Diferencia entre revisiones de «Banda 4.1»
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== Referencias == |
== Referencias == |
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== Otras lecturas == |
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*{{cite journal | author = Conboy JG | title = Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. | journal = Semin. Hematol. | volume = 30 | issue = 1 | pages = 58–73 | year = 1993 | pmid = 8434260 }} |
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*{{cite journal |authors=Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P | title = New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. | journal = Front. Biosci. | volume = 11 | pages = 1646–66 | year = 2006 | pmid = 16368544 | doi = 10.2741/1911 | s2cid = 26325962 | url = https://digital.library.unt.edu/ark:/67531/metadc892527/}} |
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*{{cite journal |authors=Dalla Venezia N, Gilsanz F, Alloisio N, Ducluzeau MT, Benz EJ, Delaunay J | title = Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene. | journal = J. Clin. Invest. | volume = 90 | issue = 5 | pages = 1713–7 | year = 1992 | pmid = 1430200 | pmc = 443228 | doi = 10.1172/JCI116044 }} |
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*{{cite journal |authors=Jöns T, Drenckhahn D | title = Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. | journal = EMBO J. | volume = 11 | issue = 8 | pages = 2863–7 | year = 1992 | pmid = 1639060 | pmc = 556766 | doi = 10.1002/j.1460-2075.1992.tb05354.x}} |
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*{{cite journal |authors=Subrahmanyam G, Bertics PJ, Anderson RA | title = Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 12 | pages = 5222–6 | year = 1991 | pmid = 1647028 | pmc = 51844 | doi = 10.1073/pnas.88.12.5222 | bibcode = 1991PNAS...88.5222S}} |
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*{{cite journal |authors=Conboy JG, Chan JY, Chasis JA, Kan YW, Mohandas N | title = Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1. | journal = J. Biol. Chem. | volume = 266 | issue = 13 | pages = 8273–80 | year = 1991 | doi = 10.1016/S0021-9258(18)92973-X | pmid = 2022644}} |
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*{{cite journal |authors=Horne WC, Prinz WC, Tang EK | title = Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1. | journal = Biochim. Biophys. Acta | volume = 1055 | issue = 1 | pages = 87–92 | year = 1990 | pmid = 2171679 | doi = 10.1016/0167-4889(90)90095-U}} |
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*{{cite journal |authors=Conboy J, Marchesi S, Kim R, Agre P, Kan YW, Mohandas N | title = Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements. | journal = J. Clin. Invest. | volume = 86 | issue = 2 | pages = 524–30 | year = 1990 | pmid = 2384598 | pmc = 296755 | doi = 10.1172/JCI114739}} |
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*{{cite journal |authors=Inaba M, Maede Y | title = O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways. | journal = J. Biol. Chem. | volume = 264 | issue = 30 | pages = 18149–55 | year = 1989 | doi = 10.1016/S0021-9258(19)84689-6 | pmid = 2808371}} |
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*{{cite journal |authors=Korsgren C, Cohen CM | title = Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. | journal = J. Biol. Chem. | volume = 263 | issue = 21 | pages = 10212–8 | year = 1988 | doi = 10.1016/S0021-9258(19)81500-4 | pmid = 2968981 }} |
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*{{cite journal |authors=Conboy JG, Chan J, Mohandas N, Kan YW | title = Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 85 | issue = 23 | pages = 9062–5 | year = 1988 | pmid = 3194408 | pmc = 282663 | doi = 10.1073/pnas.85.23.9062 | bibcode = 1988PNAS...85.9062C }} |
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*{{cite book |authors=Tang TK, Leto TL, Marchesi VT, Benz EJ | title = Molecular Biology of Hemopoiesis | chapter = Expression of Specific Isoforms of Protein 4.1 in Erythroid and Non-Erythroid Tissues | volume = 241 | pages = 81–95 | pmid = 3223413 | doi = 10.1007/978-1-4684-5571-7_12 | series = Advances in Experimental Medicine and Biology | date = 1988 | isbn = 978-1-4684-5573-1}} |
