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Article Evaluation

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Matrigel Article[1]

[edit]
  • Fix spelling of "polymerise" - should be "polymerize"
  • All relevant, updated facts
  • Additional information could be added; proper techniques
  • Tone is neutral
  • Citations function properly
  • No talk page
  1. ^ "Matrigel", Wikipedia, 2018-03-12, retrieved 2018-10-09

CDK-2 Article

[edit]
  • Article detail could be improved
  • It would be interesting to expand on and confirm the following information presented in the article:
    • "The role of this protein in G1-S transition has been recently questioned as cells lacking Cdk2 are reported to have no problem during this transition."

Cyclin E

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  • This article is more detailed than the CDK-2 article
  • Contradicts above statement regarding G1-S transition

Interleukin 28B

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  • Article describes protein in relation to hepatitis C treatment, but contains no further detail

Prospective Bibliography (CDK2) - Week 4

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  • Regulation of the initiation of DNA replication in human cells[1]
  • Low-Molecular-Weight Cyclin E in Human Cancer: Cellular Consequences and Opportunities for Targeted Therapies[2]
  • An integrated view of cyclin E function and regulation[3]
  • Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms[4]
  • Cyclin-dependent kinase[5]
  • Recent developments in cyclin-dependent kinase biochemical and structural studies[6]
  1. ^ Moiseeva, Tatiana N.; Bakkenist, Christopher J. (2018-09-12). "Regulation of the initiation of DNA replication in human cells". DNA repair. doi:10.1016/j.dnarep.2018.09.003. ISSN 1568-7856. PMID 30266203.
  2. ^ Caruso, Joseph A.; Duong, Mylinh T.; Carey, Jason P. W.; Hunt, Kelly K.; Keyomarsi, Khandan (2018-10-01). "Low-Molecular-Weight Cyclin E in Human Cancer: Cellular Consequences and Opportunities for Targeted Therapies". Cancer Research. 78 (19): 5481–5491. doi:10.1158/0008-5472.CAN-18-1235. ISSN 0008-5472. PMC 6168358. PMID 30194068.{{cite journal}}: CS1 maint: PMC format (link)
  3. ^ Siu, Ka Tat; Rosner, Marsha Rich; Minella, Alex C. (2012-01). "An integrated view of cyclin E function and regulation". Cell Cycle. 11 (1): 57–64. doi:10.4161/cc.11.1.18775. ISSN 1538-4101. PMC 3272232. PMID 22186781. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  4. ^ Satyanarayana, A.; Kaldis, P. (2009-08-20). "Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms". Oncogene. 28 (33): 2925–2939. doi:10.1038/onc.2009.170. ISSN 1476-5594. PMID 19561645.
  5. ^ Malumbres, Marcos (2014). "Cyclin-dependent kinases". Genome Biology. 15 (6): 122. doi:10.1186/gb4184. ISSN 1474-760X. PMC 4097832. PMID 25180339.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  6. ^ "Recent developments in cyclin-dependent kinase biochemical and structural studies". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804 (3): 511–519. 2010-03-01. doi:10.1016/j.bbapap.2009.10.002. ISSN 1570-9639.

small Edit

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Previous author:

The role of this protein in the G1-S transition has been recently questioned as cells lacking Cdk2 are reported to have no problem during this transition.

New addition:

Previous in vitro experiments demonstrated cell cycle arrest at the G1-S transition resulting from the deletion of Cdk2. When this experiment was replicated in vivo, the mice remained viable despite reduced body size. However, meiotic function of both male and female mice was inhibited. This suggests that Cdk2 is non-essential for the cell cycle, but essential for meiosis and reproduction. Cdk1 is believed to compensate for many aspects of Cdk2 deletion, except for meiotic function.

First Draft

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Cdk2 Dispensability

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Previous in-vitro experiments demonstrated cell cycle arrest at the G1-S transition resulting from the deletion of Cdk2. When this experiment was later replicated in vivo, the mice remained viable despite reduced body size. However, meiotic function of both male and female mice was inhibited. This suggests that Cdk2 is non-essential for the cell cycle, but essential for meiosis and reproduction. Cdk1 is believed to compensate for many aspects of Cdk2 deletion, except for meiotic function.[1]

Mechanism of Cdk2 Activation

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Like all protein kinases, cyclin-dependent kinase 2 is structured in two lobes. The lobe beginning at the N-terminal contains many beta sheets, while the C-lobe is rich in alpha helices. Cdk2 is capable of binding to many different cyclins, including cyclins A, B, E, and possibly C.

