Free-solution, label-free protein-protein interactions characterized by dynamic light scattering
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Inhibition of influenza virus replication via small molecules that induce the formation of higher-order nucleoprotein oligomersComputing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs.Engineering potent long-acting variants of the Wnt inhibitor DKK2Selecting temperature for protein crystallization screens using the temperature dependence of the second virial coefficientMicroscale thermophoresis quantifies biomolecular interactions under previously challenging conditionsThe analysis of macromolecular interactions by sedimentation equilibriumThe molecular mechanism of nuclear transport revealed by atomic-scale measurements.pH-sensitive self-associations of the N-terminal domain of NBCe1-A suggest a compact conformation under acidic intracellular conditions.Gremlin-1 is an inhibitor of macrophage migration inhibitory factor and attenuates atherosclerotic plaque growth in ApoE-/- Mice.Effects of an anticarcinogenic Bowman-Birk protease inhibitor on purified 20S proteasome and MCF-7 breast cancer cells.The multifunctional role of the pallilysin-associated Treponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradationCalcium-dependent stoichiometries of the KCa2.2 (SK) intracellular domain/calmodulin complex in solution.Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches.Light-scattering-based analysis of biomolecular interactions.Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.Inducing protein aggregation by extensional flow.Investigating the Role of Artemin Glycosylation.Measuring the effect of ligand binding on the interface stability of multimeric proteins using dynamic light scattering.Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameterTheoretical study of interactions of BSA protein in a NaCl aqueous solution.Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.Radiation-induced conformational changes in chromatin structure in resting human peripheral blood mononuclear cells.Examination and optimization of the self-assembly of biocompatible, polymeric nanoparticles by high-throughput nanoprecipitation
P2860
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P2860
Free-solution, label-free protein-protein interactions characterized by dynamic light scattering
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Free-solution, label-free prot ...... ed by dynamic light scattering
@ast
Free-solution, label-free prot ...... ed by dynamic light scattering
@en
Free-solution, label-free prot ...... ed by dynamic light scattering
@nl
type
label
Free-solution, label-free prot ...... ed by dynamic light scattering
@ast
Free-solution, label-free prot ...... ed by dynamic light scattering
@en
Free-solution, label-free prot ...... ed by dynamic light scattering
@nl
prefLabel
Free-solution, label-free prot ...... ed by dynamic light scattering
@ast
Free-solution, label-free prot ...... ed by dynamic light scattering
@en
Free-solution, label-free prot ...... ed by dynamic light scattering
@nl
P2093
P2860
P1433
P1476
Free-solution, label-free prot ...... ed by dynamic light scattering
@en
P2093
Amy D Hanlon
Michael I Larkin
Ryan M Reddick
P2860
P304
P356
10.1016/J.BPJ.2009.09.061
P407
P577
2010-01-20T00:00:00Z