Disease relevance of FOXG1

• Tumor cells from over 90% of snap frozen peripheral T-cell lymphomas reacted with BF1 and BF2 [1].
• Monoclonal antibodies (HBA4, HBE3, HBE10, HBF2, HBG9, and HBH8) from the hybridoma clones were selected for their serologic reactivity to cell surface antigens of KU-1 cells and for their unresponsiveness to 2 human lymphoma cell lines [2].
• To elucidate the structure, new allelic beta2m and five different BF2 genes were expressed solubly and purified in a pMAL-p2X/E. coli TB1 system [3].

High impact information on FOXG1

• With regard to reactivity to normal human cells and tissues, HBG9 alone was reactive to epidermis and both HBF2 and HBH8 were reactive to erythrocytes, but none of the other 3 monoclonal antibodies was reactive to any normal cells or tissues [2].
• DNA-binding protein blotting, UV crosslinking, and electroelution experiments were used to characterize the two hMREa-binding factors, termed BF1 and BF2 [4].
• VAC-ssBF1 and BF2 binding activity was detected in undifferentiated myoblasts, embryonic fibroblasts, and several smooth muscle tissues in the mouse and human [5].
• 1,3-Dipyrrolyl-1,3-propanediones, synthesized from pyrroles and malonyl chloride, form BF2 complexes, which represent a new class of naked-eye sensors for halide and oxoanions [6].
• In the case of the chloride anion complex, the formation of Cl(-)-bridged 1D networks, in which anion is associated with two BF2 complexes, is observed in the solid state [6].

Biological context of FOXG1

• The HBF-2 cDNA was isolated from a human fetal brain expression library and contains a putative open reading frame of 479 amino acids [7].
• We have isolated a second human gene (HBF-2), which is also strongly expressed in embryonic brain and has very high homology to both the rat and human brain factor-1 genes and the retroviral oncogene qin [7].
• In tests of samples of unknown B genotype in commercial broiler-breeder flocks, we identified expected BF2 alleles as well as an allele not previously encountered in one of the lines [8].

Anatomical context of FOXG1

• These antibodies were all satisfactory in the staining of normal peripheral lymphoid tissues and cortical thymic lymphocytes were reactive with BF1 and BF2 but not with WT31 [1].
• The incorporation of the negative curvature-inducing lipid egg yolk L-alpha -phosphatidylethanolamine completely suppressed the translocation of BF2, indicating the induction of the positive curvature by BF2 on the membrane is related to the translocation process, similarly to MG2 [9].

Associations of FOXG1 with chemical compounds

• A BF2 analogue with an alpha-methylproline, which fixed the peptide bond to the trans configuration, translocated similarly to the parent peptide, suggesting the cis-trans isomerization of the Pro peptide bond is not involved in the translocation process [9].
• CH...anion interaction in BF2 complexes of C3-bridged oligopyrroles [10].
• Synthesis and anion binding properties of BF2 complexes of beta-tetraethyl-substituted dipyrrolyldiketones, with and without electron-withdrawing ethoxycarbonyl moieties at pyrrole alpha-positions, are reported [11].
• Structure and bonding of transition metal-boryl compounds. Theoretical study of [(PH3)2(CO)ClOs-BR2] and [(PH3)2(CO)2ClOs-BR2] (BR2 = BH2, BF2, B(OH)2, B(OCH=CHO), Bcat) [12].
• Quantum chemical DFT calculations using the B3LYP functionals have been carried out for the electronically unsaturated 16 VE five-coordinate osmium boryl-complexes [(PH3)2(CO)ClOs-BR2] and the 18 VE six-coordinate complexes [(PH3)2(CO)2ClOs-BR2] with BR2 = BH2, BF2, B(OH)2, B(OHC=CHO), and Bcat (cat = catecholate O2C6H4) [12].

Physical interactions of FOXG1

• At the genomic level the gene for HBF-1 contains an 500 bp intron situated between the DNA binding domain II and the fork head domain while that of HBF-2 is intronless [7].

Other interactions of FOXG1

• The cDNA clones HFK2 and HFK3 were analyzed by restriction analysis and sequencing [13].

References