SKP2 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "SKP2" in Japanese language version.

refsWebsite

Global rank Japanese rank

92nih.gov

4^th place

24^th place

63doi.org

2^nd place

6^th place

7harvard.edu

18^th place

107^th place

2ensembl.org

1,626^th place

2,625^th place

2wikipedia.org

low place

1sciencedaily.com

993^rd place

2,074^th place

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Chromosomal mapping of the genes for the human CDK2/cyclin A-associated proteins p19 (SKP1A and SKP1B) and p45 (SKP2)”. Cytogenetics and Cell Genetics 73 (1–2): 104–7. (Jul 1996). doi:10.1159/000134318. PMID 8646875.
“SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box”. Cell 86 (2): 263–74. (July 1996). doi:10.1016/S0092-8674(00)80098-7. PMID 8706131.
“Regulation of Skp2 expression and activity and its role in cancer progression”. TheScientificWorldJournal 10: 1001–15. (2010). doi:10.1100/tsw.2010.89. PMC 5763972. PMID 20526532.
“Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex”. Nature 416 (6882): 703–9. (April 2002). Bibcode: 2002Natur.416..703Z. doi:10.1038/416703a. PMID 11961546.
“Regulation of the cell cycle by SCF-type ubiquitin ligases”. Seminars in Cell & Developmental Biology 16 (3): 323–33. (June 2005). doi:10.1016/j.semcdb.2005.02.010. PMID 15840441.
“The F-box protein family”. Genome Biology 1 (5): REVIEWS3002. (2000). doi:10.1186/gb-2000-1-5-reviews3002. PMC 138887. PMID 11178263.
“The SCF ubiquitin ligase: insights into a molecular machine”. Nature Reviews Molecular Cell Biology 5 (9): 739–51. (September 2004). doi:10.1038/nrm1471. PMID 15340381.
“SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27”. Nature Cell Biology 1 (4): 193–9. (August 1999). doi:10.1038/12013. PMID 10559916.
“p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27”. Current Biology 9 (12): 661–4. (June 1999). doi:10.1016/S0960-9822(99)80290-5. PMID 10375532.
“Three different binding sites of Cks1 are required for p27-ubiquitin ligation”. The Journal of Biological Chemistry 277 (44): 42233–40. (November 2002). doi:10.1074/jbc.M205254200. PMID 12140288.
“The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27”. Nature Cell Biology 3 (3): 321–4. (March 2001). doi:10.1038/35060126. PMID 11231585.
“Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase”. Nature 428 (6979): 190–3. (March 2004). doi:10.1038/nature02330. PMID 15014502.
“Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex”. Nature 428 (6979): 194–8. (March 2004). Bibcode: 2004Natur.428..194W. doi:10.1038/nature02381. PMID 15014503.
“Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APC(Cdh1) in G1 phase”. The EMBO Journal 27 (4): 679–91. (February 2008). doi:10.1038/emboj.2008.6. PMC 2262036. PMID 18239684.
“Phosphorylation of Ser72 is dispensable for Skp2 assembly into an active SCF ubiquitin ligase and its subcellular localization”. Cell Cycle 9 (5): 971–4. (March 2010). doi:10.4161/cc.9.5.10914. PMC 3827631. PMID 20160477.
“Phosphorylation of Ser72 does not regulate the ubiquitin ligase activity and subcellular localization of Skp2”. Cell Cycle 9 (5): 975–9. (March 2010). doi:10.4161/cc.9.5.10915. PMID 20160482.
“Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction”. Nature Cell Biology 11 (4): 397–408. (April 2009). doi:10.1038/ncb1847. PMC 2910589. PMID 19270695.
“A comparison between Skp2 and FOXO1 for their cytoplasmic localization by Akt1”. Cell Cycle 9 (5): 1021–2. (March 2010). doi:10.4161/cc.9.5.10916. PMC 2990537. PMID 20160512.
“Recycling the cell cycle: cyclins revisited”. Cell 116 (2): 221–34. (January 2004). doi:10.1016/S0092-8674(03)01080-8. PMID 14744433.
“Themes and variations on ubiquitylation”. Nature Reviews Molecular Cell Biology 2 (3): 169–78. (March 2001). doi:10.1038/35056563. PMID 11265246.
“Back to the future with ubiquitin”. Cell 116 (2): 181–90. (January 2004). doi:10.1016/S0092-8674(03)01074-2. PMID 14744430.
“Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer”. Nature Reviews. Cancer 8 (6): 438–49. (June 2008). doi:10.1038/nrc2396. PMC 2711846. PMID 18500245.
