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custom made matlab software  (MathWorks Inc)


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    MathWorks Inc custom made matlab software
    Custom Made Matlab Software, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 96/100, based on 334 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/data+fitting+software+origin(pro)+version+2016/MATLAB+Compiler/pm40320555-98-9-10
    Average 96 stars, based on 334 article reviews
    custom made matlab software - by Bioz Stars, 2026-11
    96/100 stars

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    other:

    Article Title: An Integrated Framework for Automated Image Segmentation and Personalized Wall Stress Estimation of Abdominal Aortic Aneurysms.
    Article Snippet: The script can be compiled into a standalone executable (e.g., via MATLAB Compiler) that runs with the free MATLAB Runtime, so end users do not require a MATLAB license [45].

    Article Title: Autophagy dysfunction in iPSCs-derived neurons and midbrain organoids carrying a SNCA triplication.
    Article Snippet: Neural stat compiler files were used for data analysis in MATLAB.

    Article Title: Field Resistance to Powdery Mildew in Lycium barbarum Germplasm, Associated Leaf Anatomical Traits, and Temporal Physiological Responses in Ningqi-1
    Article Snippet: Nonlinear fitting of the continuously monitored disease index (DI) data was performed using MATLAB Compiler Runtime 8.3 (R2014a; The MathWorks, Inc., Natick, MA, USA) with four sigmoidal equations: (1) logistic(x) = (A1 − A2)/(1 + (x/x0)p) + A2; (2) slogistic1(x) = a/(1 + exp(−k × (x − xc))); (3) slogistic2(x) = a/(1 + ((a − y0)/y0) × exp(−4 × Wmax × x/a)); and (4) slogistic3(x) = a/(1 + b × exp(−k × x)).

    Generated:

    Article Title: WAH- i : Optimising Microphone Array Geometry for Customised Localisation Accuracy
    Article Snippet: .. To support deployment beyond a MATLAB development environment, standalone executables were generated using the MATLAB Compiler ( ). ..

    Analysis:

    Article Title: Thiolactone ring dynamics in dimeric lipids enable pH-switchable supramolecular tuning in surface-engineered quantum dots.
    Article Snippet: aSchool of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation of Science, Kolkata 700032, India.. bDepartment of Chemical Sciences, Indian Institute of Science Education and Research Berhampur, Ganjam, Odisha 760003, India cSchool of Materials Sciences, Indian Association for the Cultivation of Science, Kolkata 700032, India.. dDepartment of Organic Chemistry, Indian Institute of Science, Bangalore 560012, India.

    Software:

    Article Title: Thiolactone ring dynamics in dimeric lipids enable pH-switchable supramolecular tuning in surface-engineered quantum dots.
    Article Snippet: aSchool of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation of Science, Kolkata 700032, India.. bDepartment of Chemical Sciences, Indian Institute of Science Education and Research Berhampur, Ganjam, Odisha 760003, India cSchool of Materials Sciences, Indian Association for the Cultivation of Science, Kolkata 700032, India.. dDepartment of Organic Chemistry, Indian Institute of Science, Bangalore 560012, India.



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    data fitting software origin(pro) version 2016  (OriginLab corp)
    90
    OriginLab corp data fitting software origin(pro) version 2016
    a Simplified representation of the 70S ribosome with the AMK binding site indicated with the blue star. b The unbiased ( F o – F c ) difference electron density map of AMK bound near the decoding center is contoured at 2.3σ. c AMK binds within helix h44 of the decoding center where the AHB moiety forms three unique interactions. d Time courses of f[ 3 H]Met-Phe-Phe tripeptide formation with EF-Tu ternary complex (TC) (5 μM) and EF-G (5 µM) in the absence (black) and presence of 20 μM AMK (red). Solid lines represent the double exponential fit of the data with SEM from n = 3 independent experiments. e Time evolution of fluorescence traces obtained for the EF-G (5 μM) catalyzed movement of pyrene-labeled mRNA on 70S ribosomes (0.5 μM) in the presence of various concentrations (0-5 µM) of AMK. The inhibition of mRNA movement by AMK was estimated from amplitudes of the slow phase of fluorescence traces relative to the total transition (normalized to 1) indicative of inhibited fraction of the ribosomes. f The fraction of AMK-inhibited pre-TC plotted against AMK concentration. Data were fitted with hyperbolic function (solid line) and half-inhibitory concentration ( K I ) of AMK on the inhibition of translocation was estimated from mid-point of transition. Experiments were conducted in <t>triplicates</t> and error bars indicate the SEM of data.
    Data Fitting Software Origin(pro) Version 2016, supplied by OriginLab corp, 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/data+fitting+software+origin(pro)+version+2016/curve+fitting+software+origin+8+0/pmc10400623-114-4-12
    Average 90 stars, based on 1 article reviews
    data fitting software origin(pro) version 2016 - by Bioz Stars, 2026-11
    90/100 stars
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    a Simplified representation of the 70S ribosome with the AMK binding site indicated with the blue star. b The unbiased ( F o – F c ) difference electron density map of AMK bound near the decoding center is contoured at 2.3σ. c AMK binds within helix h44 of the decoding center where the AHB moiety forms three unique interactions. d Time courses of f[ 3 H]Met-Phe-Phe tripeptide formation with EF-Tu ternary complex (TC) (5 μM) and EF-G (5 µM) in the absence (black) and presence of 20 μM AMK (red). Solid lines represent the double exponential fit of the data with SEM from n = 3 independent experiments. e Time evolution of fluorescence traces obtained for the EF-G (5 μM) catalyzed movement of pyrene-labeled mRNA on 70S ribosomes (0.5 μM) in the presence of various concentrations (0-5 µM) of AMK. The inhibition of mRNA movement by AMK was estimated from amplitudes of the slow phase of fluorescence traces relative to the total transition (normalized to 1) indicative of inhibited fraction of the ribosomes. f The fraction of AMK-inhibited pre-TC plotted against AMK concentration. Data were fitted with hyperbolic function (solid line) and half-inhibitory concentration ( K I ) of AMK on the inhibition of translocation was estimated from mid-point of transition. Experiments were conducted in triplicates and error bars indicate the SEM of data.

