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Stromal cell-derived factor 2

SDF-2, stromal cell-derived factor-2
The protein encoded by this gene is believed to be a secretory protein. It has regions of similarity to hydrophilic segments of yeast mannosyltransferases. Its expression is ubiquitous and the gene appears to be relatively conserved among mammals. Alternate splicing results in both coding and non-coding variants. A pseudogene of this gene is located on chromosome 15. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: CAN, Rdl, ACID, Phosphodiesterase, Slug
Papers on SDF-2
Stromal cell-derived factor 2 is critical for Hsp90-dependent eNOS activation.
Sessa et al., New Haven, United States. In Sci Signal, Sep 2015
Combining a tandem affinity purification approach and mass spectrometry, we identified stromal cell-derived factor 2 (SDF2) as a component of the eNOS macromolecular complex in endothelial cells.
Stromal cell derived factor-2 (Sdf2): a novel protein expressed in mouse.
Bevilacqua et al., São Paulo, Brazil. In Int J Biochem Cell Biol, 2014
SDF1 and SDF4 are chemokines; SDF2 and SDF5 are not yet functionally and structurally defined.
Regulation of SOBIR1 accumulation and activation of defense responses in bir1-1 by specific components of ER quality control.
Zhang et al., Vancouver, Canada. In Plant J, 2014
Here we report that mutations in three components of ER quality control, CALRETICULIN3 (CRT3), ER-LOCALIZED DnaJ-LIKE PROTEIN 3b (ERdj3b) and STROMAL-DERIVED FACTOR-2 (SDF2), also suppress the spontaneous cell death and constitutive defense responses in bir1-1.
The endoplasmic reticulum-quality control component SDF2 is essential for XA21-mediated immunity in rice.
Ronald et al., Davis, United States. In Plant Sci, 2013
Several endoplasmic reticulum-quality control (ER-QC) proteins including stromal-derived factor 2 (SDF2) co-purified with XA21.
Comparative genomics of the dictyostelids.
Loomis, San Diego, United States. In Methods Mol Biol, 2012
Most of the genes known to be involved in specific signal transduction pathways that mediate intercellular communication are present in each of the sequenced species but both P. pallidum and D. fasciculatum appear to be missing the gene responsible for synthesis of GABA, gadA, suggesting that release of the SDF-2 precursor AcbA is not regulated by GABA in these species as it is in D. discoideum.
The influence of environmental factors on the adhesion of combinations of probiotics to rice fibre fractions.
Bamunuarachchi et al., Palmerston North, New Zealand. In World J Microbiol Biotechnol, 2012
Nine co-cultures of the Bifidobacterium and Lactobacillus species were tested for their ability to adhere to insoluble dietary fibre (IDF1, IDF2), soluble dietary fibre (SDF1, SDF2), and total dietary fibre (TDF1, TDF2) from two rice varieties (RR1 and RR2).
The polyketide MPBD initiates the SDF-1 signaling cascade that coordinates terminal differentiation in Dictyostelium.
Loomis et al., San Diego, United States. In Eukaryot Cell, 2011
This signaling cascade shows similarities to the SDF-2 signaling pathway, which acts later to induce rapid spore encapsulation.
Identification of defense-related genes newly-associated with tomato flower abscission.
Lers et al., Ağrı, Turkey. In Plant Signal Behav, 2011
We identified four different defense-related genes, including: Cysteine-type endopeptidase, α-Dioxygenase 1 (α-DOX1), HopW-1-1-Interacting protein2 (WIN2), and Stomatal-derived factor-2 (SDF2), that are newly-associated with the late stage of the abscission process.
Methods to study stromal-cell derived factor 2 in the context of ER stress and the unfolded protein response in Arabidopsis thaliana.
Strahl et al., Heidelberg, Germany. In Methods Enzymol, 2010
Stromal cell-derived factor 2 (SDF2)-type proteins are conserved throughout the animal and plant kingdoms.
Unconventional secretion of AcbA in Dictyostelium discoideum through a vesicular intermediate.
Kuspa et al., Houston, United States. In Eukaryot Cell, 2010
The acyl coenzyme A (CoA) binding protein AcbA is secreted unconventionally and processed into spore differentiation factor 2 (SDF-2), a peptide that coordinates sporulation in Dictyostelium discoideum.
Arabidopsis stromal-derived Factor2 (SDF2) is a crucial target of the unfolded protein response in the endoplasmic reticulum.
Strahl et al., Heidelberg, Germany. In J Biol Chem, 2010
Stromal cell-derived factor2 (SDF2)-type proteins are highly conserved throughout the plant and animal kingdoms.
Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation.
Subramani et al., San Diego, United States. In J Cell Biol, 2010
We discovered, surprisingly, that the secretion, processing, and function of an AcbA-derived peptide, SDF-2, are conserved between the yeast Pichia pastoris and D. discoideum.
Transcript analyses of stromal cell derived factors (SDFs): SDF-2, SDF-4 and SDF-5 reveal a different pattern of expression and prognostic association in human breast cancer.
Jiang et al., Cardiff, United Kingdom. In Int J Oncol, 2009
SDF-2, SDF-4 and SDF-5 are expressed in mammary tissues and cells and that a reduced level of SDF-2 and SDF-4 are associated with a poor clinical outcome.
The Golgi-associated protein GRASP is required for unconventional protein secretion during development.
Malhotra et al., San Diego, United States. In Cell, 2007
Upon release, AcbA is processed to generate a peptide called spore differentiation factor-2 (SDF-2), which triggers terminal differentiation of spore cells.
What you need to know about GB virus C.
Varmaz et al., Saint Louis, United States. In Curr Gastroenterol Rep, 2005
The mechanism of this effect is not yet clear, but GBV-C has been shown to inhibit HIV replication in vitro through increased synthesis and secretion of anti-HIV b-chemokines MIP-1a, MIP-1b, RANTES, SDF-1, and SDF-2 and downregulation of CCR5 receptor expression.
Role of PKA in the timing of developmental events in Dictyostelium cells.
Loomis, San Diego, United States. In Microbiol Mol Biol Rev, 1998
A positive feedback loop results in the rapid release of a signal peptide, SDF-2, when prestalk cells are exposed to low levels of SDF-2.
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