Yu, Z.-K.; Gervais, J. L. M.; Zhang, H. (1998). “Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21CIP1/WAF1 and cyclin D proteins”. Proceedings of the National Academy of Sciences 95 (19): 11324–11329. Bibcode: 1998PNAS...9511324Y. doi:10.1073/pnas.95.19.11324. PMC 21641. PMID 9736735.
Bornstein, G.; Bloom, J.; Sitry-Shevah, D.; Nakayama, K.; Pagano, M.; Hershko, A. (2003). “Role of the SCFSkp2 Ubiquitin Ligase in the Degradation of p21Cip1 in S Phase”. Journal of Biological Chemistry 278 (28): 25752–25757. doi:10.1074/jbc.m301774200. PMID 12730199.
Kossatz, U. (2004). “Skp2-dependent degradation of p27kip1 is essential for cell cycle progression”. Genes & Development 18 (21): 2602–2607. doi:10.1101/gad.321004. PMC 525540. PMID 15520280.
Barr, Alexis R.; Heldt, Frank S.; Zhang, Tongli; Bakal, Chris; Novakl, Bela (2016). “A Dynamical Framework for the All-or-None G1/S Transition”. Cell Systems 2 (1): 27–37. doi:10.1016/j.cels.2016.01.001. PMC 4802413. PMID 27136687.
Barr, Alexis R.; Cooper, Samuel; Heldt, Frank S.; Butera, Francesca; Stoy, Henriette; Mansfeld, Jorg; Novak, Bela; Bakal, Chris (2017). “DNA damage during S-phase mediates the proliferation-quiescence decision in the subsequent G1 via p21 expression”. Nature Communications 8: 14728. Bibcode: 2017NatCo...814728B. doi:10.1038/ncomms14728. PMC 5364389. PMID 28317845.
“Role of the F-box protein Skp2 in adhesion-dependent cell cycle progression”. The Journal of Cell Biology 153 (7): 1381–90. (June 2001). doi:10.1083/jcb.153.7.1381. PMC 2150734. PMID 11425869.
“Role of the F-box protein Skp2 in lymphomagenesis”. Proceedings of the National Academy of Sciences of the United States of America 98 (5): 2515–20. (February 2001). Bibcode: 2001PNAS...98.2515L. doi:10.1073/pnas.041475098. PMC 30169. PMID 11226270.
“Emerging Roles of SKP2 in Cancer Drug Resistance”. Cells 10 (5): 1147. (May 2021). doi:10.3390/cells10051147. PMC 8150781. PMID 34068643.
“Prognostic significance of the F-box protein Skp2 expression in diffuse large B-cell lymphoma”. American Journal of Hematology 73 (4): 230–5. (August 2003). doi:10.1002/ajh.10379. PMID 12879424.
“Skp2: a novel potential therapeutic target for prostate cancer”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1825 (1): 11–7. (January 2012). doi:10.1016/j.bbcan.2011.09.002. PMC 3242930. PMID 21963805.
“Clinical relevance of SKP2 alterations in metastatic melanoma”. Pigment Cell & Melanoma Research 24 (1): 197–206. (February 2011). doi:10.1111/j.1755-148X.2010.00784.x. PMC 3341662. PMID 20883453.
“Effect of S-phase kinase-associated protein 2 expression on distant metastasis and survival in nasopharyngeal carcinoma patients”. International Journal of Radiation Oncology, Biology, Physics 73 (1): 202–7. (January 2009). doi:10.1016/j.ijrobp.2008.04.008. PMID 18538504.
“Correlation of Skp2 overexpression to prognosis of patients with nasopharyngeal carcinoma from South China”. Chinese Journal of Cancer 30 (3): 204–12. (March 2011). doi:10.5732/cjc.010.10403. PMC 4013317. PMID 21352698.
“SKP2 confers resistance of pancreatic cancer cells towards TRAIL-induced apoptosis”. International Journal of Oncology 38 (1): 219–25. (January 2011). doi:10.3892/ijo_00000841. PMID 21109943.
“Differential expression of the F-box proteins Skp2 and Skp2B in breast cancer”. Oncogene 24 (21): 3448–58. (May 2005). doi:10.1038/sj.onc.1208328. PMID 15782142.
“Relationship between levels of Skp2 and P27 in breast carcinomas and possible role of Skp2 as targeted therapy”. Steroids 70 (11): 770–4. (October 2005). doi:10.1016/j.steroids.2005.04.012. PMID 16024059.
“Significance of skp2 expression in primary breast cancer”. Clinical Cancer Research 12 (4): 1215–20. (February 2006). doi:10.1158/1078-0432.CCR-05-1709. PMID 16489076.
“Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer”. The Journal of Clinical Investigation 110 (5): 633–41. (September 2002). doi:10.1172/JCI15795. PMC 151109. PMID 12208864.
