DDX3X: Difference between revisions
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'''ATP-dependent [[:en:Helicase#RNA helicases|RNA helicase]] DDX3X''' is an [[enzyme]] that in humans is encoded by the ''DDX3X'' [[gene]].<ref name="pmid9381176">{{cite journal |vauthors=Lahn BT, Page DC | title = Functional coherence of the human Y chromosome | journal = Science | volume = 278 | issue = 5338 | pages = | '''ATP-dependent [[:en:Helicase#RNA helicases|RNA helicase]] DDX3X''' is an [[enzyme]] that in humans is encoded by the ''DDX3X'' [[gene]].<ref name="pmid9381176">{{cite journal | vauthors = Lahn BT, Page DC | title = Functional coherence of the human Y chromosome | journal = Science | volume = 278 | issue = 5338 | pages = 675–80 | date = October 1997 | pmid = 9381176 | pmc = | doi = 10.1126/science.278.5338.675 }}</ref><ref name="pmid9730595">{{cite journal | vauthors = Park SH, Lee SG, Kim Y, Song K | title = Assignment of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3→p11.23 | journal = Cytogenetics and Cell Genetics | volume = 81 | issue = 3–4 | pages = 178–9 | date = Oct 1998 | pmid = 9730595 | pmc = | doi = 10.1159/000015022 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1654 }}</ref> | ||
== Function == | == Function == | ||
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA | [[DExD/H box proteins|DEAD box proteins]], characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA [[helicase]]s. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as [[Eukaryotic translation#initiation|translation initiation]], nuclear and mitochondrial [[RNA splicing|splicing]], and [[ribosome]] and [[spliceosome]] assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.<ref name="entrez"/> | ||
== Role in cancer == | == Role in cancer == | ||
In [[:en:HeLa|HeLa cells]] DDX3X is reported to control cell cycle progression through [[:en:Cyclin E1|Cyclin E1]].<ref name=":1">{{ | DDX3X is involved in many different types of cancer. For example, it is abnormally expressed in breast epithelial cancer cells in which its expression is activated by [[:en:HIF1A|HIF1A]] during [[:en:Tumor hypoxia|hypoxia]].<ref name=":0">{{cite journal | vauthors = Botlagunta M, Krishnamachary B, Vesuna F, Winnard PT, Bol GM, Patel AH, Raman V | title = Expression of DDX3 is directly modulated by hypoxia inducible factor-1 alpha in breast epithelial cells | journal = PLOS One | volume = 6 | issue = 3 | pages = e17563 | date = March 2011 | pmid = 21448281 | doi = 10.1371/journal.pone.0017563 | website = | publisher = PLOS One | pmc=3063174}}</ref> Increased expression of DDX3X by HIF1A in hypoxia is initiated by the direct binding of HIF1A to the HIF1A [[:en:Transcription factor#Response elements|response element]],<ref name=":0" /> as verified with [[:en:Chromatin immunoprecipitation|chromatin immunoprecipitation]] and [[:en:Luciferase|luciferase reporter assay]]. Since the expression of DDX3X is affected by the activity of HIF1A, the co-localization of these proteins has also been demonstrated in [[MDA-MB-231]] [[:en:Xenograft|xenograft]] tumor samples.<ref name=":0" /> | ||
In [[:en:HeLa|HeLa cells]] DDX3X is reported to control cell cycle progression through [[:en:Cyclin E1|Cyclin E1]].<ref name=":1">{{cite journal | vauthors = Lai MC, Chang WC, Shieh SY, Tarn WY | title = DDX3 regulates cell growth through translational control of cyclin E1 | journal = Molecular and Cellular Biology | volume = 30 | issue = 22 | pages = 5444–53 | date = November 2010 | pmid = 20837705 | doi = 10.1128/MCB.00560-10 | url = http://mcb.asm.org/content/30/22/5444.long | website = | publisher = Molecular and Cellular Biology | pmc=2976371}}</ref> More specifically, DDX3X was shown to directly bind to the [[:en:Five prime untranslated region|5´ UTR]] of Cyclin E1 and thereby facilitating the translation of the protein. Increased protein levels of Cyclin E1 was demonstrated to mediate the transition of [[:en:S phase|S phase]] entry.<ref name=":1" /> | |||
