Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source
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The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosisStructural mass spectrometry of the alpha beta-tubulin dimer supports a revised model of microtubule assemblyBtubA-BtubB heterodimer is an essential intermediate in protofilament assemblyBacterial tubulin distinct loop sequences and primitive assembly properties support its origin from a eukaryotic tubulin ancestor.Challenges and dreams: physics of weak interactions essential to lifePhotoinduced partial unfolding of tubulin bound to meso-tetrakis(sulfonatophenyl) porphyrin leads to inhibition of microtubule formation in vitro.Tubulin binds to the cytoplasmic loop of TRESK background K⁺ channel in vitro.A survey of the year 2002 commercial optical biosensor literature.Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamicsDimeric states of neural- and epithelial-cadherins are distinguished by the rate of disassembly.Tubulin equilibrium unfolding followed by time-resolved fluorescence and fluorescence correlation spectroscopy.Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.Revisiting the tubulin cofactors and Arl2 in the regulation of soluble αβ-tubulin pools and their effect on microtubule dynamics.Tubulin-specific chaperones: components of a molecular machine that assembles the α/β heterodimer.Correct diffusion coefficients of proteins in fluorescence correlation spectroscopy. Application to tubulin oligomers induced by Mg2+ and Paclitaxel.Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.Emerging roles for tubulin folding cofactors at the centrosome.Weak protein-protein interactions in live cells are quantified by cell-volume modulation.Tubulin heterodimers remain functional for one cell cycle after the inactivation of tubulin-folding cofactor D in fission yeast cells.Axoneme specialization embedded in a "generalist" beta-tubulin.Why is the microtubule lattice helical?
P2860
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P2860
Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Dissociation of the tubulin di ...... he absence of an energy source
@ast
Dissociation of the tubulin di ...... he absence of an energy source
@en
type
label
Dissociation of the tubulin di ...... he absence of an energy source
@ast
Dissociation of the tubulin di ...... he absence of an energy source
@en
prefLabel
Dissociation of the tubulin di ...... he absence of an energy source
@ast
Dissociation of the tubulin di ...... he absence of an energy source
@en
P2860
P356
P1476
Dissociation of the tubulin di ...... he absence of an energy source
@en
P2093
Lanette Fee
Michael Caplow
P2860
P304
P356
10.1091/MBC.E01-10-0089
P577
2002-06-01T00:00:00Z