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  • mutation
  • Coronary artery ectasia in Noonan syndrome: Report of an individual with SOS1 mutation and literature review. (nih.gov)
  • Germ line gain of function with SOS1 mutation in hereditary gingival fibromatosis. (nih.gov)
  • Martínez Planelló A, Sotillo M, Rodríguez-Santos F. Cognitive profile of a child with SOS1 mutation in Noonan syndrome. (nih.gov)
  • Mutations
  • The SOS1 gene mutations change single protein building blocks (amino acids) in the SOS1 protein. (nih.gov)
  • Mutations in the SOS1 gene can also cause hereditary gingival fibromatosis type 1. (nih.gov)
  • Here, we explored further the spectrum of SOS1 mutations and their associated phenotypic features.Two previously unappreciated clusters predicted to enhance SOS1's recruitment to the plasma membrane, thus promoting a spatial reorientation of domains contributing to inhibition, were also recognized.Genotype-phenotype analysis confirmed our previous observations, establishing a high frequency of ectodermal anomalies and a low prevalence of cognitive impairment and reduced growth. (nih.gov)
  • We and others recently reported that missense mutations in SOS1 (MIM♯ 182530) account for a significant proportion of NS [Roberts et al. (nih.gov)
  • The majority of NS-causing SOS1 mutations were observed to affect residues predicted to be implicated in the maintenance of SOS1 in its autoinhibited conformation, and the first biochemical characterizations of mutants consistently documented enhanced protein function and increased signal flow through RAS [Roberts et al. (nih.gov)
  • receptor
  • SOS1 is a large multidomain protein characterized by an N-terminal regulatory portion including tandem histone-like folds (HF), which are followed by a Dbl-homology (DH) domain and a pleckstrin-homology (PH) domain, and a C-terminal catalytic region including the RAS exchanger motif (REM) and CDC25 domains, followed by a tail providing docking sites for adaptor proteins required for receptor anchoring (Fig. 1). (nih.gov)
  • In this study, we describe a unique mechanism of mobilization and activation of RasGRP1 in response to SDF-1, a chemokine that signals via the G protein-coupled receptor CXCR4. (jimmunol.org)
  • CXCR4 is a chemokine receptor, a G protein-coupled receptor whose sole ligand is SDF-1, also called CXCL12. (jimmunol.org)
  • The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. (abnova.com)
  • Anabolic effects of a G protein-coupled receptor kinase inhibitor expressed in osteoblasts. (abnova.com)
  • The encoded protein may help couple the Fc receptor to the activation of the respiratory burst. (abnova.com)
  • A pseudogene of the mouse Grb2 homolog, known as Grb2-ps1 (growth factor receptor bound protein 2, pseudogene 1) also has been identified. (atlasgeneticsoncology.org)
  • vacuole
  • Two well-known plant cation/proton antiporters are NHX1 and SOS1, which perform Na + and K + compartmentalization into the vacuole and Na + efflux from the cell, respectively. (beds.ac.uk)
  • SOS1 facilitates Na + efflux into the root medium, thereby delaying Na + accumulation in the cytoplasm to allow time for Na + sequestration in the vacuole. (asm.org)
  • Salt Tolerance
  • A Na + /H + antiporter-like protein (NHXLP) was isolated from Sorghum bicolor L. ( SbNHXLP ) and validated by overexpressing in tomato for salt tolerance. (frontiersin.org)
  • Within these two groups are well-characterized antiporters associated with salt tolerance in plants, the salt overly sensitive 1 (SOS1) and sodium hydrogen exchanger (NHX) proteins. (beds.ac.uk)
  • When expressed in a yeast mutant deficient in endogenous Na(+) transporters, SOS1 was able to reduce Na(+) accumulation and improve salt tolerance of the mutant cells. (semanticscholar.org)
  • SOS1, a Genetic Locus Essential for Salt Tolerance and Potassium Acquisition. (semanticscholar.org)
  • Molecular
  • She does research in molecular biology and in her free time enjoys hanging out with family and friends, taking trips to Point Reyes, and conducting imaginary interviews with the proteins she studies. (the-scientist.com)
  • In this study we performed a comprehensive molecular evolutionary analysis of the NHX and SOS1 families. (beds.ac.uk)
  • Gingival
  • At least one mutation in the SOS1 gene has been shown to cause hereditary gingival fibromatosis type 1. (nih.gov)
  • Germ line gain of function with SOS1 mutation in hereditary gingival fibromatosis. (nih.gov)
  • GTPase
  • Reciprocally, GTP hydrolysis is critical for inactivation from Ras·GTP to Ras·GDP and Ras' modest intrinsic rate of GTP hydrolysis requires the hydrolysis-augmenting action of RasGAPs (Ras GTPase activating proteins) (Figure 1 ). (frontiersin.org)
  • GTPase activating proteins (GAPs) enhance slow rate of intrinsic Ras GTPase activity, promoting the inactive GDP-bound state of Ras. (frontiersin.org)
  • Sodium
  • RNAi-based interference of SOS1 caused cell death in the root elongation zone, accompanied by fragmentation of vacuoles, inhibition of endocytosis, and apoplastic sodium influx into the stele and hence the shoot. (biomedsearch.com)
  • variants
  • Reported variants represent identical protein: NP_075593.1, NP_001167537.1 Reported variants represent identical protein: NP_001167536.1, NP_056934.2. (abnova.com)
  • 1994
  • SH2 domain-containing inositol phosphatase-1 (SHIP) was initially identified in 1994 as a tyrosine-phosphorylated protein after stimulation of blood cells by a broad number of cytokines and growth factors (Lioubin et al. (springer.com)
  • interacts
  • The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. (abnova.com)
  • residues
  • Residues affected by substitutions with unpredictable effect on SOS1 function are shown in black. (nih.gov)
  • B: Location of affected residues in SOS1 represented in its inactive conformation, according to the crystal structure of the protein truncated at the C-terminus (residues 1-1049) (PDB ID: 3KSY) [Guerasko et al. (nih.gov)
  • intrinsic
  • The PDBFlex database explores the intrinsic flexibility of protein structures by analyzing structural variations of the same protein across the archive. (rcsb.org)