== Clinical significance == | == Clinical significance == | ||
Mutations of the ''DDX3X'' gene are also associated with [[medulloblastoma]].<ref>{{cite journal |vauthors=Robinson G, Parker M, Kranenburg TA | title = Novel mutations target distinct subgroups of medulloblastoma | journal = Nature |date= | Mutations of the ''DDX3X'' gene are also associated with [[medulloblastoma]].<ref>{{cite journal | vauthors = Robinson G, Parker M, Kranenburg TA, Lu C, Chen X, Ding L, Phoenix TN, Hedlund E, Wei L, Zhu X, Chalhoub N, Baker SJ, Huether R, Kriwacki R, Curley N, Thiruvenkatam R, Wang J, Wu G, Rusch M, Hong X, Becksfort J, Gupta P, Ma J, Easton J, Vadodaria B, Onar-Thomas A, Lin T, Li S, Pounds S, Paugh S, Zhao D, Kawauchi D, Roussel MF, Finkelstein D, Ellison DW, Lau CC, Bouffet E, Hassall T, Gururangan S, Cohn R, Fulton RS, Fulton LL, Dooling DJ, Ochoa K, Gajjar A, Mardis ER, Wilson RK, Downing JR, Zhang J, Gilbertson RJ | display-authors = 6 | title = Novel mutations target distinct subgroups of medulloblastoma | journal = Nature | volume = 488 | issue = 7409 | pages = 43–8 | date = August 2012 | pmid = 22722829 | doi = 10.1038/nature11213 | pmc=3412905}}</ref><ref>{{cite journal | vauthors = Jones DT, Jäger N, Kool M, Zichner T, Hutter B, Sultan M, Cho YJ, Pugh TJ, Hovestadt V, Stütz AM, Rausch T, Warnatz HJ, Ryzhova M, Bender S, Sturm D, Pleier S, Cin H, Pfaff E, Sieber L, Wittmann A, Remke M, Witt H, Hutter S, Tzaridis T, Weischenfeldt J, Raeder B, Avci M, Amstislavskiy V, Zapatka M, Weber UD, Wang Q, Lasitschka B, Bartholomae CC, Schmidt M, von Kalle C, Ast V, Lawerenz C, Eils J, Kabbe R, Benes V, van Sluis P, Koster J, Volckmann R, Shih D, Betts MJ, Russell RB, Coco S, Tonini GP, Schüller U, Hans V, Graf N, Kim YJ, Monoranu C, Roggendorf W, Unterberg A, Herold-Mende C, Milde T, Kulozik AE, von Deimling A, Witt O, Maass E, Rössler J, Ebinger M, Schuhmann MU, Frühwald MC, Hasselblatt M, Jabado N, Rutkowski S, von Bueren AO, Williamson D, Clifford SC, McCabe MG, Collins VP, Wolf S, Wiemann S, Lehrach H, Brors B, Scheurlen W, Felsberg J, Reifenberger G, Northcott PA, Taylor MD, Meyerson M, Pomeroy SL, Yaspo ML, Korbel JO, Korshunov A, Eils R, Pfister SM, Lichter P | display-authors = 6 | title = Dissecting the genomic complexity underlying medulloblastoma | journal = Nature | volume = 488 | issue = 7409 | pages = 100–5 | date = August 2012 | pmid = 22832583 | pmc = 3662966 | doi = 10.1038/nature11284 }}</ref><ref>{{cite journal | vauthors = Pugh TJ, Weeraratne SD, Archer TC, Pomeranz Krummel DA, Auclair D, Bochicchio J, Carneiro MO, Carter SL, Cibulskis K, Erlich RL, Greulich H, Lawrence MS, Lennon NJ, McKenna A, Meldrim J, Ramos AH, Ross MG, Russ C, Shefler E, Sivachenko A, Sogoloff B, Stojanov P, Tamayo P, Mesirov JP, Amani V, Teider N, Sengupta S, Francois JP, Northcott PA, Taylor MD, Yu F, Crabtree GR, Kautzman AG, Gabriel SB, Getz G, Jäger N, Jones DT, Lichter P, Pfister SM, Roberts TM, Meyerson M, Pomeroy SL, Cho YJ | display-authors = 6 | title = Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations | journal = Nature | volume = 488 | issue = 7409 | pages = 106–10 | date = August 2012 | pmid = 22820256 | pmc = 3413789 | doi = 10.1038/nature11329 }}</ref> | ||
