ArticleProceedings of the National Academy of Sciences of the United States of America2004
Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- αII-spectrin and βII-spectrin do not affect TGFβ1-induced myofibroblast differentiation.Cell and tissue research · 2018Article
- Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution.Scientific reports · 2017Article
- Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.PloS one · 2015Article
- Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins.PloS one · 2013Article
- Structural organization of the nine spectrin repeats of Kalirin.Biochemistry · 2012Article
- Shapes of Red Blood Cells: Comparison of 3D Confocal Images with the Bilayer-Couple Model.Cellular and molecular bioengineering · 2010Article
- Stabilization of the spectrin-like domains of nesprin-1α by the evolutionarily conserved "adaptive" domain.Cellular and molecular bioengineering · 2010Article
- Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanisms.Journal of molecular biology · 2009Article
- Article
- Stability of dystrophin STR fragments in relation to junction helicity.Biochimica et biophysica acta · 2008Article
- Molecular epitopes of the ankyrin-spectrin interaction.Biochemistry · 2008Article
- The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain.Journal of molecular biology · 2008Article
- Distinguishing specific and nonspecific interdomain interactions in multidomain proteins.Biophysical journal · 2008Article
- Pathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding.Blood · 2007Article
- Spectrin domains lose cooperativity in forced unfolding.Biophysical journal · 2007Article
- Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Article
- Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Biophysical journal · 2006Article
- Hybrid spectrin type repeats produced by exon-skipping in dystrophin.Biochimica et biophysica acta · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The large size of spectrin, the flexible protein promoting reversible deformation of red cells, has been an obstacle to elucidating the molecular mechanism of its function. By studying cloned fragments of the repeating unit domain, we have found a correspondence between positions of selected spectrin repeats in a tetramer with their stabilities of folding. Six fragments consisting of two spectrin repeats were selected for study primarily on the basis of the predicted secondary structures of their linker regions. Fragments with a putatively helical linker were more stable to urea- and heat-induced unfolding than those with a putatively nonhelical linker. Two of the less stably folded fragments, human erythroid alpha-spectrin repeats 13 and 14 (HEalpha13,14) and human erythroid beta-spectrin repeats 8 and 9 (HEbeta8,9), are located opposite each other on antiparallel spectrin dimers. At least partial unfolding of these repeats under physiological conditions indicates that they may serve as a hinge. Also less stably folded, the fragment of human erythroid alpha-spectrin repeats 4 and 5 (HEalpha4,5) lies opposite the site of interaction between the partial repeats at the C- and N-terminal ends of beta- and alpha-spectrin, respectively, on the opposing dimer. More stably folded fragments, human erythroid alpha-spectrin repeats 1 and 2 (HEalpha1,2) and human erythroid alpha-spectrin repeats 2 and 3 (HEalpha2,3), lie nearly opposite each other on antiparallel spectrin dimers of a tetramer. These clusterings along the spectrin tetramer of repeats with similar stabilities of folding may have relevance for spectrin function, particularly for its well known flexibility.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.