RALA (Portuguese Wikipedia)
Analysis of information sources in references of the Wikipedia article "RALA" in Portuguese language version.
refsWebsite
Global rank
Portuguese rank
43rd place
440th place
doi.org (Global: 2nd place; Portuguese: 4th place)
dx.doi.org
- Rousseau-Merck MF, Bernheim A, Chardin P, Miglierina R, Tavitian A, Berger R. «The ras-related ral gene maps to chromosome 7p15-22». Human Genetics. 79: 132–6. PMID 3292391. doi:10.1007/BF00280551
- Simicek M, Lievens S, Laga M, Guzenko D, Aushev VN, Kalev P, Baietti MF, Strelkov SV, Gevaert K, Tavernier J, Sablina AA. «The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response». Nature Cell Biology. 15: 1220–30. PMID 24056301. doi:10.1038/ncb2847
- Tecleab A, Zhang X, Sebti SM. «Ral GTPase down-regulation stabilizes and reactivates p53 to inhibit malignant transformation». The Journal of Biological Chemistry. 289: 31296–309. PMC 4223330
. PMID 25210032. doi:10.1074/jbc.M114.565796 - DF, Kashatus. «Ral GTPases in tumorigenesis: emerging from the shadows». Experimental Cell Research. 319: 2337–42. PMC 4270277. PMID 23830877. doi:10.1016/j.yexcr.2013.06.020
- Hazelett CC, Sheff D, Yeaman C. «RalA and RalB differentially regulate development of epithelial tight junctions». Molecular Biology of the Cell. 22: 4787–800. PMC 3237622. PMID 22013078. doi:10.1091/mbc.E11-07-0657
- Shirakawa R, Horiuchi H. «Ral GTPases: crucial mediators of exocytosis and tumourigenesis». Journal of Biochemistry. 157: 285–99. PMID 25796063. doi:10.1093/jb/mvv029
- Jeon H, Zheng LT, Lee S, Lee WH, Park N, Park JY, Heo WD, Lee MS, Suk K. «Comparative analysis of the role of small G proteins in cell migration and cell death: cytoprotective and promigratory effects of RalA». Experimental Cell Research. 317: 2007–18. PMID 21645515. doi:10.1016/j.yexcr.2011.05.021
- Ohta Y, Suzuki N, Nakamura S, Hartwig JH, Stossel TP. «The small GTPase RalA targets filamin to induce filopodia». Proceedings of the National Academy of Sciences of the United States of America. 96: 2122–8. PMC 26747. PMID 10051605. doi:10.1073/pnas.96.5.2122
- Luo JQ, Liu X, Hammond SM, Colley WC, Feig LA, Frohman MA, Morris AJ, Foster DA. «RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1». Biochemical and Biophysical Research Communications. 235: 854–9. PMID 9207251. doi:10.1006/bbrc.1997.6793
- Kim JH, Lee SD, Han JM, Lee TG, Kim Y, Park JB, Lambeth JD, Suh PG, Ryu SH. «Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA». FEBS Letters. 430: 231–5. PMID 9688545. doi:10.1016/S0014-5793(98)00661-9
- Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA. «Ral GTPases regulate exocyst assembly through dual subunit interactions». The Journal of Biological Chemistry. 278: 51743–8. PMID 14525976. doi:10.1074/jbc.M308702200
- Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH. «Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity». The Journal of Biological Chemistry. 270: 22473–7. PMID 7673236. doi:10.1074/jbc.270.38.22473
- Cantor SB, Urano T, Feig LA. «Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases». Molecular and Cellular Biology. 15: 4578–84. PMC 230698. PMID 7623849. doi:10.1128/mcb.15.8.4578
- Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A. «Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral». The Journal of Biological Chemistry. 273: 814–21. PMID 9422736. doi:10.1074/jbc.273.2.814
nih.gov (Global: 4th place; Portuguese: 8th place)
ncbi.nlm.nih.gov
- «Human PubMed Reference:»
- Rousseau-Merck MF, Bernheim A, Chardin P, Miglierina R, Tavitian A, Berger R. «The ras-related ral gene maps to chromosome 7p15-22». Human Genetics. 79: 132–6. PMID 3292391. doi:10.1007/BF00280551
- «Entrez Gene: RALA v-ral simian leukemia viral oncogene homolog A (ras related)»
- Simicek M, Lievens S, Laga M, Guzenko D, Aushev VN, Kalev P, Baietti MF, Strelkov SV, Gevaert K, Tavernier J, Sablina AA. «The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response». Nature Cell Biology. 15: 1220–30. PMID 24056301. doi:10.1038/ncb2847
- Tecleab A, Zhang X, Sebti SM. «Ral GTPase down-regulation stabilizes and reactivates p53 to inhibit malignant transformation». The Journal of Biological Chemistry. 289: 31296–309. PMC 4223330. PMID 25210032. doi:10.1074/jbc.M114.565796
- DF, Kashatus. «Ral GTPases in tumorigenesis: emerging from the shadows». Experimental Cell Research. 319: 2337–42. PMC 4270277. PMID 23830877. doi:10.1016/j.yexcr.2013.06.020
- Hazelett CC, Sheff D, Yeaman C. «RalA and RalB differentially regulate development of epithelial tight junctions». Molecular Biology of the Cell. 22: 4787–800. PMC 3237622. PMID 22013078. doi:10.1091/mbc.E11-07-0657
- Shirakawa R, Horiuchi H. «Ral GTPases: crucial mediators of exocytosis and tumourigenesis». Journal of Biochemistry. 157: 285–99. PMID 25796063. doi:10.1093/jb/mvv029
- Jeon H, Zheng LT, Lee S, Lee WH, Park N, Park JY, Heo WD, Lee MS, Suk K. «Comparative analysis of the role of small G proteins in cell migration and cell death: cytoprotective and promigratory effects of RalA». Experimental Cell Research. 317: 2007–18. PMID 21645515. doi:10.1016/j.yexcr.2011.05.021
- Ohta Y, Suzuki N, Nakamura S, Hartwig JH, Stossel TP. «The small GTPase RalA targets filamin to induce filopodia». Proceedings of the National Academy of Sciences of the United States of America. 96: 2122–8. PMC 26747. PMID 10051605. doi:10.1073/pnas.96.5.2122
- Luo JQ, Liu X, Hammond SM, Colley WC, Feig LA, Frohman MA, Morris AJ, Foster DA. «RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1». Biochemical and Biophysical Research Communications. 235: 854–9. PMID 9207251. doi:10.1006/bbrc.1997.6793
- Kim JH, Lee SD, Han JM, Lee TG, Kim Y, Park JB, Lambeth JD, Suh PG, Ryu SH. «Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA». FEBS Letters. 430: 231–5. PMID 9688545. doi:10.1016/S0014-5793(98)00661-9
- Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA. «Ral GTPases regulate exocyst assembly through dual subunit interactions». The Journal of Biological Chemistry. 278: 51743–8. PMID 14525976. doi:10.1074/jbc.M308702200
- Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH. «Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity». The Journal of Biological Chemistry. 270: 22473–7. PMID 7673236. doi:10.1074/jbc.270.38.22473
- Cantor SB, Urano T, Feig LA. «Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases». Molecular and Cellular Biology. 15: 4578–84. PMC 230698. PMID 7623849. doi:10.1128/mcb.15.8.4578
- Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A. «Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral». The Journal of Biological Chemistry. 273: 814–21. PMID 9422736. doi:10.1074/jbc.273.2.814