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finite element software package comsol multiphysics version 4.4  (COMSOL Inc)

 
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    Structured Review

    COMSOL Inc finite element software package comsol multiphysics version 4.4
    Finite Element Software Package Comsol Multiphysics Version 4.4, supplied by COMSOL Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fret+software+package/comsol+multiphysics/us09370765-34-14-18
    Average 90 stars, based on 1 article reviews
    finite element software package comsol multiphysics version 4.4 - by Bioz Stars, 2026-10
    90/100 stars

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    Article Title: Numerical simulation of a continuous sonoreactor for cotton cellulose residues recovery
    Article Snippet: First, there was a ramp for 120 s at a shear rate of 1 s −1 , followed by an increase in the shear rate to 500 s −1 in 10 steps over 10 min. COMSOL Multiphysics employed the values we measured ( ) for the numerical simulations.

    Article Title: Dummy molecularly imprinted polymer nanochannel sensor for ultrasensitive detection of aniline compounds.
    Article Snippet: Aniline pollutants can cause great harm to human health and the ecosystem, while rapid and selective quantification of aniline compounds in environment samples at trace levels is a highly complex target.. In this study, a novel, efficient nanochannel sensor based on dummy molecularly imprinted polymer (DMIP) was fabricated.. The sensor works on the principle of the ion current rectification across the asymmetric charged nanoporous capillary.

    Article Title: Three-dimensional urchin-like K 2 Ti 8 O 17 / Ag NPs composite as a SERS substrate for detecting folic acid and thiram.
    Article Snippet: The three-dimensional (3D) semiconductor/noble metal composite substrates for surface-enhanced Raman scattering (SERS) have garnered increasing interest due to their excellent optical and chemical properties, as well as the capacity to trigger both electromagnetic mechanism (EM) and chemical mechanism (CM) simultaneously.. In this work, a facile 3D urchin-like K2Ti8O17/Ag nanoparticles (Ag NPs) composite substrate is designed for multi-purpose SERS sensing.. K2Ti8O17, as a dielectric medium, improves the electric field environment around Ag NPs, which is consistent with finite-different time domain (FDTD) results, and enhances the SERS performance of the K2Ti8O17/Ag composite substrate.

    Article Title: Cellulose-based bipolar heterogeneous membranes with two-dimensional lamellar composite three-dimensional network structure for osmotic energy conversion.
    Article Snippet: Reverse electrodialysis (RED) technology is extremely promising in harvesting osmotic energy.. The exchange membranes, which are the core components of RED systems, especially in the investigation of composite membrane systems, remain a challenge by balancing the key requirements of better compatibility and sufficient stability, ease of fabrication, etc.. In view of the excellent compatibility and stability of forest biomass membrane materials, this work reports a two-dimensional (2D) lamellar regenerated cellulose (RC) composite with a threedimensional (3D) network of bacterial cellulose membrane doped with alkali lignin (BC-AL) heterogeneous membrane.

    Software:

    Article Title: Long-Term Colloidal Stability of Cobalt Ferrite Nanoparticles in Magnetic Fluids: A Nine-Year Study
    Article Snippet: • Synthesis of magnetic fluids based on highly dispersible CoFe2O4 coated with oleic acid.. • Rheology and viscosity measurements of the magnetic fluids showed Newtonian

    Article Title: Metal-Support Interaction and Tip-Enhanced Electric Field Effect Co-Enhancing Oxygen Species Adsorption/Enrichment for Efficient Electrooxidation of Plastic Waste Derived Alcohol into Glycolic Acid
    Article Snippet: The limited catalytic activity and weaker stability caused by the restricted adsorption capacity of reactive oxygen species (*OH) have hindered the further development of electrocatalytic upgrading polyethylene terephthalate (PET) waste into valuable C2 chemicals, which is crucial in addressing the plastic pollution issue.. Herein, Pd@Ni (OH)2-NiO catalyst was synthesized based on the concepts of metal-support interaction and tip-enhanced electric field effect, demonstrating remarkable activity (0.60 V vs. RHE, 300 mA cm 2) and stability (250 h) for electrocatalytic upgrading PET plastic waste into glycolic acid.. A significant charge transfer occurs between metal Pd and supports Ni(OH)2-NiO due to the metal-support interaction, generating the electron-deficient Pdδ+ sites.

