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Chung Shan Medical University Hospital ... Publications | LitMetric

5 results match your criteria: "Chung Shan Medical University Hospital No. 110[Affiliation]"

The alkaline intracellular environment of cancer cells is critical for cell proliferation and controlled by various plasma membrane transporters including Na+/H+ exchangers (NHEs). NHEs can also mediate cell behavior by regulating signaling transduction. In this study, we investigated the role of NHE7 in cancer stem cell (CSC) activity in non-small cell lung cancer (NSCLC) cells and the potential therapeutic implications of targeting NHE7 and the associated immune checkpoint molecule PD-L1.

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Characterization of an SSB-dT25 complex: structural insights into the S-shaped ssDNA binding conformation.

RSC Adv

December 2019

School of Biomedical Sciences, Chung Shan Medical University No. 110, Sec. 1, Chien-Kuo N. Rd. Taichung City Taiwan +886-4-24730022 ext. 11472.

Single-stranded DNA (ssDNA)-binding proteins (SSBs) play an important role in all DNA-dependent cellular processes, such as DNA replication, recombination, repair, and replication restart. The N-terminal domain of SSBs forms an oligonucleotide/oligosaccharide-binding (OB) fold for ssDNA binding. The SSB-dC35 complex structure has revealed how an SSB (EcSSB) tetramer binds to 65-nucleotide (nt)-long ssDNA, namely, the (SSB) binding mode.

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The glycine-rich flexible region in SSB is crucial for PriA stimulation.

RSC Adv

October 2018

School of Biomedical Sciences, Chung Shan Medical University No. 110, Sec. 1, Chien-Kuo N. Rd. Taichung City Taiwan.

Single-stranded DNA-binding protein (SSB) is essential for all DNA-dependent cellular processes. The mechanism through which PriA helicase, an initiator protein in the DNA replication restart process, is stimulated by SSB in (Ec) has been established. Nevertheless, whether or not PriA stimulated by SSB is conserved among Gram-negative bacteria remains unclear, and the SSB specificity for the stimulation effect on PriA is unknown.

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Single-stranded DNA-binding proteins (SSBs) are essential to cells as they participate in DNA metabolic processes, such as DNA replication, repair, and recombination. The functions of SSBs have been studied extensively in . Unlike , which contains only one type of SSB (EcSSB), some bacteria have more than one paralogous SSB.

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The reactions of the tridentate hydrazone ligand, N'-[1-(pyridin-2-yl)ethylidene]acetohydrazide (HL), obtained by condensation of 2-acetylpyridine with acetic hyadrazide, with copper nitrate trihydrate in the presence of thiocyanate, or with CuCl2 produce two distinct coordination compounds, namely a one-dimensional helical coordination chain of [CuL(NCS)] n (1) units, and a doubly chlorido-bridged dinuclear complex [Cu2L2Cl2] (2) (where L=CH3C(O)=N-N=CCH3C5H4N). Single-crystal X-ray structural determination studies reveal that in complex 1, a deprotonated hydrazone ligand L(-) coordinates a copper(II) ion that is bridged to two neighbouring metal centres by SCN(-) anions, generating a one-dimensional helical coordination chain. In complex 2, two symmetry-related, adjacent copper(II) coordination entities are doubly chlorido-bridged, producing a dicopper entity with a Cu⋅⋅⋅Cu distance of 3.

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