Publications by authors named "Guizhen Lu"

Highly sensitive detection of enhanced terahertz (THz) fingerprint absorption spectrum of trace-amount tiny molecules is essential for biosensing. THz surface plasmon resonance (SPR) sensors based on Otto prism-coupled attenuated total reflection (OPC-ATR) configuration have been recognized as a promising technology in biomedical detection applications. However, THz-SPR sensors based on the traditional OPC-ATR configuration have long been associated with low sensitivity, poor tunability, low refractive index resolution, large sample consumption, and lack of fingerprint analysis.

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Objective: Absence of homozygosity (AOH) is a genetic characteristic known to cause human diseases mainly through autosomal recessive or imprinting mechanisms. The importance and necessity of accurate AOH detection has become more clinically significant in recent years. However, it remains a challenging task for sequencing-based methods thus far.

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Exploiting the well-arranged and tunable frameworks of crystalline materials, we herein report coordination polymers (CPs) with modulated hierarchical structures as triboelectric materials to construct and extend the application scope of triboelectric nanogenerators (TENGs). Different lengths and shapes of bridging ligands [4,4'-bpa = 1,2-bis(4-pyridyl)ethane, 4,4'-bpe = 1,2-bis(4-pyridyl)ethene, and 4,4'-bpp = 1,3-di(2-pyridyl)propane for , , and , respectively] were used to construct Cd-CP-based hierarchical frameworks. These compounds were used as triboelectric materials, and their electronic structure contributions were determined by the output of the corresponding TENGs.

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Precise control of the structure of crystalline materials is an efficient strategy to manipulate the fundamental performance of solids. In metal-organic framework (MOF) materials, this control can be realized by reversible cation-exchange through chemically driven changes in the crystalline state. Herein, we reported that the reversible structural transformations between an anionic Zn-MOF () and a topologically equivalent bimetallic Zn/Co-MOF () were accomplished.

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Precisely controlling the coordination microenvironment and electronic features of polynuclear secondary building units (SBUs) in coordination polymers (CPs) is an efficient approach to governing their fundamental performance. Here, different multinuclear SBUs (binuclear, trinuclear, and pentanuclear SBUs for -, respectively) were introduced into Cd-based CPs, which were used as frictional electrode materials, to clarify the contributions of polynuclear Cd-SBUs through the output of triboelectric nanogenerators (TENGs). The results demonstrated that -TENG with binuclear Cd-SBUs possessed the highest output, whereas -TENG with the pentanuclear Cd-SBUs indicated the minimum output, suggesting that the binuclear Cd-SBUs in lost electrons most readily and generated much more charge, which was further confirmed by density functional theory calculations.

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Precise control over the morphology and size of coordination polymers (CPs) is crucial for extending these inorganic-organic materials to many advanced applications, in particular for heterogeneous catalysis. In this work, two Zn-based CPs, {[Zn(idbt)(4,4'-dmbpy)]·HO} (1) and {[Zn(idbt)(HO)]·HO} (2) (Hidbt = 5,5'-(1H-imidazole-4,5-diyl)-bis-(2H-tetrazole), 4,4'-dmbpy = 4,4''-dimethyl-2,2'-bipyridine), were synthesized through solvothermal reactions. The morphologies and particle sizes of 1 and 2 could be controlled from large scale to nanoscale by regulating the amount of poly(vinyl alcohol) (PVA).

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Inhibition of the major lysosomal proteases, cathepsins B, D, and L, impairs growth of several cell types but leads to apoptosis in neuroblastoma. The goal of this study was to examine the mechanisms by which enzyme inhibition could cause cell death. Cathepsin inhibition caused cellular accumulation of fragments of the insulin growth factor 1 (IGF-1) receptor.

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Purpose: The results of a study to determine the stability of solutions of furosemide and chlorothiazide over 96 hours are reported.

Methods: Chlorothiazide and furosemide were diluted in 5% dextrose USP to final concentrations of 10 and 1 mg/mL, respectively, and combined. In addition, sample solutions of chlorothiazide in dextrose, furosemide in dextrose, and dextrose alone were prepared for control purposes.

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This study was designed to test the hypothesis that specific inhibition of cathepsins B and L will cause death of neuroblastoma cells. Five compounds that differ in mode and rate of inhibition of these two enzymes were all shown to cause neuroblastoma cell death. Efficacy of the different compounds was related to their ability to inhibit the activity of the isolated enzymes.

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A specific irreversible inhibitor of both cathepsins B and L, Fmoc-Tyr-Ala-CHN(2) (FYAD) induced apoptosis of neuroblastoma cells but not other tumor cells. Cysteine protease inhibitors that were not efficient inhibitors of both proteases did not cause death of any cell line tested. Apoptosis was preceded by accumulation of large electron dense vesicles and multivesicular bodies in the cytoplasm.

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Cathepsin P is a recently discovered placental cysteine protease that is structurally related to the more ubiquitously expressed, broad-specificity enzyme, cathepsin L. We studied the substrate specificity requirements of recombinant mouse cathepsin P using fluorescence resonance energy transfer (FRET) peptides derived from the lead sequence Abz-KLRSSKQ-EDDnp (Abz, ortho-aminobenzoic acid and EDDnp, N-[2,4-dinitrophenyl]ethylenediamine). Systematic modifications were introduced resulting in five series of peptides to map the S(3) to S(2)(') subsites of the enzyme.

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The mouse genome contains a family of clan C1A proteases that appear to be restricted to rodents within Eutherian (placental) mammals. mRNA analysis has shown that these genes are expressed exclusively in placenta. Sequence analysis predicts that the expressed proteins will be functional and consequently it was proposed that this family of proteases may have evolved to perform subspecialized functions of the closely related protease, cathepsin L, that is expressed in placental tissues of all mammalian species.

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