    Article Title: Electropolishing of nonplanar surface of a Zr-based bulk metallic glass in NaCl-ethylene glycol electrolyte through a planar cathode
    Article Snippet: Bulk metallic glasses (BMGs) have been widely used in precise manufacturing industry, and their surface quality is one of the key properties for practical applications.. Electropolishing (EP) is an effective technique to improve surface roughness for metal materials with good precision and no tool wear.. In this work, the feasibility of electropolishing nonplanar surfaces with planar electrode is verified by multi-physics simulation.



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    Domain mapping of the interaction between MCU and Miro1. A, Mutations on the dime motif of MCU (257EYSW260 to 257AAAA260 or 261DIME264 to 261AAAA264) did not affect the interaction between MCU and Miro1. B, MCU did not interact with Myc-Miro1 without transmembrane domain, but still immunoprecipitated Myc-Miro1 lacking 3 aa (616KQR618). C, <t>FRET</t> <t>analysis</t> of Myc-Miro1 and Flag-MCU showed a significantly higher FRET efficiency compared with that of TOMM20-Myc and Flag-MCU. Mutation on the dime motif of MCU (257EYSW260 to 257AAAA260) did not affect Myc-Miro1 binding, while elimination of MCU's N-terminal domain [Flag-MCU(Δ2–57)] or adding Ca2+ significantly reduced interaction with Myc-Miro1. N = Flag-MCU + TOMM20-Myc: 72 mitochondria. Flag-MCU + Myc-Miro1: 78 mitochondria, Flag-MCU (257EYSW260 to 257AAAA260) + Myc-Miro1: 25 mitochondria, Flag-MCU(Δ2–57) + Myc-Miro1: 23 mitochondria. Scale bar, 1 μm. *p < 0.0001. Tukey's box plot profile is shown. D, Ca2+ elevation alters MCU–Miro1 interaction. MCU expression vector dually tagged in the N-terminus (Flag) and the C-terminus (sfGFP), respectively, was prepared and used to investigate localization of these tags after treating cells with 2 μm ionomycin for 10 min. The R2 correlation between Flag and sfGFP was compared between paired samples with or without addition of 2 μm ionomycin. N = 5 experiments, *p = 0.0171. E, HEK cells transfected with MCU-Flag were treated with 2 μm ionomycin as shown above and then blotted for Flag. Graph shows the ratio of the full-length MCU band (top band) to the processed MCU (bottom band). N = 7 experiments, **p = 0.0094. Tukey's boxplot profile is shown.
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    Domain mapping of the interaction between MCU and Miro1. A, Mutations on the dime motif of MCU (257EYSW260 to 257AAAA260 or 261DIME264 to 261AAAA264) did not affect the interaction between MCU and Miro1. B, MCU did not interact with Myc-Miro1 without transmembrane domain, but still immunoprecipitated Myc-Miro1 lacking 3 aa (616KQR618). C, <t>FRET</t> <t>analysis</t> of Myc-Miro1 and Flag-MCU showed a significantly higher FRET efficiency compared with that of TOMM20-Myc and Flag-MCU. Mutation on the dime motif of MCU (257EYSW260 to 257AAAA260) did not affect Myc-Miro1 binding, while elimination of MCU's N-terminal domain [Flag-MCU(Δ2–57)] or adding Ca2+ significantly reduced interaction with Myc-Miro1. N = Flag-MCU + TOMM20-Myc: 72 mitochondria. Flag-MCU + Myc-Miro1: 78 mitochondria, Flag-MCU (257EYSW260 to 257AAAA260) + Myc-Miro1: 25 mitochondria, Flag-MCU(Δ2–57) + Myc-Miro1: 23 mitochondria. Scale bar, 1 μm. *p < 0.0001. Tukey's box plot profile is shown. D, Ca2+ elevation alters MCU–Miro1 interaction. MCU expression vector dually tagged in the N-terminus (Flag) and the C-terminus (sfGFP), respectively, was prepared and used to investigate localization of these tags after treating cells with 2 μm ionomycin for 10 min. The R2 correlation between Flag and sfGFP was compared between paired samples with or without addition of 2 μm ionomycin. N = 5 experiments, *p = 0.0171. E, HEK cells transfected with MCU-Flag were treated with 2 μm ionomycin as shown above and then blotted for Flag. Graph shows the ratio of the full-length MCU band (top band) to the processed MCU (bottom band). N = 7 experiments, **p = 0.0094. Tukey's boxplot profile is shown.
