Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin
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Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motifN-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperoneCrystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens functionNon-3D domain swapped crystal structure of truncated zebrafish alphaA crystallinSolid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneityMultiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approachNewly folded substrates inside the molecular cage of the HtrA chaperone DegQThe congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallinFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsIn Vitro Structural and Functional Characterization of the Small Heat Shock Proteins (sHSP) of the Cyanophage S-ShM2 and Its Host, Synechococcus sp. WH7803Traveling-wave Ion Mobility-Mass Spectrometry Reveals Additional Mechanistic Details in the Stabilization of Protein Complex Ions through Tuned Salt Additives.The eye lens chaperone alpha-crystallin forms defined globular assemblies.Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthaseAlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice.The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.Quaternary dynamics and plasticity underlie small heat shock protein chaperone functionCrystallin-αB regulates skeletal muscle homeostasis via modulation of argonaute2 activity.Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsidsA Mechanism of Subunit Recruitment in Human Small Heat Shock Protein OligomersDissecting the functional role of the N-terminal domain of the human small heat shock protein HSPB6.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationExtensive Charge Reduction and Dissociation of Intact Protein Complexes Following Electron Transfer on a Quadrupole-Ion Mobility-Time-of-Flight MS.A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosisA novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study.Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis.The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.Mass spectrometry captures structural intermediates in protein fiber self-assemblyDissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach.Analysis of Native-Like Proteins and Protein Complexes Using Cation to Anion Proton Transfer Reactions (CAPTR).Noncovalent protein tetramers and pentamers with "n" charges yield monomers with n/4 and n/5 chargesStructural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27New insight into the dynamical system of αB-crystallin oligomers.The Human 343delT HSPB5 Chaperone Associated with Early-onset Skeletal Myopathy Causes Defects in Protein SolubilitySmall heat shock protein activity is regulated by variable oligomeric substructure.Alpha crystallin: the quest for a homogeneous quaternary structure.Regulated structural transitions unleash the chaperone activity of αB-crystallinUltraslow oligomerization equilibria of p53 and its implications.One size does not fit all: the oligomeric states of αB crystallin.Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.
P2860
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P2860
Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@ast
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@en
type
label
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@ast
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@en
prefLabel
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@ast
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@en
P2093
P2860
P356
P1476
Polydispersity of a mammalian ...... oligomers in alphaB-crystallin
@en
P2093
Christine Slingsby
J Andrew Aquilina
Orval A Bateman
P2860
P304
10611-10616
P356
10.1073/PNAS.1932958100
P407
P577
2003-08-28T00:00:00Z