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Caenorhabditis elegans beta-G spectrin is dispensable for establishment of epithelial polarity, but essential for muscular and neuronal functionMapping the human erythrocyte beta-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the alpha-actinin dimer siteIdentification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexesNovel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzymeThe folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Identification of the main ubiquitination site in human erythroid alpha-spectrin.The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments.Low expression allele alpha LELY of red cell spectrin is associated with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with partial skipping of exon 46.Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins.Extending a spectrin repeat unit. II: rupture behaviorComplex folding kinetics of a multidomain protein.Spectrin domains lose cooperativity in forced unfolding.Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin.Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domainsInterchain binding at the tail end of the Drosophila spectrin moleculeStabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.Drosophila development requires spectrin network formation.Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster.Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanismsMolecular epitopes of the ankyrin-spectrin interaction.Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis.Identification of the vinculin-binding site in the cytoskeletal protein alpha-actinin.Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.A Two-amino Acid Mutation Encountered in Duchenne Muscular Dystrophy Decreases Stability of the Rod Domain 23 (R23) Spectrin-like Repeat of Dystrophin.Site-directed mutagenesis of either the highly conserved Trp-22 or the moderately conserved Trp-95 to a large, hydrophobic residue reduces the thermodynamic stability of a spectrin repeating unit.The spectrin repeat folds into a three-helix bundle in solution.Severe poikilocytosis associated with a de novo alpha 28 Arg-->Cys mutation in spectrin.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Phasing the conformational unit of spectrin.
@en
Phasing the conformational unit of spectrin.
@nl
type
label
Phasing the conformational unit of spectrin.
@en
Phasing the conformational unit of spectrin.
@nl
prefLabel
Phasing the conformational unit of spectrin.
@en
Phasing the conformational unit of spectrin.
@nl
P2860
P356
P1476
Phasing the conformational unit of spectrin.
@en
P2093
P2860
P304
10788-10791
P356
10.1073/PNAS.88.23.10788
P407
P577
1991-12-01T00:00:00Z