== See also == | |||
*[[Eukaryotic translation]] | |||
*[[DExD/H box proteins]] | |||
*[[DHX29]] | |||
==References== | == References == | ||
{{reflist}} | {{reflist}} | ||
==Further reading== | == Further reading == | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{cite journal | * {{cite journal | vauthors = Li L, Li HS, Pauza CD, Bukrinsky M, Zhao RY | title = Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions | journal = Cell Research | volume = 15 | issue = 11–12 | pages = 923–34 | year = 2006 | pmid = 16354571 | doi = 10.1038/sj.cr.7290370 }} | ||
*{{cite journal | * {{cite journal | vauthors = Owsianka AM, Patel AH | title = Hepatitis C virus core protein interacts with a human DEAD box protein DDX3 | journal = Virology | volume = 257 | issue = 2 | pages = 330–40 | date = May 1999 | pmid = 10329544 | doi = 10.1006/viro.1999.9659 }} | ||
*{{cite journal | * {{cite journal | vauthors = Mamiya N, Worman HJ | title = Hepatitis C virus core protein binds to a DEAD box RNA helicase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 22 | pages = 15751–6 | date = May 1999 | pmid = 10336476 | doi = 10.1074/jbc.274.22.15751 }} | ||
* {{cite journal | vauthors = Yagüe J, Alvarez I, Rognan D, Ramos M, Vázquez J, de Castro JA | title = An N-acetylated natural ligand of human histocompatibility leukocyte antigen (HLA)-B39. Classical major histocompatibility complex class I proteins bind peptides with a blocked NH(2) terminus in vivo | journal = The Journal of Experimental Medicine | volume = 191 | issue = 12 | pages = 2083–92 | date = June 2000 | pmid = 10859333 | pmc = 2193201 | doi = 10.1084/jem.191.12.2083 }} | |||
*{{cite journal | * {{cite journal | vauthors = Kim YS, Lee SG, Park SH, Song K | title = Gene structure of the human DDX3 and chromosome mapping of its related sequences | journal = Molecules and Cells | volume = 12 | issue = 2 | pages = 209–14 | date = October 2001 | pmid = 11710523 | doi = }} | ||
*{{cite journal | * {{cite journal | vauthors = Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG | title = Regulation of alternative splicing by SRrp86 and its interacting proteins | journal = Molecular and Cellular Biology | volume = 23 | issue = 21 | pages = 7437–47 | date = November 2003 | pmid = 14559993 | pmc = 207616 | doi = 10.1128/MCB.23.21.7437-7447.2003 }} | ||
*{{cite journal | * {{cite journal | vauthors = Shu H, Chen S, Bi Q, Mumby M, Brekken DL | title = Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line | journal = Molecular & Cellular Proteomics | volume = 3 | issue = 3 | pages = 279–86 | date = March 2004 | pmid = 14729942 | doi = 10.1074/mcp.D300003-MCP200 }} | ||
*{{cite journal | * {{cite journal | vauthors = Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G | title = A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway | journal = Nature Cell Biology | volume = 6 | issue = 2 | pages = 97–105 | date = February 2004 | pmid = 14743216 | doi = 10.1038/ncb1086 }} | ||
*{{cite journal | * {{cite journal | vauthors = Yedavalli VS, Neuveut C, Chi YH, Kleiman L, Jeang KT | title = Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function | journal = Cell | volume = 119 | issue = 3 | pages = 381–92 | date = October 2004 | pmid = 15507209 | doi = 10.1016/j.cell.2004.09.029 }} | ||
* {{cite journal | vauthors = Dayton AI | title = Within you, without you: HIV-1 Rev and RNA export | journal = Retrovirology | volume = 1 | issue = | pages = 35 | date = October 2004 | pmid = 15516266 | pmc = 526764 | doi = 10.1186/1742-4690-1-35 }} | |||
