Copper sulfide with morphology-dependent photodynamic and photothermal antibacterial activities.

Metal chalcogenides have been intensively investigated as antibacterial agents due to their unique structures and superior photoactivities. Herein, various structures of copper sulfide (CuS), a metal chalcogenide, such as microspheres (MSs), nanosheets (NSs), and nanoparticles (NPs), were developed in this work for antibacterial applications. A hydrothermal process was utilized to synthesize CuS MSs, CuS NSs, and CuS NPs.

Helicobacter pylori-derived heat shock protein 60 increases the induction of regulatory T-cells associated with persistent infection.

Local Treg responses are involved in Helicobacter pylori-related inflammation and clinical outcomes after infection, and H. pylori-derived HSP60 (HpHSP60) is an important virulence factor associated with gastric carcinogenesis. This study to investigate the role of HpHSP60 in immunosuppression, particularly with regard to whether it could induce the production of Treg cells.

A rapid and convenient method to enhance transgenic expression in target cells.

Gene therapy provides a novel strategy and a new hope for patients with cancer. Unfortunately, the specifics of the delivery systems or the promoters have not achieved the specified efficacy so far, and the perfection of either system will be extremely difficult. In this study, we introduce a simple concept that a combination of a partially specific delivery system and a partially specific promoter activity may achieve a more specific effect on transgenic expression in target cells.

Antibodies against Helicobacter pylori heat shock protein 60 aggravate HSP60-mediated proinflammatory responses.

Anti-Helicobacter pylori heat shock protein 60 (HpHSP60) antibodies are usually found in H. pylori-infected patients and are known to be associated with the progression of gastric diseases. However, the effects of these antibodies on the functions of HpHSP60 have not been identified.

Helicobacter pylori-derived Heat shock protein 60 enhances angiogenesis via a CXCR2-mediated signaling pathway.

Helicobacter pylori is a potent carcinogen associated with gastric cancer malignancy. Recently, H. pylori Heat shock protein 60 (HpHSP60) has been reported to promote cancer development by inducing chronic inflammation and promoting tumor cell migration.

A potential role for Helicobacter pylori heat shock protein 60 in gastric tumorigenesis.

Helicobacter pylori has been found to promote the malignant process leading to gastric cancer. Heat shock protein 60 of H. pylori (HpHSP60) was previously been identified as a potent immunogene.

Characterizing the polymeric status of Helicobacter pylori heat shock protein 60.

Helicobacter pylori heat shock protein 60 (HpHsp60) was first identified as an adhesion molecule associated with H. pylori infection. Here we have analyzed the structure of HpHsp60 via amino acid BLAST, circular dichroism, and electrophoresis and the results indicate that most recombinant HpHsp60 molecules exist as dimers or tetramers, which is quite different from Escherichia coli Hsp60.