ArticleThe Journal of cell biology1989
Primary structure of the brain alpha-spectrin.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers.
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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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Who cites it
44 citing papers in PubMed, 162 citations in OpenAlex.
- Spectrins: molecular organizers and targets of neurological disorders.Nature reviews. Neuroscience · 2023Review
- βII spectrin (SPTBN1): biological function and clinical potential in cancer and other diseases.International journal of biological sciences · 2021Review
- Spectrin and phospholipids - the current picture of their fascinating interplay.Cellular & molecular biology letters · 2014Review
- Molecular epitopes of the ankyrin-spectrin interaction.Biochemistry · 2008Article
- Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Biophysical journal · 2006Article
- Extending a spectrin repeat unit. II: rupture behavior.Biophysical journal · 2006Article
- Functional links between membrane transport and the spectrin cytoskeleton.The Journal of membrane biology · 2006Review
- Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Monoclonal antibodies to alphaI spectrin Src homology 3 domain associate with macropinocytic vesicles in nonerythroid cells.Brain research · 2001Article
- Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles.The Journal of cell biology · 1996Article
- A Ras-GTPase-activating protein SH3-domain-binding protein.Molecular and cellular biology · 1996Article
- The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.The EMBO journal · 1995Article
- Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains.Molecular and cellular biology · 1995Article
- The regulation of tyrosine kinase signalling pathways by growth factor and G-protein-coupled receptors.The Biochemical journal · 1995Review
- Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions.The EMBO journal · 1995Article
- myoA of Aspergillus nidulans encodes an essential myosin I required for secretion and polarized growth.The Journal of cell biology · 1995Article
- An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane.The EMBO journal · 1994Article
- Phosphatidylinositol 3-kinase binds to alpha-actinin through the p85 subunit.The Biochemical journal · 1994Article
- c-Abl kinase regulates the protein binding activity of c-Crk.The EMBO journal · 1994Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have determined the nucleotide sequence coding for the chicken brain alpha-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail. The deduced amino acid sequence was used to map the domain structure of the protein. The alpha-chain of brain spectrin contains 22 segments of which 20 correspond to the repeat of the human erythrocyte spectrin (Speicher, D. W., and V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made of 106 residues. These homologous segments probably account for the flexible, rod-like structure of spectrin. Secondary structure prediction suggests predominantly alpha-helical structure for the entire chain. Parts of the primary structure are excluded from the repetitive pattern and they reside in the middle part of the sequence and in its COOH terminus. Search for homology in other proteins showed the presence of the following distinct structures in these nonrepetitive regions: (a) the COOH-terminal part of the molecule that shows homology with alpha-actinin, (b) two typical EF-hand (i.e., Ca2+-binding) structures in this region, (c) a sequence close to the EF-hand that fulfills the criteria for a calmodulin-binding site, and (d) a domain in the middle of the sequence that is homologous to a NH2-terminal segment of several src-tyrosine kinases and to a domain of phospholipase C. These regions are good candidates to carry some established as well as some yet unestablished functions of spectrin. Comparative analysis showed that alpha-spectrin is well conserved across the species boundaries from Xenopus to man, and that the human erythrocyte alpha-spectrin is divergent from the other spectrins.
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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.