Publications by authors named "Yue Jiachang"

A novel biosensor regulated by the rotator of F0F1-ATPase was developed to analyze 2-dodecylcyclobutanone (2-DCB) to detect γ-ray irradiated beef rapidly. The biosensor was assembled by conjugating 2-DCB monoclonal antibodies with the "rotator" ε-subunit of F0F1-ATPase within chromatophores through an ε-subunit monoclonal antibody-biotin-avidin-biotin linker. The limit of detection (LOD) of 2-DCB was approximately 10(-8) μg/mL.

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We report on thrombolysis acceleration of a nanomachine powered by light-driving δ-subunit-free F0F1-ATPase motor. It is composed of a mechanical device, locating device, energy storage device, and propeller. The rotory δ-subunit-free F0F1-ATPase motor acts as a mechanical device, which was obtained by reconstructing an original chromatophore extracted from Rhodospirillum rubrum.

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To develop a specific, rapid and convenient method based on molecular motor biosensor to detect food-borne rotavirus. A specific probe was encompassed the conservative region of rotavirus's VP7 segment, and a molecular motor detect device was constructed by connecting probes to F0F1-ATPase molecular motor through biotin-streptavidin system. This biosensor's sensitivity was 0.

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We designed a rotary biosensor as a damping effector, with the rotation of the F(0)F(1)-ATPase driven by Adenosine Triphosphate (ATP) synthesis being indicated by the fluorescence intensity and a damping effect force being induced by the binding of an RNA molecule to its probe on the rotary biosensor. We found that the damping effect could contribute to the resonance phenomenon and energy transfer process of our rotary biosensor in the liquid phase. This result indicates that the ability of the rotary motor to operate in the vibration harmonic mode depends on the environmental conditions and mechanism in that a few molecules of the rotary biosensor could induce all of the sensor molecules to fluoresce together.

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A novel biosensor (immuno-rotary biosensor) was developed by conjugating deoxynivalenol (DON) monoclonal antibodies with the "rotator" ε-subunit of F(0)F(1)-ATPase within chromatophores with an ε-subunit monoclonal antibody-biotin-avidin-biotin linker to capture DON residues. The conjugation conditions were then optimized. The capture of DON was based on the antibody-antigen reaction and it is indicated by the change in ATP synthetic activity of F(0)F(1)-ATPase, which is measured via chemiluminescence using the luciferin-luciferase system with a computerized microplate luminometer analyzer.

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A novel ATPase/nanoporous membrane system was prepared. In this system, the activity of F(0)F(1)-ATPase was preserved. The two sides of F(0)F(1)-ATPase were successfully separated macroscopically, and the chemical environments of the two sides could be manipulated in situ individually and freely.

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F(o)F(1)-ATPase is an amazing molecular rotary motor at the nanoscale. Single molecule technologies have contributed much to the understanding of the motor. For example, fluorescence imaging and spectroscopy revealed the physical rotation of isolated F(1) and F(o), or F(o)F(1) holoenzyme.

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F(o)F(1)-ATPase activity is regulated by external links on beta subunits with different molecular weight. It is inhibited when anti-beta subunit antibody, streptavidin and H9 antibody link on the beta subunits successively, but is activated when virus was binded. Western blotting indicated that the employed anti-beta antibody target was on the non-catalytic site of the beta subunit.

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The effects of extremely low frequency (ELF) magnetic fields on membrane F(0)F(1)-ATPase activity have been studied. When the F(0)F(1)-ATPase was exposed to 60 Hz magnetic fields of different magnetic intensities, 0.3 and 0.

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F0F1-ATPase motors have unique mechanical properties, making them attractive building blocks in the field of nanotechnology. However, their organization into well-defined structures with practical functions remains a critical challenge. Here, we describe a self-assembling complex formed by F0F1-ATPase and a ghost which is ordered.

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DPN (Dip-Pen nanolithography) is one kind of widely used technique to create nanoscopic patterns of many different materials. FoF1-ATPase is nano scale rotary molecular motor, and it would be an ideal motor or energy providing device in micro/nano system. In this paper, we used DPN technique to create nanoarrays of F0F1-ATPase within chromatophore on gold surface.

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We have developed a novel micro-mixer using a biological molecular ATP motor. The micro-mixer was constructed from arrays of chromatophore-embedded delta-free F(0)F(1)-ATPases, where the delta-free F(1) part acted as a rotator to mix solutions, and the F(0) part was driven by light. Confocal microscope studies indicated that the micro-mixer did not touch directly on the fibrin labeled with FITC.

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Objective: To study the effects of extremely low frequency sinusoidal magnetic fields on hydrolysis of F(0)F(1)-ATPase and its mechanism.

Methods: The F(0)F(1)-ATPases which was localized on the outer surface of chromatophores were prepared from the cells of Rhodospirillum rubrum and were exposed to 0.1 approximately 0.

