Elucidating protein binding mechanisms by variable-c ITC. - Wikidata - awgldk - TriplyDB

Elucidating protein binding mechanisms by variable-c ITC.

Elucidating protein binding mechanisms by variable-c ITC.

http://www.wikidata.org/entity/Q35206507

about

NMR insights into protein allostery Fitting two- and three-site binding models to isothermal titration calorimetric data.Integration and global analysis of isothermal titration calorimetry data for studying macromolecular interactions.Van't Hoff global analyses of variable temperature isothermal titration calorimetry data.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Collecting variable-concentration isothermal titration calorimetry datasets in order to determine binding mechanisms SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism.Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Understanding and overcoming aminoglycoside resistance caused by N-6'-acetyltransferase.A cooperative-binding split aptamer assay for rapid, specific and ultra-sensitive fluorescence detection of cocaine in saliva.Survey of the year 2009: applications of isothermal titration calorimetry.Salt-mediated two-site ligand binding by the cocaine-binding aptamer.Global ITC fitting methods in studies of protein allostery.Interactions of cisplatin analogues with lysozyme: a comparative analysis.Bacterial Thymidylate Synthase Binds Two Molecules of Substrate and Cofactor without Cooperativity.Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme.High-precision, automated integration of multiple isothermal titration calorimetric thermograms: new features of NITPIC Preferential binding of K+ ions in the selectivity filter at equilibrium explains high selectivity of K+ channels.Calmodulin regulates Cav3 T-type channels at their gating brake.Ion Binding to Transport Proteins using Isothermal Titration Calorimetry.G-Quadruplex-Forming DNA Aptamers Inhibit the DNA-Binding Function of HupB and Mycobacteriumtuberculosis Entry into Host Cells

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Elucidating protein binding mechanisms by variable-c ITC.

http://www.wikidata.org/entity/Q35206507

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

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2009年論文

@zh-hk

2009年論文

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2009年論文

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2009年论文

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name

Elucidating protein binding mechanisms by variable-c ITC.

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Elucidating protein binding mechanisms by variable-c ITC.

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Elucidating protein binding mechanisms by variable-c ITC.

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Elucidating protein binding mechanisms by variable-c ITC.

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Elucidating protein binding mechanisms by variable-c ITC.

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Anthony K Mittermaier

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Karine Auclair

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Lee A Freiburger

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P2860

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

Estimation of parvalbumin Ca(2+)- and Mg(2+)-binding constants by global least-squares analysis of isothermal titration calorimetry data.

Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: application to adaptor protein complexes in cell signaling.

Direct measurement of protein binding energetics by isothermal titration calorimetry.

Allostery and cooperativity revisited.

Overexpression and characterization of the chromosomal aminoglycoside 6'-N-acetyltransferase from Enterococcus faecium.

A survey of the year 2007 literature on applications of isothermal titration calorimetry.

Kinetic mechanism of the GCN5-related chromosomal aminoglycoside acetyltransferase AAC(6')-Ii from Enterococcus faecium: evidence of dimer subunit cooperativity.

Isothermal titration calorimetry: general formalism using binding polynomials.

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2871-2873

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scholarly article

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10.1002/CBIC.200900614

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18

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10

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2009-12-01T00:00:00Z

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19856370

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