about
Interactions causing the kinetic trap in serpin protein foldingCrystal structure of cleaved vaspin (serpinA12)Cavities of alpha(1)-antitrypsin that play structural and functional rolesA procedure for detection and quantitation of cavity volumes proteins. Application to measure the strength of the hydrophobic driving force in protein folding.Molecular interactions within the halophilic, thermophilic, and mesophilic prokaryotic ribosomal complexes: clues to environmental adaptation.Cavities and atomic packing in protein structures and interfaces.Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major virulence factor of Porphyromonas gingivalis in periodontitis.Structure of the essential Plasmodium host cell traversal protein SPECT1.Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.Stabilized homoserine o-succinyltransferases (MetA) or L-methionine partially recovers the growth defect in Escherichia coli lacking ATP-dependent proteases or the DnaK chaperone.A comparison of structural and evolutionary attributes of Escherichia coli and Thermus thermophilus small ribosomal subunits: signatures of thermal adaptationA novel mode of polymerization of alpha1-proteinase inhibitor.Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.How structure defines affinity in protein-protein interactions.The human serpin proteinase inhibitor-9 self-associates at physiological temperatures.Integrating folding kinetics and protein function: biphasic kinetics and dual binding specificity in a WW domain.Probing serpin conformational change using mass spectrometry and related methods.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Hydrostatic pressure induces the fusion-active state of enveloped viruses.The metastable state of nucleocapsids of enveloped viruses as probed by high hydrostatic pressure.A hydrophobic patch surrounding Trp154 in human neuroserpin controls the helix F dynamics with implications in inhibition and aggregation.Structural factors affecting the choice between latency transition and polymerization in inhibitory serpins.Specific interactions of serpins in their native forms attenuate their conformational transitions.Retarded protein folding of deficient human alpha 1-antitrypsin D256V and L41P variants.Functional unfolding of alpha1-antitrypsin probed by hydrogen-deuterium exchange coupled with mass spectrometry.Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop.Concerted regulation of inhibitory activity of alpha 1-antitrypsin by the native strain distributed throughout the molecule.Local and global effects of a cavity filling mutation in a metastable serpin.Packing of the extracellular domain hydrophobic core has evolved to facilitate pentameric ligand-gated ion channel function.The bilayer enhances rhodopsin kinetic stability in bovine rod outer segment disk membranes.Structural transformations accompanying the assembly of bacteriophage P22 portal protein rings in vitro.Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition.Kinetic dissection of alpha 1-antitrypsin inhibition mechanism.Targeting a surface cavity of alpha 1-antitrypsin to prevent conformational disease.On the folding of a structurally complex protein to its metastable active state.Molecular bases of neuroserpin function and pathology.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Regulation of protein function by native metastability
@ast
Regulation of protein function by native metastability
@en
type
label
Regulation of protein function by native metastability
@ast
Regulation of protein function by native metastability
@en
prefLabel
Regulation of protein function by native metastability
@ast
Regulation of protein function by native metastability
@en
P2093
P2860
P356
P1476
Regulation of protein function by native metastability
@en
P2093
P2860
P304
P356
10.1073/PNAS.97.14.7727
P407
P577
2000-07-01T00:00:00Z