    Journal: Nature Communications

    Article Title: Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome

    doi: 10.1038/s41467-023-40416-5

    Figure Lengend Snippet: a Simplified representation of the 70S ribosome with the AMK binding site indicated with the blue star. b The unbiased ( F o – F c ) difference electron density map of AMK bound near the decoding center is contoured at 2.3σ. c AMK binds within helix h44 of the decoding center where the AHB moiety forms three unique interactions. d Time courses of f[ 3 H]Met-Phe-Phe tripeptide formation with EF-Tu ternary complex (TC) (5 μM) and EF-G (5 µM) in the absence (black) and presence of 20 μM AMK (red). Solid lines represent the double exponential fit of the data with SEM from n = 3 independent experiments. e Time evolution of fluorescence traces obtained for the EF-G (5 μM) catalyzed movement of pyrene-labeled mRNA on 70S ribosomes (0.5 μM) in the presence of various concentrations (0-5 µM) of AMK. The inhibition of mRNA movement by AMK was estimated from amplitudes of the slow phase of fluorescence traces relative to the total transition (normalized to 1) indicative of inhibited fraction of the ribosomes. f The fraction of AMK-inhibited pre-TC plotted against AMK concentration. Data were fitted with hyperbolic function (solid line) and half-inhibitory concentration ( K I ) of AMK on the inhibition of translocation was estimated from mid-point of transition. Experiments were conducted in triplicates and error bars indicate the SEM of data.

    Article Snippet: Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Techniques: Binding Assay, Fluorescence, Labeling, Inhibition, Concentration Assay, Translocation Assay

    a Time courses of BOP-Met-Phe-Leu release from the P site of the ribosomes in pre-TC (0.1 μM) upon mixing with RF2 (1 μM) in the presence of various concentrations of AMK (0-1 μM). The near monophasic curves are fitted with double exponential function (solid lines) and the rates and amplitudes of the predominant fast phase (> 99%) were determined. The fraction inhibited was estimated from the fractional loss in fluorescence amplitude for a given AMK concentration considering the total amplitude of fluorescence transition (without AMK) as 1. b Fraction inhibition of RF2-mediated peptide release as the function of increasing concentrations of AMK. Solid line is the hyperbolic fit of data from which half-maximal inhibitory concentration ( K I ) of AMK for peptide release was estimated. c Time tra c es for Rayleigh light scattering upon splitting of post-TC ribosomes (0.5 μM) into subunits by the concerted action of RRF (20 μM) and EF-G (10 μM) in the presence of various concentrations of AMK (0–20 μM). The scattering traces were fitted with double exponential function and the rates and amplitudes of both the fast and slow phases were determined. d Fraction inhibition of RRF and EF-G-mediated ribosome splitting was estimated from the fractional loss of the amplitude of the fast phase considering amplitude of the entire transition without AMK as 1. The solid line represents the hyperbolic fit of the fraction inhibition plotted against AMK concentration from which the half-maximal concentration ( K I ) of AMK to inhibit ribosome recycling was estimated. Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Journal: Nature Communications

    Article Title: Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome

    doi: 10.1038/s41467-023-40416-5

    Figure Lengend Snippet: a Time courses of BOP-Met-Phe-Leu release from the P site of the ribosomes in pre-TC (0.1 μM) upon mixing with RF2 (1 μM) in the presence of various concentrations of AMK (0-1 μM). The near monophasic curves are fitted with double exponential function (solid lines) and the rates and amplitudes of the predominant fast phase (> 99%) were determined. The fraction inhibited was estimated from the fractional loss in fluorescence amplitude for a given AMK concentration considering the total amplitude of fluorescence transition (without AMK) as 1. b Fraction inhibition of RF2-mediated peptide release as the function of increasing concentrations of AMK. Solid line is the hyperbolic fit of data from which half-maximal inhibitory concentration ( K I ) of AMK for peptide release was estimated. c Time tra c es for Rayleigh light scattering upon splitting of post-TC ribosomes (0.5 μM) into subunits by the concerted action of RRF (20 μM) and EF-G (10 μM) in the presence of various concentrations of AMK (0–20 μM). The scattering traces were fitted with double exponential function and the rates and amplitudes of both the fast and slow phases were determined. d Fraction inhibition of RRF and EF-G-mediated ribosome splitting was estimated from the fractional loss of the amplitude of the fast phase considering amplitude of the entire transition without AMK as 1. The solid line represents the hyperbolic fit of the fraction inhibition plotted against AMK concentration from which the half-maximal concentration ( K I ) of AMK to inhibit ribosome recycling was estimated. Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Article Snippet: Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Techniques: Fluorescence, Concentration Assay, Inhibition