Co-operativity in protein-protein association. The structure and stability of the actin filament.
about
Primary structure and domain organization of human alpha and beta adducinTau protein binds to microtubules through a flexible array of distributed weak sites3D domain swapping: a mechanism for oligomer assemblyRefined structure of dimeric diphtheria toxin at 2.0 A resolutionThe origins and evolution of freeze-etch electron microscopyThermodynamics and kinetics of actin filament nucleation.Theory of free energy and entropy in noncovalent bindingMimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels.REACH coarse-grained normal mode analysis of protein dimer interaction dynamics.Dynamic and elastic properties of F-actin: a normal-modes analysisNitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization.Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?Characterization of actin filament severing by actophorin from Acanthamoeba castellaniiSimulations of tubulin sheet polymers as possible structural intermediates in microtubule assembly.Functional consequences of actin nitration: in vitro and in disease states.Towards understanding the mechanisms of molecular recognition by computer simulations of ligand-protein interactions.A cooperative model for receptor recognition and cell adhesion: evidence from the molecular packing in the 1.6-A crystal structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi.Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.The statistical-thermodynamic basis for computation of binding affinities: a critical reviewThermodynamic and structural analysis of microtubule assembly: the role of GTP hydrolysis.Dynamic instability of microtubules: Monte Carlo simulation and application to different types of microtubule lattice.Estimates of lateral and longitudinal bond energies within the microtubule lattice.Annealing accounts for the length of actin filaments formed by spontaneous polymerization.A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.A molecular-mechanical model of the microtubuleATP hydrolysis stimulates large length fluctuations in single actin filamentsA comprehensive examination of the contributions to the binding entropy of protein-ligand complexes.Domain swapping: entangling alliances between proteins.Fragmentation is crucial for the steady-state dynamics of actin filaments.Tension management in the kinetochore.Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectinSynaptotagmin C2A loop 2 mediates Ca2+-dependent SNARE interactions essential for Ca2+-triggered vesicle exocytosisCell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response.A mechanochemical model of actin filamentsModels of the collective behavior of proteins in cells: tubulin, actin and motor proteins.A preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor designRigidity of microtubules is increased by stabilizing agents.Kinetics of protein-protein association explained by Brownian dynamics computer simulation.Modeling the physics of FtsZ assembly and force generation.On the binding affinity of macromolecular interactions: daring to ask why proteins interact.
P2860
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P2860
Co-operativity in protein-protein association. The structure and stability of the actin filament.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Co-operativity in protein-prot ...... ability of the actin filament.
@en
Co-operativity in protein-prot ...... ability of the actin filament.
@nl
type
label
Co-operativity in protein-prot ...... ability of the actin filament.
@en
Co-operativity in protein-prot ...... ability of the actin filament.
@nl
prefLabel
Co-operativity in protein-prot ...... ability of the actin filament.
@en
Co-operativity in protein-prot ...... ability of the actin filament.
@nl
P1476
Co-operativity in protein-prot ...... ability of the actin filament.
@en
P2093
Erickson HP
P304
P356
10.1016/0022-2836(89)90494-4
P407
P577
1989-04-01T00:00:00Z