Cdk2 becomes active when a cyclin protein binds at the active site located between the N and C lobes of the kinase. It is unique in the way that it interacts with the respective cyclins over both lobes of the protein. Cdk2 contains an important alpha helix located in the C lobe of the kinase, called the C-helix. Hydrophobic interactions cause the C-helix to associate with another helix in the activating cyclin. Activation induces a conformational change where the helix rotates and moves closer to the N-lobe. This allows the glutamic acid located on the C-helix to form an ion pair with a nearby lysine side chain. This conformational change also relocates the activation loop to the C-lobe, revealing the ATP binding site now available for new interactions.

Finally, a threonine residue is exposed and phosphorylated as the C-lobe activation segment is displaced from the catalytic site. The phosphorylated threonine residue creates stability in the final enzyme conformation. It is important to note that throughout this activation process, cyclins binding to Cdk2 do not undergo any conformational change.

Cdk2-Cyclin E Complex and DNA Replication

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The success of the cell division process is dependent on the precise regulation of processes at both cellular and tissue levels. Complex interactions between proteins and DNA within the cell, as well as the cell with the surrounding tissue and extracellular matrix, allow cells to pass genomic DNA to daughter cells and incorporate new cells into a tissue. At the cellular level, the process is controlled by different levels of cyclin-dependent kinases and their partner cyclins throughout the cycle.

Cells utilize various checkpoints as a means of delaying cell cycle progression until it can repair defects.[2] Cyclin E is a major binding partner of Cdk2, and it acts as a G1-S checkpoint control. The S phase is also known as the synthesis phase, when DNA is replicated prior to division. The Cdk2/Cyclin E complex reaches peak activity levels in late G1 phase. The ubiquitin proteasome degrades cyclin E as the cell nears the end of S phase. Therefore, cdk2 and cyclin E have a significant role in the initiation of S phase and, consequently, the DNA replication process.[3] NPAT, a known substrate of the Cdk2-Cyclin E complex, functions to activate histone gene transcription when phosphorylated. This increases the synthesis of histone proteins, the major protein component of chromatin. This subsequently supports the DNA replication stage of the cell cycle.

Relationship Between Cdk2 Defects and Cancer

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Although Cdk2 has been proven "dispensable" in the cell cycle, it is critical in the growth and proliferation of cancer cells. Cdk2 has been proven to associate with E2F transcription factors and other tumor suppressor proteins. For example, the retinoblastoma protein (often abbreviated Rb or pRb) is a tumor suppressor protein that prevents S-phase entry and cell growth.[4] It suppresses gene transcription necessary for G1-S phase progression when bound to the E2F transactivation domain and gene promoters.[5]

Notes from Greg:

  • There are a lot of sentences with information that needs to be cited, e.g. the entire CDK2 activation section.
  • You probably want to capitalize the whole acronym CDK to keep the style of the main article.
  • Wikilinks are not present, and they would be particularly useful when mentioning terms unknown to most people -- such as beta sheets/alpha helices -- and when mentioning things most people won't be able to recall -- such as the life cycle of the cell.
  • In CDK2 dispensability, it will probably be worth mentioning when in the life cylce of the mice the in vitro experiment began and how it was performed. i.e. Were the genes knocked out when they were still zygotes, were the proteins inhibited when the mouse was a juvenile, etc.
  • In the DNA replication section, the second sentence is a bit difficult to follow, IMO. First, I think it will be worth breaking it into two separate sentences for clarity. Perhaps state what happens in one sentence, then explain why/how it happens that way in the following sentence. Second, when you say they "incorporate new cells into a tissue," I'm assuming you mean that these daughter cells continue to exist within the same tissue, but maybe clarify it. You could say, for example, that the "daughter cells are incorporated into the parent cell's tissue."
  • In the last sentence of that same paragraph, maybe swap out "controlled" for "regulated," as I think that's a slightly more precise phrasing.
  • In your second paragraph in the DNA replication section, you mention the ubiquitin proteasome out of the blue. Is it present the whole time? Does it get activated at the end of the S phase? It seems like you're trying to go through this process chronologically -- which is good -- but I am struggling to see how this sentence ties in other than simply the fact that the S phase gets stopped.
  • You could think about splitting this same paragraph into two paragraphs. One paragraph could be about the G1-S regulation, and the other could be about histone gene transcription, etc. These feel like independent topics to me.
  • In the last sentence of your cancer section, is "it" CDK2 or Rb? It's probably best to swap the word "it" for whichever protein is doing the suppression.
  • In the cancer section, is CDK2 stopping cancer or aiding its growth? Your first sentence makes it sound like cancer cells require CDK2 to grow and proliferate, but then it seems as though you're talking about CDK2 preventing cancer's growth in subsequent sentences.
  • If you want to add an image, you could probably try to find a picture of meioses happening and label where the CDK2 would be located.

