Recombinant Human Spectrin alpha chain, erythrocyte (SPTA1), partial

1. a novel HE case with a His54Pro mutation in the SPTA1 gene was reported. The results suggested that the His54Pro mutation influenced the role of erythrocyte membrane proteins without reducing its level of expression. PMID: 29484404
2. A novel SPTA1 mutation (H54P) was identified in a case of hereditary elliptocytosis. PMID: 28694211
3. The authors show that SUB1-mediated processing of MSP1 is important for parasite viability, the processing modifies the secondary structure of MSP1 and activates its capacity to bind spectrin. PMID: 26468747
4. The authors demonstrate that the initial vacuolar membrane around internalized Babesia divergens is formed from protein and lipid components of the red blood cells plasma membrane, including band 3, glycophorin A and spectrin. PMID: 25628009
5. a new function for spectrins in the stability of invadosomes and the coupling between actin regulation and ECM degradation PMID: 25830635
6. Case Report: severe hemolytic jaundice and a phenotype of hereditary spherocytosis due alpha-spectrin mutations. PMID: 25277063
7. In this review, we summarize the state of knowledge about interactions between spectrin and membrane lipids PMID: 24569979
8. A novel exon 2 alpha spectrin mutation is identified in two families of European ancestry with hereditary pyropoikilocytosis. PMID: 24077844
9. The heterozygous c.121C>T mutation of SPTA1 gene induces an amino acid change p.Arg41Trp in the alpha1 domain of the alpha-spectrin protein. PMID: 24003435
10. Data show that transcription cofactor TAF3 is required for transcription of the alpha spectrin SPTA1 gene. PMID: 23935956
11. The common hereditary elliptocytosis-associated alpha-spectrin leucine260proline mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. PMID: 23974198
12. The unusually slow, two-state kinetics of spectrin assembly in solution, was investigated. PMID: 23200054
13. In this review, we summarize recent findings concerning structure and function of spectrin together with its possible role in pathology. PMID: 23373410
14. These data further suggest that residues 44 and 53, which are key players in the nucleation-condensation mechanism of folding, are also important triggers of the aggregation process. PMID: 22727745
15. analysis of glycosylation of erythrocyte spectrin and its modification in visceral leishmaniasis PMID: 22164239
16. Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that those proteins are needed for efficient docking of enterohaemorrhagic Escherichia coli to host cells. PMID: 22197999
17. Results suggest that it is possible for cellular proteins to differentially associate with the C-termini of different beta-spectrin isoforms to regulate alpha- and beta-spectrin association to form functional spectrin tetramers. PMID: 21412925
18. lipid rafts are associated with the spectrin skeleton in human erythrocytes PMID: 20807499
19. The data show that the alpha-spectrin EF domain greatly amplifies the function of the beta-spectrin actin-binding domain in forming the spectrin-actin-4.1R complex. PMID: 20585040
20. The functional roles of residues 21-43 and 55-59 in the alpha-spectrin N-terminal region in forming tetramers were determined;mutations may also introduce abnormalities to erythrocytes. PMID: 19747366
21. identification and characterization of the gene promoter; requires GATA-1- and NF-E2-binding proteins to direct high level expression in erythroid cells in vitro. PMID: 12196550
22. Quantitative analysis of erythrocyte membrane proteins revealed increase in alpha-spectrin from patients with homozygous and heterozygous forms of beta-thalassemia. PMID: 15310273
23. a region 3' of the alpha-spectrin core promoter contains a GATA-1-dependent positive regulatory element that is required in its proper genomic orientation PMID: 15456760
24. analysis of erythroid alpha and beta spectrin chaperone activity and prodan binding PMID: 15492010
25. Ubiquitination of alpha-spectrin does not regulate heterodimer formation. PMID: 15795915
26. splicing mutation in hereditary pyropoikilocytosis kindred PMID: 16150946
27. We found that cysteine 2071 & cysteine 2100 are critical for alpha-spectrin (2005-2415) E2/E3 activity; also demonstrated that both Cys2071 & Cys2100 are capable of transferring ubiquitin from an E1 enzyme to target sites within alpha-spectrin (2005-2415) PMID: 16171554
28. the interaction of the alphaII-spectrin SH3 domain with EVL PMID: 16336193
29. These results suggest a role for spectrin in providing a dynamic and reversible signaling platform to the specific domains of the plasma membrane in response to stimulation of GPCR. PMID: 16551696
30. Results provide evidence that protein degradation of alphaII-spectrin is a reliable marker of severe traumatic brain injury (TBI) in humans and that both necrotic and apoptotic cell death mechanisms are activated in humans following a severe TBI. PMID: 16841024
31. REVIEW: Culture studies of Plasmodium falciparum in elliptocytes bearing such elliptocytogenic alleles of spectrin showed that these alleles are supplementary genetic factors of malaria resistance PMID: 17414207
32. The absence of particular spectrin isoforms may correlate with transformation or aggressive biologic behavior for some lymphoma subtypes. PMID: 17885671
33. analysis of the conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin PMID: 17905835
34. This model supports the hypothesis that initial docking of the correct alpha and beta repeats from among many very similar repeats in both subunits is driven primarily by long range electrostatic interactions. PMID: 17977835
35. All alpha0 HE/HPP mutations studied here appear to exert their destabilizing effects through molecular recognition rather than structural mechanisms. PMID: 18218854
36. Erythrocytes from most jereditary pyropoikilocytosis (inherited hemolytic anemia) exhibit abnormalities in the alpha-spectrin gene. PMID: 18815189
37. exon 1' and intron 1' are excellent candidate regions for mutations in patients with spectrin-linked hemolytic anemia PMID: 19008453
38. The L49F mutation in alpha erythroid spectrin leads to an unstable triple helical bundle of alpha beta-spectrin partial domains, and thus unstable tetramers. PMID: 19593814

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HGNC: 11272

OMIM: 130600

KEGG: hsa:6708

STRING: 9606.ENSP00000357130

UniGene: Hs.119825