“Phosphorylation-dependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB”. Nature Cell Biology 11 (4): 420–32. (April 2009). doi:10.1038/ncb1849. PMC 2830812. PMID 19270694.
“Skp2 targeting suppresses tumorigenesis by Arf-p53-independent cellular senescence”. Nature 464 (7287): 374–9. (March 2010). Bibcode: 2010Natur.464..374L. doi:10.1038/nature08815. PMC 2928066. PMID 20237562.
“Tumor suppressor ARF inhibits HER-2/neu-mediated oncogenic growth”. Oncogene 23 (42): 7132–43. (September 2004). doi:10.1038/sj.onc.1207918. PMID 15273726.
“The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis”. Cell 149 (5): 1098–111. (May 2012). doi:10.1016/j.cell.2012.02.065. PMC 3586339. PMID 22632973.
“Specific small molecule inhibitors of Skp2-mediated p27 degradation”. Chemistry & Biology 19 (12): 1515–24. (December 2012). doi:10.1016/j.chembiol.2012.09.015. PMC 3530153. PMID 23261596.
“Pharmacological inactivation of Skp2 SCF ubiquitin ligase restricts cancer stem cell traits and cancer progression”. Cell 154 (3): 556–68. (August 2013). doi:10.1016/j.cell.2013.06.048. PMC 3845452. PMID 23911321.
“Tuberin binds p27 and negatively regulates its interaction with the SCF component Skp2”. The Journal of Biological Chemistry 279 (47): 48707–15. (November 2004). doi:10.1074/jbc.M405528200. PMID 15355997.
“Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation”. Nature Cell Biology 1 (1): 14–9. (May 1999). doi:10.1038/8984. PMID 10559858.
“Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2”. Molecular and Cellular Biology 19 (1): 635–45. (January 1999). doi:10.1128/mcb.19.1.635. PMC 83921. PMID 9858587.
“Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase”. The Journal of Biological Chemistry 278 (28): 25752–7. (July 2003). doi:10.1074/jbc.M301774200. PMID 12730199.
“A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1”. The Journal of Biological Chemistry 278 (34): 32390–6. (August 2003). doi:10.1074/jbc.M305241200. PMID 12813041.
“Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization”. The Journal of Biological Chemistry 277 (32): 28706–13. (August 2002). doi:10.1074/jbc.M203668200. PMID 12042314.
“Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma”. Cancer Research 68 (11): 4192–200. (June 2008). doi:10.1158/0008-5472.CAN-07-6157. PMID 18519678.
“Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase”. Molecular Cell 20 (1): 9–19. (October 2005). doi:10.1016/j.molcel.2005.09.003. PMID 16209941.
“The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation”. The Journal of Biological Chemistry 278 (33): 30854–8. (August 2003). doi:10.1074/jbc.C300251200. PMID 12840033.
“TIP120A associates with cullins and modulates ubiquitin ligase activity”. The Journal of Biological Chemistry 278 (18): 15905–10. (May 2003). doi:10.1074/jbc.M213070200. PMID 12609982.
“Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34 with the F-box protein p45(SKP2): evidence for evolutionary conservation in the subunit composition of the CDC34-SCF pathway”. The EMBO Journal 17 (2): 368–83. (January 1998). doi:10.1093/emboj/17.2.368. PMC 1170388. PMID 9430629.
“Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome”. BMC Biochemistry 9: 1. (2008). doi:10.1186/1471-2091-9-1. PMC 2265268. PMID 18173839.
“Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication”. Molecular Cell 9 (3): 481–91. (March 2002). doi:10.1016/S1097-2765(02)00467-7. PMID 11931757.
“SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4”. Oncogene 19 (31): 3529–36. (July 2000). doi:10.1038/sj.onc.1203647. PMID 10918611.
“Characterization of the cullin and F-box protein partner Skp1”. FEBS Letters 438 (3): 183–9. (November 1998). doi:10.1016/S0014-5793(98)01299-X. PMID 9827542.
“Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex”. Nature 408 (6810): 381–6. (November 2000). Bibcode: 2000Natur.408..381S. doi:10.1038/35042620. PMID 11099048.
“Identification of a family of human F-box proteins”. Current Biology 9 (20): 1177–9. (October 1999). doi:10.1016/S0960-9822(00)80020-2. PMID 10531035.

