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1.  Ligand-dependent EphB1 signaling suppresses glioma invasion and correlates with patient survival 
Neuro-Oncology  2013;15(12):1710-1720.
Extensive evidence implicates the Eph receptor family of tyrosine kinases and its ligand, ephrin, in glioma invasion, but it remains incompletely understood how these receptors affect chemotactic behavior of glioma. We sought to identify the Eph family members that correlate with patients' survival and to reveal the function of Eph in glioma invasion.
Clinical relevance of EphB genes was confirmed in a clinically annotated expression data set of 195 brain biopsy specimens. The function of EphB was analyzed in vitro and in vivo.
Levels of mRNA of certain EphB members were significantly different in histological grades of glioma. According to Kaplan–Meier analysis, only the EphB1 level among 5 members of EphB emerged to be a powerful predictor of favorable survival in malignant glioma (n = 97, P = .0048), although the levels of EphB1 expression did not vary across the tumor grades. Immunoprecipitation showed that tyrosine phosphorylated EphB1 was not detected in all glioma cells tested. Forced overexpression and autophosphorylation of EphB1 in low expressor cell lines (U251, U87) did not affect cell migration or invasion in vitro, whereas EphB1 phosphorylation induced by ephrin-B2/Fc significantly decreased migration and invasion. Cells expressing ephrin-B2 showed noteworthy morphological changes consistent with migration induction; this alteration was negated by EphB1 overexpression. Concomitantly, overexpression of EphB1 abrogated the increased migration and invasion induced by ephrin-B2 in vitro and in vivo.
These data suggest that ligand-dependent EphB1 signaling negatively regulates glioma cell invasion, identifying EphB1 as a favorable prognostic factor in malignant glioma.
PMCID: PMC3829595  PMID: 24121831
glioma; invasion; migration; Eph-ephrin; tyrosine kinase
2.  Intraoperative Fluorescence-Guided Resection of High-Grade Malignant Gliomas Using 5-Aminolevulinic Acid–Induced Porphyrins: A Systematic Review and Meta-Analysis of Prospective Studies 
PLoS ONE  2013;8(5):e63682.
We performed a systematic review and meta-analysis to address the (added) value of intraoperative 5-aminolevulinic acid (5-ALA)-guided resection of high-grade malignant gliomas compared with conventional neuronavigation-guided resection, with respect to diagnostic accuracy, extent of tumor resection, safety, and survival.
Methods and Findings
An electronic database search of Medline, Embase, and the Cochrane Library was undertaken. The review process followed the guidelines of the Cochrane Collaboration. 10 studies matched all selection criteria, and were thus used for qualitative synthesis. 5-ALA-guided resection demonstrated an overall sensitivity of 0.87 (95% confidence interval [CI], 0.81–0.92), specificity of 0.89 (95% CI, 0.79–0.94), positive likelihood ratio (LR) of 7.62 (95% CI, 3.87–15.01), negative LR of 0.14 (95% CI, 0.09–0.23), and diagnostic odds ratio (OR) of 53.06 (95% CI, 18.70–150.51). Summary receiver operating characteristic curves (SROC) showed an area under curve (AUC) of 94%. Contrast-enhancing tumor was completely resected in patients assigned 5-ALA as compared with patients assigned white light. Patients in the 5-ALA group had higher 6-month progression free survival and overall survival than those in the white light group.
Based on available literature, there is level 2 evidence that 5-ALA-guided surgery is more effective than conventional neuronavigation-guided surgery in increasing diagnostic accuracy and extent of tumor resection, enhancing quality of life, or prolonging survival in patients with high-grade malignant gliomas.
PMCID: PMC3665818  PMID: 23723993
3.  Aberrant Signaling Pathways in Glioma 
Cancers  2011;3(3):3242-3278.
Glioblastoma multiforme (GBM), a WHO grade IV malignant glioma, is the most common and lethal primary brain tumor in adults; few treatments are available. Median survival rates range from 12–15 months. The biological characteristics of this tumor are exemplified by prominent proliferation, active invasiveness, and rich angiogenesis. This is mainly due to highly deregulated signaling pathways in the tumor. Studies of these signaling pathways have greatly increased our understanding of the biology and clinical behavior of GBM. An integrated view of signal transduction will provide a more useful approach in designing novel therapies for this devastating disease. In this review, we summarize the current understanding of GBM signaling pathways with a focus on potential molecular targets for anti-signaling molecular therapies.
PMCID: PMC3759196  PMID: 24212955
glioblastoma; signaling; proliferation; invasion; angiogenesis; molecular target
4.  1-[5-(Dimethyl­amino)-1-naphthylsulfon­yl]imidazolidine-2-thione 
In the title mol­ecule, C15H17N3O2S2, the dihedral angle between the naphthalene ring system and the imidazole ring is 89.63 (2)°. The crystal structure is stablized by weak inter­molecuar C—H⋯π and N—H⋯π inter­actions.
PMCID: PMC3007268  PMID: 21588459
5.  Knockout of p47phox Uncovers a Critical Role of p40phox in Reactive Oxygen Species Production in Microvascular Endothelial Cells 
p40phox is an important regulatory subunit of NADPH oxidase, but its role in endothelial reactive oxygen species (ROS) production remains unknown.
