Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation.
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Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domainsCooperative interactions at the SLP-76 complex are critical for actin polymerizationSubunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complexCrystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrinStathmin and Interfacial Microtubule Inhibitors Recognize a Naturally Curved Conformation of Tubulin DimersThe Cytosolic DNA Sensor cGAS Forms an Oligomeric Complex with DNA and Undergoes Switch-like Conformational Changes in the Activation LoopGMF severs actin-Arp2/3 complex branch junctions by a cofilin-like mechanism.Assembly and dynamics of the autophagy-initiating Atg1 complex.Investigation of beta-carotene-gelatin composite particles with a multiwavelength UV/vis detector for the analytical ultracentrifuge.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.alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli.Some statistical properties of differencing schemes for baseline correction of sedimentation velocity dataMechanism of interaction between single-stranded DNA binding protein and DNAStructure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complexUsing Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions.Sedimentation patterns of rapidly reversible protein interactions.Diffusion of the reaction boundary of rapidly interacting macromolecules in sedimentation velocityOn computational approaches for size-and-shape distributions from sedimentation velocity analytical ultracentrifugation.Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocitySedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)Sedimentation velocity analysis of heterogeneous protein-protein interactions: sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theoryA new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase.Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation.Multi-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes.Determination of protein complex stoichiometry through multisignal sedimentation velocity experiments.The boundary structure in the analysis of reversibly interacting systems by sedimentation velocity.Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity.On the distribution of protein refractive index increments.Arp2/3 complex is bound and activated by two WASP proteins.SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Using prior knowledge in the determination of macromolecular size-distributions by analytical ultracentrifugation.A mechanism for assembly of complexes of vitronectin and plasminogen activator inhibitor-1 from sedimentation velocity analysis.3D-Printing for Analytical UltracentrifugationSimilar enzymes, different structures: phthalate dioxygenase is an alpha3alpha3 stacked hexamer, not an alpha3beta3 trimer like "normal" Rieske oxygenasesA new adaptive grid-size algorithm for the simulation of sedimentation velocity profiles in analytical ultracentrifugationOverview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Analytical Ultracentrifugation as a Tool for Studying Protein Interactions.Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation.
P2860
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P2860
Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
name
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@ast
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@en
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@nl
type
label
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@ast
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@en
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@nl
prefLabel
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@ast
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@en
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@nl
P2093
P2860
P356
P1476
Studying multiprotein complexe ...... nalytical ultracentrifugation.
@en
P2093
Andrea Balbo
Carlos A Velikovsky
Cynthia B Peterson
Kenneth H Minor
Roy A Mariuzza
P2860
P356
10.1073/PNAS.0408399102
P407
P50
P577
2004-12-21T00:00:00Z