Fluorescence detection for the XLI analytical ultracentrifuge.
about
Investigation of stable and transient protein-protein interactions: Past, present, and futureThe DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc FingerSubunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromersStructural Basis for the Oligomerization-State Switch from a Dimer to a Trimer of an Engineered Cortexillin-1 Coiled-Coil VariantInvestigation of beta-carotene-gelatin composite particles with a multiwavelength UV/vis detector for the analytical ultracentrifuge.Are fluorescence-detected sedimentation velocity data reliable?Sedimentation equilibrium of a small oligomer-forming membrane protein: effect of histidine protonation on pentameric stabilityConservation of DNA-binding specificity and oligomerisation properties within the p53 family.The Open AUC Project.Analytical ultracentrifugation with fluorescence detection system reveals differences in complex formation between recombinant human TNF and different biological TNF antagonists in various environments.Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool.An equilibrium model for linear and closed-loop amyloid fibril formation.Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocityThe modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugationEnergetics of SecA dimerization.Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Tools for the quantitative analysis of sedimentation boundaries detected by fluorescence optical analytical ultracentrifugationAnalysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations.A histogram approach to the quality of fit in sedimentation velocity analyses.Identification of a hypochlorite-specific transcription factor from Escherichia coli.Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.Stoichiometry and Change of the mRNA Closed-Loop Factors as Translating Ribosomes Transit from Initiation to Elongation.Detection of high-molecular-weight amyloid serum protein complexes using biological on-line tracer sedimentation.Methods for the design and analysis of sedimentation velocity and sedimentation equilibrium experiments with proteinsCharacterization of conformational changes and protein-protein interactions of rod photoreceptor phosphodiesterase (PDE6).3D-Printing for Analytical UltracentrifugationEDTA aggregates induce SYPRO orange-based fluorescence in thermal shift assay.Studying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.Monochromatic multicomponent fluorescence sedimentation velocity for the study of high-affinity protein interactions.EGFP oligomers as natural fluorescence and hydrodynamic standards.Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium.Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external referencesMultiple discrete soluble aggregates influence polyglutamine toxicity in a Huntington's disease model systemAnalysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic controlAnalysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity.Histidine-tag-directed chromophores for tracer analyses in the analytical ultracentrifugeBinding of MetJ repressor to specific and nonspecific DNA and effect of S-adenosylmethionine on these interactions.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Assessment and significance of protein-protein interactions during development of protein biopharmaceuticals.
P2860
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P2860
Fluorescence detection for the XLI analytical ultracentrifuge.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Fluorescence detection for the XLI analytical ultracentrifuge.
@ast
Fluorescence detection for the XLI analytical ultracentrifuge.
@en
type
label
Fluorescence detection for the XLI analytical ultracentrifuge.
@ast
Fluorescence detection for the XLI analytical ultracentrifuge.
@en
prefLabel
Fluorescence detection for the XLI analytical ultracentrifuge.
@ast
Fluorescence detection for the XLI analytical ultracentrifuge.
@en
P2093
P1476
Fluorescence detection for the XLI analytical ultracentrifuge.
@en
P2093
Arthur L Anderson
Ian K MacGregor
Thomas M Laue
P304
P356
10.1016/J.BPC.2003.10.018
P577
2004-03-01T00:00:00Z