* {{cite journal | vauthors = Krishnan V, Zeichner SL | title = Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication | journal = Retrovirology | volume = 1 | issue = | pages = 42 | date = December 2004 | pmid = 15588285 | pmc = 543576 | doi = 10.1186/1742-4690-1-42 }} | |||
* {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nature Biotechnology | volume = 23 | issue = 1 | pages = 94–101 | date = January 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 }} | |||
* {{cite journal | vauthors = Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R | title = Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry | journal = Nature Methods | volume = 2 | issue = 8 | pages = 591–8 | date = August 2005 | pmid = 16094384 | doi = 10.1038/nmeth776 }} | |||
* {{cite journal | vauthors = Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J | title = Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC | journal = Proteomics | volume = 5 | issue = 14 | pages = 3589–99 | date = September 2005 | pmid = 16097034 | doi = 10.1002/pmic.200401217 }} | |||
* {{cite journal | vauthors = Chang PC, Chi CW, Chau GY, Li FY, Tsai YH, Wu JC, Wu Lee YH | title = DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control | journal = Oncogene | volume = 25 | issue = 14 | pages = 1991–2003 | date = March 2006 | pmid = 16301996 | doi = 10.1038/sj.onc.1209239 }} | |||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=1654}} | {{PDB Gallery|geneid=1654}} | ||
Latest revision as of 09:05, 5 March 2018
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ATP-dependent RNA helicase DDX3X is an enzyme that in humans is encoded by the DDX3X gene.[1][2][3]
Function
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.[3]
Role in cancer
DDX3X is involved in many different types of cancer. For example, it is abnormally expressed in breast epithelial cancer cells in which its expression is activated by HIF1A during hypoxia.[4] Increased expression of DDX3X by HIF1A in hypoxia is initiated by the direct binding of HIF1A to the HIF1A response element,[4] as verified with chromatin immunoprecipitation and luciferase reporter assay. Since the expression of DDX3X is affected by the activity of HIF1A, the co-localization of these proteins has also been demonstrated in MDA-MB-231 xenograft tumor samples.[4]
In HeLa cells DDX3X is reported to control cell cycle progression through Cyclin E1.[5] More specifically, DDX3X was shown to directly bind to the 5´ UTR of Cyclin E1 and thereby facilitating the translation of the protein. Increased protein levels of Cyclin E1 was demonstrated to mediate the transition of S phase entry.[5]
Clinical significance
Mutations of the DDX3X gene are also associated with medulloblastoma.[6][7][8]
See also
References
- ↑ Lahn BT, Page DC (October 1997). "Functional coherence of the human Y chromosome". Science. 278 (5338): 675–80. doi:10.1126/science.278.5338.675. PMID 9381176.
- ↑ Park SH, Lee SG, Kim Y, Song K (Oct 1998). "Assignment of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3→p11.23". Cytogenetics and Cell Genetics. 81 (3–4): 178–9. doi:10.1159/000015022. PMID 9730595.
- ↑ 3.0 3.1 "Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked".
- ↑ 4.0 4.1 4.2 Botlagunta M, Krishnamachary B, Vesuna F, Winnard PT, Bol GM, Patel AH, Raman V (March 2011). "Expression of DDX3 is directly modulated by hypoxia inducible factor-1 alpha in breast epithelial cells". PLOS One. PLOS One. 6 (3): e17563. doi:10.1371/journal.pone.0017563. PMC 3063174. PMID 21448281.