Heather's peer review is in your talk page.

  1. ^ Cite error: The named reference :0 was invoked but never defined (see the help page).
  2. ^ Bartek, Jiri; Lukas, Claudia; Lukas, Jiri (2004-10). "Checking on DNA damage in S phase". Nature Reviews Molecular Cell Biology. 5 (10): 792–804. doi:10.1038/nrm1493. ISSN 1471-0072. {{cite journal}}: Check date values in: |date= (help)
  3. ^ Caruso, Joseph A.; Duong, Mylinh T.; Carey, Jason P. W.; Hunt, Kelly K.; Keyomarsi, Khandan (2018-10-01). "Low-Molecular-Weight Cyclin E in Human Cancer: Cellular Consequences and Opportunities for Targeted Therapies". Cancer Research. 78 (19): 5481–5491. doi:10.1158/0008-5472.CAN-18-1235. ISSN 0008-5472. PMC 6168358. PMID 30194068.{{cite journal}}: CS1 maint: PMC format (link)
  4. ^ The molecular basis of cancer. Mendelsohn, John, 1936-, Gray, Joe W.,, Howley, Peter M.,, Israel, Mark A.,, Thompson, Craig (Craig B.), (Fourth edition ed.). Philadelphia, PA. ISBN 9781455740666. OCLC 870870610. {{cite book}}: |edition= has extra text (help)CS1 maint: extra punctuation (link) CS1 maint: others (link)
  5. ^ Giacinti, C; Giordano, A (2006-08). "RB and cell cycle progression". Oncogene. 25 (38): 5220–5227. doi:10.1038/sj.onc.1209615. ISSN 0950-9232. {{cite journal}}: Check date values in: |date= (help)

Did You Know - Article Nomination

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Did you know that a protein called cyclin-dependent kinase 2 is a possible target for new cancer therapies?

"CDK2" redirects here. For the airport with the Transport Canada identifier CDK2, see Diavik Airport.

An Error has occurred retrieving Wikidata item for infobox Cyclin-dependent kinase 2, also known as cell division protein kinase 2, is an enzyme that in humans is encoded by the CDK2 gene.[1][2]

Function

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The protein encoded by this gene is a member of the cyclin-dependent kinase family of Ser/Thr protein kinases. This protein kinase is highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2, also known as Cdk1 in humans. It is a catalytic subunit of the cyclin-dependent kinase complex, whose activity is restricted to the G1-S phase of the cell cycle. This protein associates with and is regulated by the regulatory subunits of the complex including cyclin E or A. Cyclin E binds G1 phase Cdk2, which is required for the transition from G1 to S phase while binding with Cyclin A is required to progress through the S phase.[3] Its activity is also regulated by phosphorylation. Two alternatively spliced variants and multiple transcription initiation sites of this gene have been reported.[2]

The role of this protein in G1-S transition has been recently questioned as cells lacking Cdk2 are reported to have no problem during this transition.[4] Previous in vitro experiments demonstrated cell cycle arrest at the G1-S transition resulting from the deletion of Cdk2. When this experiment was later replicated in vivo, the mice remained viable despite reduced body size. However, meiotic function of both male and female mice was inhibited. This suggests that Cdk2 is non-essential for the cell cycle, but essential for meiosis and reproduction. Cdk1 is believed to compensate for many aspects of Cdk2 deletion, except for meiotic function.[5]

Inhibitors

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Known CDK inhibitors are p21Cip1 (CDKN1A) and p27Kip1 (CDKN1B).[6]

Drugs that inhibit Cdk2 and arrest the cell cycle, such as GW8510 and the experimental cancer drug seliciclib, may reduce the sensitivity of the epithelium to many cell cycle-active antitumor agents and, therefore, represent a strategy for prevention of chemotherapy-induced alopecia.[7]

Rosmarinic acid methyl ester is a plant-derived Cdk2 inhibitor, which was shown to suppress proliferation of vascular smooth muscle cells and to reduce neointima formation in mouse restenosis model.[8]

See also the PDB gallery below showing interactions with many inhibitors (inc Purvalanol B)

Gene regulation

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In melanocytic cell types, expression of the CDK2 gene is regulated by the Microphthalmia-associated transcription factor.[9][10]

Interactions

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Cyclin-dependent kinase 2 has been shown to interact with:

Overview of signal transduction pathways involved in apoptosis.

