Shih-Ming Lin

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H(+)-translocating pyrophosphatases (H(+)-PPases) are active proton transporters that establish a proton gradient across the endomembrane by means of pyrophosphate (PP(i)) hydrolysis. H(+)-PPases are found primarily as homodimers in the vacuolar membrane of plants and the plasma membrane of several protozoa and prokaryotes. The three-dimensional structure(More)
We present a ZnO(1-x) nanorod array (NR)/ZnO thin film (TF) bilayer structure synthesized at a low temperature, exhibiting a uniquely rectifying characteristic as a homojunction diode and a resistive switching behavior as memory at different biases. The homojunction diode is due to asymmetric Schottky barriers at interfaces of the Pt/ZnO NRs and the ZnO(More)
A spontaneously formed ZnO/ZnWOx bilayer resistive memory via an interfacial engineering by one-step sputtering process with controllable high resistance states was demonstrated. The detailed formation mechanism and microstructure of the ZnWOx layer was explored by X-ray photoemission spectroscopy (XPS) and transmission electron microscope in detail. The(More)
Vacuolar H(+)-pyrophosphatase (V-PPase; EC 3.6.1.1) plays a significant role in the maintenance of the pH in cytoplasm and vacuoles via proton translocation from the cytosol to the vacuolar lumen at the expense of PP(i) hydrolysis. The topology of V-PPase as predicted by TopPred II suggests that the catalytic site is putatively located in loop e and exposed(More)
H+-translocating pyrophosphatase (H+-PPase; EC 3.6.1.1) drives proton transport against an electrochemical potential gradient by hydrolyzing pyrophosphate (PPi) and is found in various endomembranes of higher plants, bacteria, and some protists. H+-PPase contains seven highly conserved lysines. We examined the functional roles of these lysines, which are,(More)
Homodimeric H(+)-pyrophosphatase (H(+)-PPase; EC 3.6.1.1) is a unique enzyme playing a pivotal physiological role in pH homeostasis of organisms. This novel H(+)-PPase supplies energy at the expense of hydrolyzing metabolic byproduct, pyrophosphate (PP(i)), for H(+) translocation across membrane. The functional unit for the translocation is considered to be(More)
OBJECTIVES To study effects of various concentrations of hydrogen peroxide on mature waterline biofilms and in controlling planktonic (free-floating) organisms in simulated dental treatment water systems; and to study in vitro the effects of 2%, 3%, and 7% hydrogen peroxide on the removal of mature biofilms and inorganic compounds in dental waterlines. (More)
Vacuolar proton-translocating pyrophosphatase (V-PPase) generates a proton electrochemical gradient across the membrane by hydrolyzing pyrophosphate for maintenance of acidic condition of vacuoles and translocation of secondary metabolites, ions, and even toxics. The enzymatic activity of V-PPase could be stimulated by relatively high concentration of K,(More)
Vacuolar H(+)-translocating inorganic pyrophosphatase [vacuolar H(+)-pyrophosphatase (V-PPase); EC 3.6.1.1] is a homodimeric proton translocase; it plays a pivotal role in electrogenic translocation of protons from the cytosol to the vacuolar lumen, at the expense of PP(i) hydrolysis, for the storage of ions, sugars, and other metabolites. Dimerization of(More)
The Ku heterodimer, a DNA repair protein complex consisting of 70- and 80-kDa subunits, is involved in the non-homologous end-joining (NHEJ) pathway. Plants are thought to use the NHEJ pathway primarily for the repair of DNA double-strand breaks (DSBs). The Ku70/80 protein has been identified in many plants and been shown to possess several similar(More)