Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis.
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Mixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of anotherStratum corneum protein dynamics as evaluated by a spin-label maleimide derivative: effect of ureaLactate dehydrogenase undergoes a substantial structural change to bind its substrateSalt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Solutes modify a conformational transition in a membrane transport protein.An overview of the importance of conformational flexibility in gene regulation by the transcription factors.Counteraction of urea-induced protein denaturation by trimethylamine N-oxide: a chemical chaperone at atomic resolution.Effect of osmolytes on protein dynamics in the lactate dehydrogenase-catalyzed reaction.Backbone additivity in the transfer model of protein solvation.Naturally occurring osmolyte, trehalose induces functional conformation in an intrinsically disordered activation domain of glucocorticoid receptor.Role of protein stabilizers on the conformation of the unfolded state of cytochrome c and its early folding kinetics: investigation at single molecular resolution.Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domainsEffect of osmolytes on the binding of EGR1 transcription factor to DNA.Forced folding of a disordered protein accesses an alternative folding landscape.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Testing the ability of non-methylamine osmolytes present in kidney cells to counteract the deleterious effects of urea on structure, stability and function of proteins.Structural characteristic of the initial unfolded state on refolding determines catalytic efficiency of the folded protein in presence of osmolytes.Restored mutant receptor:Corticoid binding in chaperone complexes by trimethylamine N-oxideStabilizing effect of TMAO on globular PNIPAM states: preferential attraction induces preferential hydration.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Combined pressure and cosolvent effects on enzyme activity - a high-pressure stopped-flow kinetic study on α-chymotrypsin.Counteraction of urea by trimethylamine N-oxide is due to direct interactionOsmolyte-induced conformational changes in the Hsp90 molecular chaperone.Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor.The paradox between m values and deltaCp's for denaturation of ribonuclease T1 with disulfide bonds intact and broken.Relationship between functional activity and protein stability in the presence of all classes of stabilizing osmolytes.Urea and KCl have differential effects on enzyme activities in liver and muscle of estivating versus nonestivating species.Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride.Influence of TMAO and urea on the structure of water studied by inelastic X-ray scattering.Testing polyols' compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes.Thermodynamic and Structural Adaptation Differences between the Mesophilic and Psychrophilic Lactate Dehydrogenases.Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor.A chemical chaperone induces inhomogeneous conformational changes in flexible proteins.Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.Nanostructures from self-assembling triazine tertiary amine N-oxide amphiphiles.A Natural Deep Eutectic Solvent Formulated to Stabilize β-Lactam Antibiotics
P2860
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P2860
Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@ast
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@en
type
label
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@ast
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@en
prefLabel
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@ast
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@en
P2093
P2860
P1433
P1476
Trimethylamine-N-oxide counter ...... the counteraction hypothesis.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(98)77972-X
P407
P577
1998-05-01T00:00:00Z