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000145604 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000054115 - Ensembl, May 2017

harvard.edu (Global: 18^th place; Japanese: 107^th place)

ui.adsabs.harvard.edu

“Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex”. Nature 416 (6882): 703–9. (April 2002). Bibcode: 2002Natur.416..703Z. doi:10.1038/416703a. PMID 11961546.
“Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex”. Nature 428 (6979): 194–8. (March 2004). Bibcode: 2004Natur.428..194W. doi:10.1038/nature02381. PMID 15014503.
Yu, Z.-K.; Gervais, J. L. M.; Zhang, H. (1998). “Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21CIP1/WAF1 and cyclin D proteins”. Proceedings of the National Academy of Sciences 95 (19): 11324–11329. Bibcode: 1998PNAS...9511324Y. doi:10.1073/pnas.95.19.11324. PMC 21641. PMID 9736735.
Barr, Alexis R.; Cooper, Samuel; Heldt, Frank S.; Butera, Francesca; Stoy, Henriette; Mansfeld, Jorg; Novak, Bela; Bakal, Chris (2017). “DNA damage during S-phase mediates the proliferation-quiescence decision in the subsequent G1 via p21 expression”. Nature Communications 8: 14728. Bibcode: 2017NatCo...814728B. doi:10.1038/ncomms14728. PMC 5364389. PMID 28317845.
“Role of the F-box protein Skp2 in lymphomagenesis”. Proceedings of the National Academy of Sciences of the United States of America 98 (5): 2515–20. (February 2001). Bibcode: 2001PNAS...98.2515L. doi:10.1073/pnas.041475098. PMC 30169. PMID 11226270.
“Skp2 targeting suppresses tumorigenesis by Arf-p53-independent cellular senescence”. Nature 464 (7287): 374–9. (March 2010). Bibcode: 2010Natur.464..374L. doi:10.1038/nature08815. PMC 2928066. PMID 20237562.
“Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex”. Nature 408 (6810): 381–6. (November 2000). Bibcode: 2000Natur.408..381S. doi:10.1038/35042620. PMID 11099048.