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    Domain mapping of the interaction between MCU and Miro1. A, Mutations on the dime motif of MCU (257EYSW260 to 257AAAA260 or 261DIME264 to 261AAAA264) did not affect the interaction between MCU and Miro1. B, MCU did not interact with Myc-Miro1 without transmembrane domain, but still immunoprecipitated Myc-Miro1 lacking 3 aa (616KQR618). C, <t>FRET</t> <t>analysis</t> of Myc-Miro1 and Flag-MCU showed a significantly higher FRET efficiency compared with that of TOMM20-Myc and Flag-MCU. Mutation on the dime motif of MCU (257EYSW260 to 257AAAA260) did not affect Myc-Miro1 binding, while elimination of MCU's N-terminal domain [Flag-MCU(Δ2–57)] or adding Ca2+ significantly reduced interaction with Myc-Miro1. N = Flag-MCU + TOMM20-Myc: 72 mitochondria. Flag-MCU + Myc-Miro1: 78 mitochondria, Flag-MCU (257EYSW260 to 257AAAA260) + Myc-Miro1: 25 mitochondria, Flag-MCU(Δ2–57) + Myc-Miro1: 23 mitochondria. Scale bar, 1 μm. *p < 0.0001. Tukey's box plot profile is shown. D, Ca2+ elevation alters MCU–Miro1 interaction. MCU expression vector dually tagged in the N-terminus (Flag) and the C-terminus (sfGFP), respectively, was prepared and used to investigate localization of these tags after treating cells with 2 μm ionomycin for 10 min. The R2 correlation between Flag and sfGFP was compared between paired samples with or without addition of 2 μm ionomycin. N = 5 experiments, *p = 0.0171. E, HEK cells transfected with MCU-Flag were treated with 2 μm ionomycin as shown above and then blotted for Flag. Graph shows the ratio of the full-length MCU band (top band) to the processed MCU (bottom band). N = 7 experiments, **p = 0.0094. Tukey's boxplot profile is shown.
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    Domain mapping of the interaction between MCU and Miro1. A, Mutations on the dime motif of MCU (257EYSW260 to 257AAAA260 or 261DIME264 to 261AAAA264) did not affect the interaction between MCU and Miro1. B, MCU did not interact with Myc-Miro1 without transmembrane domain, but still immunoprecipitated Myc-Miro1 lacking 3 aa (616KQR618). C, <t>FRET</t> <t>analysis</t> of Myc-Miro1 and Flag-MCU showed a significantly higher FRET efficiency compared with that of TOMM20-Myc and Flag-MCU. Mutation on the dime motif of MCU (257EYSW260 to 257AAAA260) did not affect Myc-Miro1 binding, while elimination of MCU's N-terminal domain [Flag-MCU(Δ2–57)] or adding Ca2+ significantly reduced interaction with Myc-Miro1. N = Flag-MCU + TOMM20-Myc: 72 mitochondria. Flag-MCU + Myc-Miro1: 78 mitochondria, Flag-MCU (257EYSW260 to 257AAAA260) + Myc-Miro1: 25 mitochondria, Flag-MCU(Δ2–57) + Myc-Miro1: 23 mitochondria. Scale bar, 1 μm. *p < 0.0001. Tukey's box plot profile is shown. D, Ca2+ elevation alters MCU–Miro1 interaction. MCU expression vector dually tagged in the N-terminus (Flag) and the C-terminus (sfGFP), respectively, was prepared and used to investigate localization of these tags after treating cells with 2 μm ionomycin for 10 min. The R2 correlation between Flag and sfGFP was compared between paired samples with or without addition of 2 μm ionomycin. N = 5 experiments, *p = 0.0171. E, HEK cells transfected with MCU-Flag were treated with 2 μm ionomycin as shown above and then blotted for Flag. Graph shows the ratio of the full-length MCU band (top band) to the processed MCU (bottom band). N = 7 experiments, **p = 0.0094. Tukey's boxplot profile is shown.
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    Domain mapping of the interaction between MCU and Miro1. A, Mutations on the dime motif of MCU (257EYSW260 to 257AAAA260 or 261DIME264 to 261AAAA264) did not affect the interaction between MCU and Miro1. B, MCU did not interact with Myc-Miro1 without transmembrane domain, but still immunoprecipitated Myc-Miro1 lacking 3 aa (616KQR618). C, FRET analysis of Myc-Miro1 and Flag-MCU showed a significantly higher FRET efficiency compared with that of TOMM20-Myc and Flag-MCU. Mutation on the dime motif of MCU (257EYSW260 to 257AAAA260) did not affect Myc-Miro1 binding, while elimination of MCU's N-terminal domain [Flag-MCU(Δ2–57)] or adding Ca2+ significantly reduced interaction with Myc-Miro1. N = Flag-MCU + TOMM20-Myc: 72 mitochondria. Flag-MCU + Myc-Miro1: 78 mitochondria, Flag-MCU (257EYSW260 to 257AAAA260) + Myc-Miro1: 25 mitochondria, Flag-MCU(Δ2–57) + Myc-Miro1: 23 mitochondria. Scale bar, 1 μm. *p < 0.0001. Tukey's box plot profile is shown. D, Ca2+ elevation alters MCU–Miro1 interaction. MCU expression vector dually tagged in the N-terminus (Flag) and the C-terminus (sfGFP), respectively, was prepared and used to investigate localization of these tags after treating cells with 2 μm ionomycin for 10 min. The R2 correlation between Flag and sfGFP was compared between paired samples with or without addition of 2 μm ionomycin. N = 5 experiments, *p = 0.0171. E, HEK cells transfected with MCU-Flag were treated with 2 μm ionomycin as shown above and then blotted for Flag. Graph shows the ratio of the full-length MCU band (top band) to the processed MCU (bottom band). N = 7 experiments, **p = 0.0094. Tukey's boxplot profile is shown.

