Matrix asher software

Sign In. Advanced Search. Search Menu. Article Navigation. Close mobile search navigation Article Navigation. Volume Article Contents Abstract. Pires , Douglas E. Oxford Academic. David B. Tom L. Associate Editor: Alfanso Valencia. Revision received:. Cite Cite Douglas E. Select Format Select format. Permissions Icon Permissions. Abstract Motivation: Mutations play fundamental roles in evolution by introducing diversity into genomes.

Open in new tab Download slide. Table 1. Data set. Protein stability change S Regression 5-fold cross-validation Dehouck et al. Open in new tab. The second set of experiments aims to assess the performance of mCSM signatures in predicting the impact of mutations on affinity of protein—protein complexes, in both regression and classification tasks i.

Table 2. Comparative regression experiments using the S data set. Number of predictions. Automute 0. Google Scholar Crossref. Search ADS. Protein—DNA interactions: structural, thermodynamic and clustering patterns of conserved residues in DNA-binding proteins.

Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains. Targeted rescue of a destabilized mutant of p53 by an in silico screened drug. Large-scale prediction of protein geometry and stability changes for arbitrary single point mutations. Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound.

Improving the prediction of disease-related variants using protein three-dimensional structure. Predicting protein stability changes from sequences using support vector machines. Residue depth: a novel parameter for the analysis of protein structure and stability. Prediction of protein stability changes for single-site mutations using support vector machines. Prediction by graph theoretic measures of structural effects in proteins arising from non-synonymous single nucleotide polymorphisms.

Protein cutoff scanning: a comparative analysis of cutoff dependent and cutoff free methods for prospecting contacts in proteins. Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC BeAtMuSiC: prediction of changes in protein-protein binding affinity on mutations.

Dissection of the structure and activity of the tyrosyl-trna synthetase by site-directed mutagenesis. Predicting changes in the stability of proteins and protein complexes: a study of more than mutations. Small peptides activate the latent sequence-specific DNA binding function of p Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Role of conformational sampling in computing mutation-induced changes in protein structure and stability.

A simple physical model for binding energy hot spots in protein—protein complexes. Protherm and pronit: thermodynamic databases for proteins and protein—nucleic acid interactions. Targeting p53 in vivo: A first-in-human study with ptargeting compound apr in refractory hematologic malignancies and prostate cancer.

Accurate prediction of stability changes in protein mutants by combining machine learning with structure based computational mutagenesis. SKEMPI: a structural kinetic and energetic database of mutant protein interactions and its use in empirical models. Protein—protein binding affinity prediction on a diverse set of structures. SCOP: a structural classification of proteins database for the investigation of sequences and structures.

Google Scholar PubMed. Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. The iarc tp53 database: new online mutation analysis and recommendations to users.

Cutoff Scanning Matrix CSM : structural classification and function prediction by protein inter-residue distance patterns. Reactivation of mutant p53 through interaction of a c-terminal peptide with the core domain. Predicting changes in protein thermostability brought about by single-or multi-site mutations.

Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables. SDM — a server for predicting effects of mutations on protein stability and malfunction. These benefits are coupled with exceptional reliability proven in more than System One installations worldwide. The Matrix Model is available free-standing as shown here or in a through-the-wall configuration. Controlled Resist Removal. High Throughput.

Photocell Endpoint Automatic endpoint detection for optimizing throughput. Please contact us for more information on the product:. All the Matrix Plasma Asher Plasma Descum semiconductor process equipment trademarks belongs to Matrix Integrated Systems, Inc , the original equipment manufacturer. All rights reserved. Please contact us to check the availability of the following Plasma Asher equipment. They are only for end user.

They are subject to prior sale without notice. Perkin-ELmer L. Matrix Category: Asher Tag: Matrix. Wafer Size: 6 inch configuration. Lead Time : 4 weeks after payment Warranty : 6 months non-consumable parts. Installation and training : Available at extra charge Service Contract : Available at extra charge Matrix plasma Asher Plasma descum semiconductor equipment General Description The Matrix plasma Asher Plasma descum semiconductor equipment represents the Industry Standard in single-wafer photoresist removal and the mainstay of the highly successful System One family.

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