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*{{cite journal |authors=Tang TK, Leto TL, Correas I, Alonso MA, Marchesi VT, Benz EJ | title = Selective expression of an erythroid-specific isoform of protein 4.1. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 85 | issue = 11 | pages = 3713–7 | year = 1988 | pmid = 3375238 | pmc = 280288 | doi = 10.1073/pnas.85.11.3713 | bibcode = 1988PNAS...85.3713T}} |
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*{{cite journal |authors=Conboy J, Kan YW, Shohet SB, Mohandas N | title = Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 83 | issue = 24 | pages = 9512–6 | year = 1987 | pmid = 3467321 | pmc = 387170 | doi = 10.1073/pnas.83.24.9512}} |
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*{{cite journal |authors=Correas I, Speicher DW, Marchesi VT | title = Structure of the spectrin-actin binding site of erythrocyte protein 4.1. | journal = J. Biol. Chem. | volume = 261 | issue = 28 | pages = 13362–6 | year = 1986 | doi = 10.1016/S0021-9258(18)69313-5 | pmid = 3531202}} |
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*{{cite journal |authors=Tchernia G, Mohandas N, Shohet SB | title = Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. | journal = J. Clin. Invest. | volume = 68 | issue = 2 | pages = 454–60 | year = 1981 | pmid = 6894932 | pmc = 370818 | doi = 10.1172/JCI110275 }} |
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*{{cite journal |authors=Schischmanoff PO, Winardi R, Discher DE, Parra MK, Bicknese SE, Witkowska HE, Conboy JG, Mohandas N | title = Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding. | journal = J. Biol. Chem. | volume = 270 | issue = 36 | pages = 21243–50 | year = 1995 | pmid = 7673158 | doi = 10.1074/jbc.270.36.21243}} |
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*{{cite journal |authors=Lue RA, Marfatia SM, Branton D, Chishti AH | title = Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 91 | issue = 21 | pages = 9818–22 | year = 1994 | pmid = 7937897 | pmc = 44908 | doi = 10.1073/pnas.91.21.9818 | bibcode = 1994PNAS...91.9818L}} |
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*{{cite journal |authors=Conboy JG, Chasis JA, Winardi R, Tchernia G, Kan YW, Mohandas N | title = An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells. | journal = J. Clin. Invest. | volume = 91 | issue = 1 | pages = 77–82 | year = 1993 | pmid = 8423235 | pmc = 329997 | doi = 10.1172/JCI116203 }} |
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{{Control de autoridades}} |
{{Control de autoridades}} |
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Revisión actual - 03:38 24 abr 2024
| Banda 4.1 | ||||
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 Proteína banda 4.1 | ||||
| Estructuras disponibles | ||||
| PDB |
Lista de códigos PDB 1gg3
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| Identificadores | ||||
| Símbolo | EPB41 (HGNC: 3377) | |||
| Identificadores externos | ||||
| Locus | Cr. 1 p36.2-34 | |||
| Ortólogos | ||||
| Especies |
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| Entrez |
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| UniProt |
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| RefSeq (ARNm) |
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Banda 4.1 o Proteína 4.1R o Sinaprina. en un miembro de la superfamilia de proteínas 4.1. Es una de las proteínas que participa en la unión del citoesqueleto a la membrana plasmática en los eritrocitos. Posee un dominio FERM con el que interacciona con glucoproteínas de la membrana plasmática, un dominio SABD que permite su interacción con la actina y con la espectrina y un dominio CTD en la zona del carboxi-terminal. Es expresada a partir del gen EPB41 localizado en el cromosoma 1 (1p36.2-34) con una extensión de 200kpb.[1]
Referencias[editar]
Otras lecturas[editar]
- Conboy JG (1993). «Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells.». Semin. Hematol. 30 (1): 58-73. PMID 8434260.
- Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P (2006). «New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium.». Front. Biosci. 11: 1646-66. PMID 16368544. S2CID 26325962. doi:10.2741/1911.
- Dalla Venezia N, Gilsanz F, Alloisio N, Ducluzeau MT, Benz EJ, Delaunay J (1992). «Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene.». J. Clin. Invest. 90 (5): 1713-7. PMC 443228. PMID 1430200. doi:10.1172/JCI116044.
- Jöns T, Drenckhahn D (1992). «Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger.». EMBO J. 11 (8): 2863-7. PMC 556766. PMID 1639060. doi:10.1002/j.1460-2075.1992.tb05354.x.