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Chromosomal mapping of the genes for the human CDK2/cyclin A-associated proteins p19 (SKP1A and SKP1B) and p45 (SKP2)”. Cytogenetics and Cell Genetics 73 (1–2): 104–7. (Jul 1996). doi:10.1159/000134318. PMID 8646875.
“SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box”. Cell 86 (2): 263–74. (July 1996). doi:10.1016/S0092-8674(00)80098-7. PMID 8706131.
“Regulation of Skp2 expression and activity and its role in cancer progression”. TheScientificWorldJournal 10: 1001–15. (2010). doi:10.1100/tsw.2010.89. PMC 5763972. PMID 20526532.
“Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex”. Nature 416 (6882): 703–9. (April 2002). Bibcode: 2002Natur.416..703Z. doi:10.1038/416703a. PMID 11961546.
“Regulation of the cell cycle by SCF-type ubiquitin ligases”. Seminars in Cell & Developmental Biology 16 (3): 323–33. (June 2005). doi:10.1016/j.semcdb.2005.02.010. PMID 15840441.
“The F-box protein family”. Genome Biology 1 (5): REVIEWS3002. (2000). doi:10.1186/gb-2000-1-5-reviews3002. PMC 138887. PMID 11178263.
“The SCF ubiquitin ligase: insights into a molecular machine”. Nature Reviews Molecular Cell Biology 5 (9): 739–51. (September 2004). doi:10.1038/nrm1471. PMID 15340381.
“SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27”. Nature Cell Biology 1 (4): 193–9. (August 1999). doi:10.1038/12013. PMID 10559916.
“p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27”. Current Biology 9 (12): 661–4. (June 1999). doi:10.1016/S0960-9822(99)80290-5. PMID 10375532.
“Three different binding sites of Cks1 are required for p27-ubiquitin ligation”. The Journal of Biological Chemistry 277 (44): 42233–40. (November 2002). doi:10.1074/jbc.M205254200. PMID 12140288.
“The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27”. Nature Cell Biology 3 (3): 321–4. (March 2001). doi:10.1038/35060126. PMID 11231585.
“Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase”. Nature 428 (6979): 190–3. (March 2004). doi:10.1038/nature02330. PMID 15014502.
“Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex”. Nature 428 (6979): 194–8. (March 2004). Bibcode: 2004Natur.428..194W. doi:10.1038/nature02381. PMID 15014503.
“Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APC(Cdh1) in G1 phase”. The EMBO Journal 27 (4): 679–91. (February 2008). doi:10.1038/emboj.2008.6. PMC 2262036. PMID 18239684.
“Phosphorylation of Ser72 is dispensable for Skp2 assembly into an active SCF ubiquitin ligase and its subcellular localization”. Cell Cycle 9 (5): 971–4. (March 2010). doi:10.4161/cc.9.5.10914. PMC 3827631. PMID 20160477.
“Phosphorylation of Ser72 does not regulate the ubiquitin ligase activity and subcellular localization of Skp2”. Cell Cycle 9 (5): 975–9. (March 2010). doi:10.4161/cc.9.5.10915. PMID 20160482.
“Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction”. Nature Cell Biology 11 (4): 397–408. (April 2009). doi:10.1038/ncb1847. PMC 2910589. PMID 19270695.
“A comparison between Skp2 and FOXO1 for their cytoplasmic localization by Akt1”. Cell Cycle 9 (5): 1021–2. (March 2010). doi:10.4161/cc.9.5.10916. PMC 2990537. PMID 20160512.
“Recycling the cell cycle: cyclins revisited”. Cell 116 (2): 221–34. (January 2004). doi:10.1016/S0092-8674(03)01080-8. PMID 14744433.
“Themes and variations on ubiquitylation”. Nature Reviews Molecular Cell Biology 2 (3): 169–78. (March 2001). doi:10.1038/35056563. PMID 11265246.
“Back to the future with ubiquitin”. Cell 116 (2): 181–90. (January 2004). doi:10.1016/S0092-8674(03)01074-2. PMID 14744430.
“Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer”. Nature Reviews. Cancer 8 (6): 438–49. (June 2008). doi:10.1038/nrc2396. PMC 2711846. PMID 18500245.
Yu, Z.-K.; Gervais, J. L. M.; Zhang, H. (1998). “Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21CIP1/WAF1 and cyclin D proteins”. Proceedings of the National Academy of Sciences 95 (19): 11324–11329. Bibcode: 1998PNAS...9511324Y. doi:10.1073/pnas.95.19.11324. PMC 21641. PMID 9736735.
Bornstein, G.; Bloom, J.; Sitry-Shevah, D.; Nakayama, K.; Pagano, M.; Hershko, A. (2003). “Role of the SCFSkp2 Ubiquitin Ligase in the Degradation of p21Cip1 in S Phase”. Journal of Biological Chemistry 278 (28): 25752–25757. doi:10.1074/jbc.m301774200. PMID 12730199.
Kossatz, U. (2004). “Skp2-dependent degradation of p27kip1 is essential for cell cycle progression”. Genes & Development 18 (21): 2602–2607. doi:10.1101/gad.321004. PMC 525540. PMID 15520280.