Methods and Results
Using coronary microvascular endothelial cells isolated from wild-type and p47phox knockout mice, we found that knockout of p47phox increased the level of p40phox expression, whereas depletion of p40phox in wild-type cells increased p47phox expression. In both cases, the basal ROS production (without agonist stimulation) was well preserved. Double knockout of p40phox and p47phox dramatically reduced (≈65%) ROS production and cells started to die. The transcriptional regulation of p40phox and p47phox expressions involves HBP1. p40phox was prephosphorylated in resting cells. PMA stimulation induced p40phox swift dephosphorylation (within 1 minute) in parallel with the start of p47phox phosphorylation. p40phox was then rephosphorylated, and this was accompanied with an increase in ROS production. Depletion of p40phox resulted in ≈67% loss in agonist-induced ROS production despite the presence of p47phox. These were further supported by experiments on mouse aortas stimulated with angiotensin II.
p40phox is prephosphorylated in resting endothelial cells and can compensate p47phox in keeping basal ROS production. Dephosphorylation of p40phox is a prerequisite for agonist-induced p47phox phosphorylation, and p40phox through its dynamic dephosphorylation and rephosphorylation is involved in the regulation of agonist-induced ROS production.
PMCID: PMC2888064  PMID: 19608974
NADPH oxidase; endothelial cells; gene regulation; reactive oxygen species
6.  Ethyl 3-amino-1-phenyl-1H-benzo[f]chromene-2-carboxyl­ate 
The pyranyl ring of the title compound, C22H19NO3, adopts a flattened-boat conformation. The dihedral angle between naphthalene and phenyl rings is 78.3 (1)°The mol­ecule also features an intra­molecular N—H⋯Ocarbon­yl hydrogen bond. Adjacent mol­ecules are linked by an inter­molecular N—H⋯Ocarbon­yl hydrogen bond, forming a zigzag chain that runs along the c axis.
PMCID: PMC2969098  PMID: 21582501
7.  5-(1H-Imidazol-1-ylsulfon­yl)-N,N-dimethyl­naphthalen-1-amine 
In the title mol­ecule, C15H15N3O2S, the dihedral angle between the naphthalene ring system and the imidazole ring is 86.1 (2)°. In the crystal structure, weak inter­molecular C—H⋯O and C—H⋯N hydrogen bonds, as well as weak C—H⋯π inter­actions, connect mol­ecules, forming a two-dimensional network.
PMCID: PMC2967969  PMID: 21581696
8.  4-(1,3-Benzothia­zol-2-yl)-N-(2-pyridylmeth­yl)aniline monohydrate 
In the title compound, C19H15N3S·H2O, the benzothia­zole ring system forms a dihedral angle of 7.22 (1)° with the benzene ring and the benzene ring forms a dihedral angle of 80.89 (1)° with the pyridine ring. An intra­molecular N—H⋯O inter­action is present. The crystal structure is stablized by inter­molecular O—H⋯N hydrogen bonds, π–π [centroid–centroid distances = 3.782 (1), 3.946 (1) and 3.913 (1) Å] and C—H⋯π inter­actions, forming a three dimensional-network.
PMCID: PMC2967994  PMID: 21581724
9.  2-(4-Amino­phen­yl)-1,3-benzothia­zole 
The title compound, C13H10N2S, contains two independent mol­ecules in its asymmetric unit, with slightly different conformations. In one mol­ecule, the dihedral angle between the benzothia­zole unit and the benzene ring is 6.73 (1)°, while the corresponding angle in the other mol­ecule is 1.8 (1)°. In the crystal structure, the mol­ecules are linked into layers by N—H⋯N hydrogen bonds.
PMCID: PMC2959689  PMID: 21580931
10.  A polymorph of terephthalaldehyde 
A new ortho­rhom­bic polymorph of terephthalaldehyde, C8H6O2, with a melting point of 372 K, has been obtained by recrystallization from ethanol. At room temperature, the crystals transform into the well known monoclinic form, with a melting point of 389 K. The crystal structure of the monoclinic form involves C—H⋯O hydrogen bonds, but no such bonds are observed in the orthorhombic form. The molecule is planar.
PMCID: PMC2962184  PMID: 21203265
11.  2-(4-Amino­phen­yl)-1,3-benzoxazole 
In the title mol­ecule, C13H10N2O, the dihedral angle between the benzoxazole ring system and the benzene ring is 11.8 (1)°. In the crystal structure, mol­ecules are linked by inter­molecular N—H⋯N hydrogen bonds and π⋯π inter­actions [centroid–centroid distance = 3.6560 (15) Å] to form a two-dimensional network.
PMCID: PMC2961872  PMID: 21202849
12.  Diacetatobis[1,3-bis­(benzimidazol-2-yl)benzene]zinc(II) dihydrate 
In the title complex, [Zn(CH3COO)2(C20H14N4)2]·2H2O, the ZnII atom, which lies on a crystallographic twofold axis, is coordinated by two O atoms of two acetate ligands and two N atoms from two 1,3-bis­(benzimidazol-2-yl)benzene ligands in a distorted tetra­hedral geometry. The complex mol­ecules and solvent water mol­ecules are connected via O—H⋯N, O—H⋯O and N—H⋯O hydrogen bonds, forming a three-dimensional network.
PMCID: PMC2960180  PMID: 21201289

Results 1-12 (12)