- Subrahmanyam G, Bertics PJ, Anderson RA (1991). «Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro.». Proc. Natl. Acad. Sci. U.S.A. 88 (12): 5222-6. Bibcode:1991PNAS...88.5222S. PMC 51844. PMID 1647028. doi:10.1073/pnas.88.12.5222.
- Conboy JG, Chan JY, Chasis JA, Kan YW, Mohandas N (1991). «Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1.». J. Biol. Chem. 266 (13): 8273-80. PMID 2022644. doi:10.1016/S0021-9258(18)92973-X.
- Horne WC, Prinz WC, Tang EK (1990). «Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1.». Biochim. Biophys. Acta 1055 (1): 87-92. PMID 2171679. doi:10.1016/0167-4889(90)90095-U.
- Conboy J, Marchesi S, Kim R, Agre P, Kan YW, Mohandas N (1990). «Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements.». J. Clin. Invest. 86 (2): 524-30. PMC 296755. PMID 2384598. doi:10.1172/JCI114739.
- Inaba M, Maede Y (1989). «O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.». J. Biol. Chem. 264 (30): 18149-55. PMID 2808371. doi:10.1016/S0021-9258(19)84689-6.
- Korsgren C, Cohen CM (1988). «Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3.». J. Biol. Chem. 263 (21): 10212-8. PMID 2968981. doi:10.1016/S0021-9258(19)81500-4.
- Conboy JG, Chan J, Mohandas N, Kan YW (1988). «Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells.». Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9062-5. Bibcode:1988PNAS...85.9062C. PMC 282663. PMID 3194408. doi:10.1073/pnas.85.23.9062.
- Tang TK, Leto TL, Marchesi VT, Benz EJ (1988). «Expression of Specific Isoforms of Protein 4.1 in Erythroid and Non-Erythroid Tissues». Molecular Biology of Hemopoiesis. Advances in Experimental Medicine and Biology 241. pp. 81-95. ISBN 978-1-4684-5573-1. PMID 3223413. doi:10.1007/978-1-4684-5571-7_12.
- Tang TK, Leto TL, Correas I, Alonso MA, Marchesi VT, Benz EJ (1988). «Selective expression of an erythroid-specific isoform of protein 4.1.». Proc. Natl. Acad. Sci. U.S.A. 85 (11): 3713-7. Bibcode:1988PNAS...85.3713T. PMC 280288. PMID 3375238. doi:10.1073/pnas.85.11.3713.
- Conboy J, Kan YW, Shohet SB, Mohandas N (1987). «Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton.». Proc. Natl. Acad. Sci. U.S.A. 83 (24): 9512-6. PMC 387170. PMID 3467321. doi:10.1073/pnas.83.24.9512.
- Correas I, Speicher DW, Marchesi VT (1986). «Structure of the spectrin-actin binding site of erythrocyte protein 4.1.». J. Biol. Chem. 261 (28): 13362-6. PMID 3531202. doi:10.1016/S0021-9258(18)69313-5.
- Tchernia G, Mohandas N, Shohet SB (1981). «Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability.». J. Clin. Invest. 68 (2): 454-60. PMC 370818. PMID 6894932. doi:10.1172/JCI110275.
- Schischmanoff PO, Winardi R, Discher DE, Parra MK, Bicknese SE, Witkowska HE, Conboy JG, Mohandas N (1995). «Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding.». J. Biol. Chem. 270 (36): 21243-50. PMID 7673158. doi:10.1074/jbc.270.36.21243.
- Lue RA, Marfatia SM, Branton D, Chishti AH (1994). «Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1.». Proc. Natl. Acad. Sci. U.S.A. 91 (21): 9818-22. Bibcode:1994PNAS...91.9818L. PMC 44908. PMID 7937897. doi:10.1073/pnas.91.21.9818.
- Conboy JG, Chasis JA, Winardi R, Tchernia G, Kan YW, Mohandas N (1993). «An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells.». J. Clin. Invest. 91 (1): 77-82. PMC 329997. PMID 8423235. doi:10.1172/JCI116203.
Datos: Q14908148