ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions - Test2 - elhamkhani - TriplyDB

ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions

ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions

http://www.wikidata.org/entity/Q25255830

about

PRIDB: a Protein-RNA interface database A backbone-based theory of protein folding Protein stability: computation, sequence statistics, and new experimental methods Merging molecular mechanism and evolution: theory and computation at the interface of biophysics and evolutionary population genetics Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins Highly accurate sequence-based prediction of half-sphere exposures of amino acid residues in proteins Thermodynamics of neutral protein evolution Kinetic Characterization of 100 Glycoside Hydrolase Mutants Enables the Discovery of Structural Features Correlated with Kinetic Constants Variation Ontology for annotation of variation effects and mechanisms Bioinformatics for personal genome interpretation mCSM-lig: quantifying the effects of mutations on protein-small molecule affinity in genetic disease and emergence of drug resistance A Web Resource for Standardized Benchmark Datasets, Metrics, and Rosetta Protocols for Macromolecular Modeling and Design Modeling protein-peptide recognition based on classical quantitative structure-affinity relationship approach: implication for proteome-wide inference of peptide-mediated interactions.Thermal stability and kinetic constants for 129 variants of a family 1 glycoside hydrolase reveal that enzyme activity and stability can be separately designed Analysis of the unique structural and physicochemical properties of the DraD/AfaD invasin in the context of its belonging to the family of chaperone/usher type fimbrial subunits.The evolution of protein structures and structural ensembles under functional constraint.Mutatomics analysis of the systematic thermostability profile of Bacillus subtilis lipase A.Platinum: a database of experimentally measured effects of mutations on structurally defined protein-ligand complexes.Testing the Coulomb/Accessible Surface Area solvent model for protein stability, ligand binding, and protein design.A three-state prediction of single point mutations on protein stability changes.Improvisation in evolution of genes and genomes: whose structure is it anyway?SPROUTS: a database for the evaluation of protein stability upon point mutation.INPS: predicting the impact of non-synonymous variations on protein stability from sequence.Computational approaches to study the effects of small genomic variations.A model for protein sequence evolution based on selective pressure for protein stability: application to hemoglobins Predicting protein thermal stability changes upon point mutations using statistical potentials: Introducing HoTMuSiC.STRUM: structure-based prediction of protein stability changes upon single-point mutation.Large scale analysis of protein stability in OMIM disease related human protein variants The Mutational Landscape of the Oncogenic MZF1 SCAN Domain in Cancer.In Silico Analysis of the deleterious nsSNP's (missense) in the Homeobox domain of human HOXB13 gene responsible for hereditary prostate cancer.Role of conformational sampling in computing mutation-induced changes in protein structure and stability Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.mCSM-NA: predicting the effects of mutations on protein-nucleic acids interactions.NewProt - a protein engineering portal.Fast side chain replacement in proteins using a coarse-grained approach for evaluating the effects of mutation during evolution.Effects of point mutations on protein structure are nonexponentially distributed.Predict impact of single amino acid change upon protein structure.Using rigidity analysis to probe mutation-induced structural changes in proteins.Sequence-only evolutionary and predicted structural features for the prediction of stability changes in protein mutants.Protein-DNA docking with a coarse-grained force field.

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P2860

ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions

http://www.wikidata.org/entity/Q25255830

description

2006 nî lūn-bûn

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2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2006 թվականի հունվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

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P356

P1433

Nucleic Acids Research

P1476

ProTherm and ProNIT: thermodyn ...... tein-nucleic acid interactions

@en

P2093

Akinori Sarai

http://www.w3.org/2001/XMLSchema#string

Hatsuho Uedaira

http://www.w3.org/2001/XMLSchema#string

K Abdulla Bava

http://www.w3.org/2001/XMLSchema#string

Koji Kitajima

http://www.w3.org/2001/XMLSchema#string

M D Shaji Kumar

http://www.w3.org/2001/XMLSchema#string

Ponraj Prabakaran

http://www.w3.org/2001/XMLSchema#string

P2860

The Protein Data Bank

The Diamond STING server

The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003

ProTherm, version 4.0: thermodynamic database for proteins and mutants

The Protein Information Resource.

Thermodynamic databases for proteins and protein-nucleic acid interactions.

ProTherm, Thermodynamic Database for Proteins and Mutants: developments in version 3.0.

ProTherm: Thermodynamic Database for Proteins and Mutants.

The Nucleic Acid Database: A resource for nucleic acid science.

Thermodynamic database for protein-nucleic acid interactions (ProNIT).

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D204-6

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scholarly article

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189295

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10.1093/NAR/GKJ103

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P433

Database issue

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34

http://www.w3.org/2001/XMLSchema#string

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M Michael Gromiha

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2006-01-01T00:00:00Z

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7389276

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16381846

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1347465

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