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Article Synopsis
  • HER2 is a transmembrane protein involved in key cellular processes and cancer development, belonging to the epidermal growth factor receptor family.
  • Researchers used single-molecule fluorescence microscopy to observe how HER2 molecules move within living cells, noting different diffusion rates and behaviors.
  • Activation by heregulin beta1 increased HER2 mobility, which was linked to tyrosine phosphorylation of HER2 or EGFR, shedding light on HER2 activation and its role in signaling through the HER2/HER3 heterodimer.
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This article has been withdrawn consistent with Elsevier Policy on Article Withdrawal (http://www.elsevier.com/locate/withdrawalpolicy).

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Although there are many reports about the efficacy of siRNAs, it is not clear whether those siRNAs with high C/G contents can be used to silence their target mRNAs efficiently. In this study, we investigated the structure and function of a group of siRNAs with high C/G contents. The results showed that single siRNAs against the Calpain, Otoferlin and Her2 mRNAs could induce different silencing effects on their targets, suggesting that the accessibility to target sequences influences the efficacy of siRNA.

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F(0)F(1)-ATPase within chromatophores, which was labeled with pH-sensitive quantum dots, was encapsulated in large unilamellar lipid vesicles (LUVs) through reverse-phase evaporation. Then a microarray of chromatophore-containing LUVs was created using a micro-contact printing (mu-CP) technique. Through controlled dehydration-rehydration of the lipid patterns, a microarray of single chromatophore-containing giant unilamellar lipid vesicles (GUVs) was formed with desired size and uniform shape.

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One of the most highlighted and fastest moving interfaces of nanotechnology is the application of quantum dots (QDs) in biology. The unparalleled advantages of the size-tunable fluorescent emission and the simultaneous excitation at a single wavelength make QDs the great possibility for use in optical encoding detection. In this paper, we report that green and orange CdTe QDs as convenient, cheap, reversible, and effective pH-sensitive fluorescent probes could monitor the proton (H+) flux driven by ATP synthesis for dual simultaneous and independent detection of viruses on the basis of antibody-antigen reactions.

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Semiconductor nanocrystals, often known as quantum dots, have been used extensively for a wide range of applications in bioimaging and biosensing. In this article, we report that the pH-sensitive cadmium telluride (CdTe) quantum dots (QDs) were used as a proton sensor to detect proton flux that was driven by ATP synthesis in chromatophores. To confirm that these QD-labeled chromatophores were responding to proton flux pumping driven by ATP synthesis, N,N'-dicyclohexylcarbodiimide (DCCD) was used as an inhibitor of ATPase activity.

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F(0)F(1)-ATPase is a rotary molecular motor. It is well known that the rotary torque is generated by ATP hydrolysis in F(1) but little is known about how it produces the proton-motive force (PMF) in F(0). Here a cross-linking approach was used to estimate the rotary torque produced by PMF.

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The heregulinbeta (HRGbeta) is a ligand to activate c-erbB2/c-erbB3 interaction and can subsequently increases cytosolic [Ca(2+)](i). In the two human breast cancer cell lines, MCF-7 shows a low c-erbB2 expression level, whereas SK-BR-3 overexpress c-erbB2 receptor. In this article, we have found that in MCF-7, HRGbeta induced Ca(2+) release from the endoplasmic reticulums (ER) and subsequently activated Ca(2+) entry via store-operated Ca(2+) channel (SOC).

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A Nanodevice was constructed by delta-free F(o)F(1)-ATPase within chromatophores and actin filaments through biotinlipid-streptavidin-biotin-(AC(5))(2)Sulfo-OSu system. One actin filament linking with many chromatophores functions as the Nanodevice body and many delta-free F(o)F(1)-ATPase as the Nanodevice motors. Movement of the Nanodevice was observed directly by fluorescence microscopy with CCD camera after illumination.

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In order to observe mechanically driven proton flux in F(0)F(1)-ATPase coupled with artificial driven rotation on F(1) simultaneously, a double channel observation system was established. An artificial delta-free F(0)F(1)-ATPase was constructed with alpha(3), beta(3), epsilon, gamma, and c(n) subunits as rotator and a, b(2) as stator. The chromatophore was immobilized on the glass surface through biotin-streptavidin-biotin system, and the magnetic bead was attached to the beta subunit of delta-free F(0)F(1)-ATPase.

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F(0)F(1)-ATPase within chromatophore was constructed as a biosensor (immuno-rotary biosensor) for the purpose of capturing single virus. Capture of virus was based on antibody-antigen reaction. The detection of virus based on proton flux change driven by ATP-synthesis of F(0)F(1)-ATPase, which was indicated by F1300, was directly observed by a fluorescence microscope.

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N-(Fluorescein-5-thiocarbamoyl)-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethylammonium salt (F-DHPE) is a lipid fluorescence dye sensitive to pH changes and is used in this study for detecting proton flux through F0F1-ATPase within chromatophores driven by ATP hydrolysis. F-DHPE is easily labeled to the outer surface of chromatophores. In the range of pH 7.

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