2,6-Dimethyl-4-m-tolyl­cyclo­hex-3-enecarboxylic acid

The title compound, C16H20O2, was synthesized to study the hydrogen-bonding inter­action of the two enanti­omers in the solid state. The racemate is made up of carboxylic acid RS dimers. Inter­molecular O—H⋯O hydrogen bonds produce centrosymmetric R 2 2(8) rings which dimerize the two chiral enanti­omers through their carboxyl groups. The chirality of this compound is generated by the presence of the double bond in the cyclo­hexene ring and a chiral axis due to the meta-methyl substituent on the aromatic ring

Racemic 4-(4-tert-butyl­phen­yl)-2,6-dimethyl­cyclo­hex-3-enecarboxylic acid

The chirality of the title compound, C19H26O2, is solely generated by the presence of the double bond in the cyclo­hexene ring. This compound was synthesized to study the inter­action of the two enanti­omers in the solid state. The resultant racemate is made up of carboxylic acid RS dimers. Inter­molecular O—H⋯O hydrogen bonds produce centrosymmetric R 2 2(8) rings which dimerize the two chiral enanti­omers through their carboxyl groups

4-(3-Methoxy­phen­yl)-2,6-dimethyl­cyclo­hex-3-enecarboxylic acid

The racemic title compound, C16H20O3, was synthesized to study the hydrogen-bonding inter­action of the two enanti­o­mers in the solid state. In the crystal structure, R and S pairs of the racemate are linked by pairs of inter­molecular O—H⋯O hydrogen bonds, producing centrosymmetric R 2 2(8) rings

rac-4-(2-Meth­oxy­phen­yl)-2,6-dimethyl­cyclo­hex-3-ene­carb­oxy­lic acid

The title compound, C16H20O3, was synthesized to study the hydrogen-bonding inter­actions of the two enanti­omers in the solid state. Inter­molecular O—H⋯O hydrogen bonds produce centrosymmetric R 2 2(8) rings which dimerize the two chiral enanti­omers together through their carboxyl groups

Trihydrophobin 1 Phosphorylation by c-Src Regulates MAPK/ERK Signaling and Cell Migration

c-Src activates Ras-MAPK/ERK signaling pathway and regulates cell migration, while trihydrophobin 1 (TH1) inhibits MAPK/ERK activation and cell migration through interaction with A-Raf and PAK1 and inhibiting their kinase activities. Here we show that c-Src interacts with TH1 by GST-pull down assay, coimmunoprecipitation and confocal microscopy assay. The interaction leads to phosphorylation of TH1 at Tyr-6 in vivo and in vitro. Phosphorylation of TH1 decreases its association with A-Raf and PAK1. Further study reveals that Tyr-6 phosphorylation of TH1 reduces its inhibition on MAPK/ERK signaling, enhances c-Src mediated cell migration. Moreover, induced tyrosine phosphorylation of TH1 has been found by EGF and estrogen treatments. Taken together, our findings demonstrate a novel mechanism for the comprehensive regulation of Ras/Raf/MEK/ERK signaling and cell migration involving tyrosine phosphorylation of TH1 by c-Src

Relationship between ID1 and EGFR-TKI Resistance in Non-small Cell Lung Cancer

Background and objective Non-small cell lung cancer (NSCLC) presents the highest morbidity and mortality among malignant tumors worldwide. The overall effective rate of epidermal growth factor receptor-tyrosine kinase inhibitor (EGFR-TKI) is 30% to 40%, and PFS (progression-free sruvival) is 12 months. However, EGFR-TKI resistance is typical in clinical observations, and this phenomenon significantly affects tumor suppression. To overcome this resistance, a new prognostic factor associated with lung cancer drug resistance should be discovered. This study investigated the relationship between the inhibitor of differentiation 1 (ID1) and non-small cell lung cancer EGFR-TKI resistance in vivo and in vitro to determine any statistical significance and discuss the underlying mechanism. Methods Western blot and qRT-PCR were used to quantify the expression of ID1 in lung cancer. IHC was used to detect the expression of ID1 in pathological tissues (lung cancer tissues and adjacent tissues). MTT was used to detect cell proliferation, in which the cells were treated with gefitinib after being transfected by ID1 slow virus vector. Lung cancer cells were inoculated in nude mice until the tumor diameter grew to certain measurement. Gefitinib treatment was started, and the tumor volume was estimated. Results ID1 was highly expressed in NSCLC (P<0.05). Both ID1 expression and drug resistance of EGFR-TKI in NSCLC were positively correlated (P<0.05). The treatment group with gefitinib showed obviously less expression than the control group. Conclusion ID1 is highly expressed in NSCLC. ID1 expression was positively related to drug resistance of EGFR-TKI in NSCLC. Gefitinib can be used to effectively treat NSCLC, and the mechanism may be associated with an increased level of STAT3 phosphorylation