- ↑ 5.0 5.1 Lai MC, Chang WC, Shieh SY, Tarn WY (November 2010). "DDX3 regulates cell growth through translational control of cyclin E1". Molecular and Cellular Biology. Molecular and Cellular Biology. 30 (22): 5444–53. doi:10.1128/MCB.00560-10. PMC 2976371. PMID 20837705.
- ↑ Robinson G, Parker M, Kranenburg TA, Lu C, Chen X, Ding L, et al. (August 2012). "Novel mutations target distinct subgroups of medulloblastoma". Nature. 488 (7409): 43–8. doi:10.1038/nature11213. PMC 3412905. PMID 22722829.
- ↑ Jones DT, Jäger N, Kool M, Zichner T, Hutter B, Sultan M, et al. (August 2012). "Dissecting the genomic complexity underlying medulloblastoma". Nature. 488 (7409): 100–5. doi:10.1038/nature11284. PMC 3662966. PMID 22832583.
- ↑ Pugh TJ, Weeraratne SD, Archer TC, Pomeranz Krummel DA, Auclair D, Bochicchio J, et al. (August 2012). "Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations". Nature. 488 (7409): 106–10. doi:10.1038/nature11329. PMC 3413789. PMID 22820256.
Further reading
- Li L, Li HS, Pauza CD, Bukrinsky M, Zhao RY (2006). "Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions". Cell Research. 15 (11–12): 923–34. doi:10.1038/sj.cr.7290370. PMID 16354571.
- Owsianka AM, Patel AH (May 1999). "Hepatitis C virus core protein interacts with a human DEAD box protein DDX3". Virology. 257 (2): 330–40. doi:10.1006/viro.1999.9659. PMID 10329544.
- Mamiya N, Worman HJ (May 1999). "Hepatitis C virus core protein binds to a DEAD box RNA helicase". The Journal of Biological Chemistry. 274 (22): 15751–6. doi:10.1074/jbc.274.22.15751. PMID 10336476.
- Yagüe J, Alvarez I, Rognan D, Ramos M, Vázquez J, de Castro JA (June 2000). "An N-acetylated natural ligand of human histocompatibility leukocyte antigen (HLA)-B39. Classical major histocompatibility complex class I proteins bind peptides with a blocked NH(2) terminus in vivo". The Journal of Experimental Medicine. 191 (12): 2083–92. doi:10.1084/jem.191.12.2083. PMC 2193201. PMID 10859333.
- Kim YS, Lee SG, Park SH, Song K (October 2001). "Gene structure of the human DDX3 and chromosome mapping of its related sequences". Molecules and Cells. 12 (2): 209–14. PMID 11710523.
- Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (November 2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins". Molecular and Cellular Biology. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. PMID 14559993.
- Shu H, Chen S, Bi Q, Mumby M, Brekken DL (March 2004). "Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line". Molecular & Cellular Proteomics. 3 (3): 279–86. doi:10.1074/mcp.D300003-MCP200. PMID 14729942.
- Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
- Yedavalli VS, Neuveut C, Chi YH, Kleiman L, Jeang KT (October 2004). "Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function". Cell. 119 (3): 381–92. doi:10.1016/j.cell.2004.09.029. PMID 15507209.
- Dayton AI (October 2004). "Within you, without you: HIV-1 Rev and RNA export". Retrovirology. 1: 35. doi:10.1186/1742-4690-1-35. PMC 526764. PMID 15516266.
- Krishnan V, Zeichner SL (December 2004). "Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication". Retrovirology. 1: 42. doi:10.1186/1742-4690-1-42. PMC 543576. PMID 15588285.
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
- Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (August 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nature Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
- Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J (September 2005). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC". Proteomics. 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034.
- Chang PC, Chi CW, Chau GY, Li FY, Tsai YH, Wu JC, Wu Lee YH (March 2006). "DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control". Oncogene. 25 (14): 1991–2003. doi:10.1038/sj.onc.1209239. PMID 16301996.
