ArticleBlood2007
Pathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding.
Article in Blood, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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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.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Red cell shape regulation by band 3-ankyrin-spectrin linkage: implications for clinical severity of bovine hereditary spherocytosis.Blood red cells & iron · 2025Article
- A genome-wide scan study identifies a single nucleotide substitution in MC1R gene associated with white coat colour in fallow deer (Dama dama).BMC genetics · 2020Article
- Red cell membrane protein abnormalities as defined by sds-page among patients with anemia in a West African region hospital practice.Caspian journal of internal medicine · 2020Article
- Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin.PLoS computational biology · 2018Article
- Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Novel exon 2 α spectrin mutation and intragenic crossover: three morphological phenotypes associated with four distinct α spectrin defects.Haematologica · 2013Article
- Article
- Understanding pathogenic single-nucleotide polymorphisms in multidomain proteins--studies of isolated domains are not enough.The FEBS journal · 2013Article
- Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics.Cytoskeleton (Hoboken, N.J.) · 2010Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- Control of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage.Biochemistry · 2010Article
- A folding zone in the ribosomal exit tunnel for Kv1.3 helix formation.Journal of molecular biology · 2010Article
- Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family.Nature · 2010Article
- Article
- Elasticity and rupture of a multi-domain neural cell adhesion molecule complex.Biophysical journal · 2009Article
- Studying the folding of multidomain proteins.HFSP journal · 2008Article
- Red cell membrane: past, present, and future.Blood · 2008Review
- Article
- Unique elastic properties of the spectrin tetramer as revealed by multiscale coarse-grained modeling.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Pathogenic mutations in alpha and beta spectrin result in a variety of syndromes, including hereditary elliptocytosis (HE), hereditary pyropoikilocytosis (HPP), and hereditary spherocytosis (HS). Although some mutations clearly lie at sites of interaction, such as the sites of spectrin alpha-betatetramer formation, a surprising number of HE-causing mutations have been identified within linker regions between distal spectrin repeats. Here we apply solution structural and single molecule methods to the folding and stability of recombinant proteins consisting of the first 5 spectrin repeats of alpha-spectrin, comparing normal spectrin with a pathogenic linker mutation, Q471P, between repeats R4 and R5. Results show that the linker mutation destabilizes a significant fraction of the 5-repeat construct at 37 degrees C, whereas the WT remains fully folded well above body temperature. In WT protein, helical linkers propagate stability from one repeat to the next, but the mutation disrupts the stabilizing influence of adjacent repeats. The results suggest a molecular mechanism for the high frequency of disease caused by proline mutations in spectrin linkers.
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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.