    Journal: The Journal of Neuroscience

    Article Title: MCU Interacts with Miro1 to Modulate Mitochondrial Functions in Neurons

    doi: 10.1523/JNEUROSCI.0504-18.2018

    Figure Lengend Snippet: Domain mapping of the interaction between MCU and Miro1. A, Mutations on the dime motif of MCU (257EYSW260 to 257AAAA260 or 261DIME264 to 261AAAA264) did not affect the interaction between MCU and Miro1. B, MCU did not interact with Myc-Miro1 without transmembrane domain, but still immunoprecipitated Myc-Miro1 lacking 3 aa (616KQR618). C, FRET analysis of Myc-Miro1 and Flag-MCU showed a significantly higher FRET efficiency compared with that of TOMM20-Myc and Flag-MCU. Mutation on the dime motif of MCU (257EYSW260 to 257AAAA260) did not affect Myc-Miro1 binding, while elimination of MCU's N-terminal domain [Flag-MCU(Δ2–57)] or adding Ca2+ significantly reduced interaction with Myc-Miro1. N = Flag-MCU + TOMM20-Myc: 72 mitochondria. Flag-MCU + Myc-Miro1: 78 mitochondria, Flag-MCU (257EYSW260 to 257AAAA260) + Myc-Miro1: 25 mitochondria, Flag-MCU(Δ2–57) + Myc-Miro1: 23 mitochondria. Scale bar, 1 μm. *p < 0.0001. Tukey's box plot profile is shown. D, Ca2+ elevation alters MCU–Miro1 interaction. MCU expression vector dually tagged in the N-terminus (Flag) and the C-terminus (sfGFP), respectively, was prepared and used to investigate localization of these tags after treating cells with 2 μm ionomycin for 10 min. The R2 correlation between Flag and sfGFP was compared between paired samples with or without addition of 2 μm ionomycin. N = 5 experiments, *p = 0.0171. E, HEK cells transfected with MCU-Flag were treated with 2 μm ionomycin as shown above and then blotted for Flag. Graph shows the ratio of the full-length MCU band (top band) to the processed MCU (bottom band). N = 7 experiments, **p = 0.0094. Tukey's boxplot profile is shown.

    Article Snippet: All FRET efficiencies were calculated and normalized using the Zeiss FRET analysis software package.

    Techniques: Immunoprecipitation, Mutagenesis, Binding Assay, Expressing, Plasmid Preparation, Transfection