Barr, Alexis R.; Heldt, Frank S.; Zhang, Tongli; Bakal, Chris; Novakl, Bela (2016). “A Dynamical Framework for the All-or-None G1/S Transition”. Cell Systems 2 (1): 27–37. doi:10.1016/j.cels.2016.01.001. PMC 4802413. PMID 27136687.
Barr, Alexis R.; Cooper, Samuel; Heldt, Frank S.; Butera, Francesca; Stoy, Henriette; Mansfeld, Jorg; Novak, Bela; Bakal, Chris (2017). “DNA damage during S-phase mediates the proliferation-quiescence decision in the subsequent G1 via p21 expression”. Nature Communications 8: 14728. Bibcode: 2017NatCo...814728B. doi:10.1038/ncomms14728. PMC 5364389. PMID 28317845.
“Role of the F-box protein Skp2 in adhesion-dependent cell cycle progression”. The Journal of Cell Biology 153 (7): 1381–90. (June 2001). doi:10.1083/jcb.153.7.1381. PMC 2150734. PMID 11425869.
“Role of the F-box protein Skp2 in lymphomagenesis”. Proceedings of the National Academy of Sciences of the United States of America 98 (5): 2515–20. (February 2001). Bibcode: 2001PNAS...98.2515L. doi:10.1073/pnas.041475098. PMC 30169. PMID 11226270.
“Emerging Roles of SKP2 in Cancer Drug Resistance”. Cells 10 (5): 1147. (May 2021). doi:10.3390/cells10051147. PMC 8150781. PMID 34068643.
“Prognostic significance of the F-box protein Skp2 expression in diffuse large B-cell lymphoma”. American Journal of Hematology 73 (4): 230–5. (August 2003). doi:10.1002/ajh.10379. PMID 12879424.
“Skp2: a novel potential therapeutic target for prostate cancer”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1825 (1): 11–7. (January 2012). doi:10.1016/j.bbcan.2011.09.002. PMC 3242930. PMID 21963805.
“Clinical relevance of SKP2 alterations in metastatic melanoma”. Pigment Cell & Melanoma Research 24 (1): 197–206. (February 2011). doi:10.1111/j.1755-148X.2010.00784.x. PMC 3341662. PMID 20883453.
“Effect of S-phase kinase-associated protein 2 expression on distant metastasis and survival in nasopharyngeal carcinoma patients”. International Journal of Radiation Oncology, Biology, Physics 73 (1): 202–7. (January 2009). doi:10.1016/j.ijrobp.2008.04.008. PMID 18538504.
“Correlation of Skp2 overexpression to prognosis of patients with nasopharyngeal carcinoma from South China”. Chinese Journal of Cancer 30 (3): 204–12. (March 2011). doi:10.5732/cjc.010.10403. PMC 4013317. PMID 21352698.
“SKP2 confers resistance of pancreatic cancer cells towards TRAIL-induced apoptosis”. International Journal of Oncology 38 (1): 219–25. (January 2011). doi:10.3892/ijo_00000841. PMID 21109943.
“Differential expression of the F-box proteins Skp2 and Skp2B in breast cancer”. Oncogene 24 (21): 3448–58. (May 2005). doi:10.1038/sj.onc.1208328. PMID 15782142.
“Relationship between levels of Skp2 and P27 in breast carcinomas and possible role of Skp2 as targeted therapy”. Steroids 70 (11): 770–4. (October 2005). doi:10.1016/j.steroids.2005.04.012. PMID 16024059.
“Significance of skp2 expression in primary breast cancer”. Clinical Cancer Research 12 (4): 1215–20. (February 2006). doi:10.1158/1078-0432.CCR-05-1709. PMID 16489076.
“Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer”. The Journal of Clinical Investigation 110 (5): 633–41. (September 2002). doi:10.1172/JCI15795. PMC 151109. PMID 12208864.
“Phosphorylation-dependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB”. Nature Cell Biology 11 (4): 420–32. (April 2009). doi:10.1038/ncb1849. PMC 2830812. PMID 19270694.
“Skp2 targeting suppresses tumorigenesis by Arf-p53-independent cellular senescence”. Nature 464 (7287): 374–9. (March 2010). Bibcode: 2010Natur.464..374L. doi:10.1038/nature08815. PMC 2928066. PMID 20237562.
“Tumor suppressor ARF inhibits HER-2/neu-mediated oncogenic growth”. Oncogene 23 (42): 7132–43. (September 2004). doi:10.1038/sj.onc.1207918. PMID 15273726.
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pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

Human PubMed Reference:
Mouse PubMed Reference:
“Entrez Gene: SKP2 S-phase kinase-associated protein 2 (p45)”. 2024年6月29日閲覧。

sciencedaily.com (Global: 993^rd place; Japanese: 2,074^th place)

“Disabling Skp2 gene helps shut down cancer growth” (英語). ScienceDaily. 2024年6月30日閲覧。

wikipedia.org (Global: low place; Japanese: low place)

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000145604 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000054115 - Ensembl, May 2017