activating protein 1 (srGAP1), leading to activation of Cdc42, recruitment of PI3K to Robo1, enhancment of eotaxin-induced eosinophil chemotaxis, and exaggeration of allergic airway inflammation.
Dynamic expression of the Slit-Robo GTPase activating protein genes during development of the murine nervous system.
Rappold et al., Heidelberg, Germany. In J Comp Neurol, 2009
Data show that srGAP3 is expressed in ventricular zones of neurogenesis in many different tissues of the central nervous system.
FNBP2 gene on human chromosome 1q32.1 encodes ARHGAP family protein with FCH, FBH, RhoGAP and SH3 domains.
Katoh et al., Narashino, Japan. In Int J Mol Med, 2003
FNBP2, ARHGAP13, ARHGAP14 and ARHGAP4 constitute the FNBP2 family characterized by FCH, RhoGAP and SH3 domains.
Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway.
Rao et al., Saint Louis, United States. In Cell, 2001
Slit increased srGAP1-Robo1 interaction and inactivated Cdc42.
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