References

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  1. ^ Tsai LH, Harlow E, Meyerson M (September 1991). "Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase". Nature. 353 (6340): 174–7. doi:10.1038/353174a0. PMID 1653904.
  2. ^ a b "Entrez Gene: CDK2 cyclin-dependent kinase 2".
  3. ^ Echalier, Aude; Endicott, Jane A.; Noble, Martin E.M. (March 2010). "Recent developments in cyclin-dependent kinase biochemical and structural studies". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804 (3): 511–519. doi:10.1016/j.bbapap.2009.10.002. ISSN 1570-9639.
  4. ^ Berthet C, Aleem E, Coppola V, Tessarollo L, Kaldis P (October 2003). "Cdk2 knockout mice are viable". Curr. Biol. 13 (20): 1775–85. doi:10.1016/j.cub.2003.09.024. PMID 14561402.
  5. ^ Satyanarayana A, Kaldis P (August 2009). "Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms". Oncogene. 28 (33): 2925–39. doi:10.1038/onc.2009.170. PMID 19561645.
  6. ^ Levkau B, Koyama H, Raines EW, Clurman BE, Herren B, Orth K, Roberts JM, Ross R (March 1998). "Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: role of a caspase cascade". Mol. Cell. 1 (4): 553–63. doi:10.1016/S1097-2765(00)80055-6. PMID 9660939.
  7. ^ Davis ST, Benson BG, Bramson HN, Chapman DE, Dickerson SH, Dold KM, Eberwein DJ, Edelstein M, Frye SV, Gampe Jr RT, Griffin RJ, Harris PA, Hassell AM, Holmes WD, Hunter RN, Knick VB, Lackey K, Lovejoy B, Luzzio MJ, Murray D, Parker P, Rocque WJ, Shewchuk L, Veal JM, Walker DH, Kuyper LF (January 2001). "Prevention of chemotherapy-induced alopecia in rats by CDK inhibitors". Science. 291 (5501): 134–7. doi:10.1126/science.291.5501.134. PMID 11141566.
  8. ^ Liu R, Heiss EH, Waltenberger B, Blažević T, Schachner D, Jiang B, Krystof V, Liu W, Schwaiger S, Peña-Rodríguez LM, Breuss JM, Stuppner H, Dirsch VM, Atanasov AG (April 2018). "Constituents of Mediterranean Spices Counteracting Vascular Smooth Muscle Cell Proliferation: Identification and Characterization of Rosmarinic Acid Methyl Ester as a Novel Inhibitor". Molecular Nutrition & Food Research. 62 (7): e1700860. doi:10.1002/mnfr.201700860. PMID 29405576.
  9. ^ Du J, Widlund HR, Horstmann MA, Ramaswamy S, Ross K, Huber WE, Nishimura EK, Golub TR, Fisher DE (2004). "Critical role of CDK2 for melanoma growth linked to its melanocyte-specific transcriptional regulation by MITF". Cancer Cell. 6 (6): 565–76. doi:10.1016/j.ccr.2004.10.014. PMID 15607961.
  10. ^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
  11. ^ Chen Y, Farmer AA, Chen CF, Jones DC, Chen PL, Lee WH (July 1996). "BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner". Cancer Res. 56 (14): 3168–72. PMID 8764100.
  12. ^ Ruffner H, Jiang W, Craig AG, Hunter T, Verma IM (July 1999). "BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site". Mol. Cell. Biol. 19 (7): 4843–54. PMC 84283. PMID 10373534.
  13. ^ Wang H, Shao N, Ding QM, Cui J, Reddy ES, Rao VN (July 1997). "BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases". Oncogene. 15 (2): 143–57. doi:10.1038/sj.onc.1201252. PMID 9244350.
  14. ^ Shintani S, Ohyama H, Zhang X, McBride J, Matsuo K, Tsuji T, Hu MG, Hu G, Kohno Y, Lerman M, Todd R, Wong DT (September 2000). "p12(DOC-1) is a novel cyclin-dependent kinase 2-associated protein". Mol. Cell. Biol. 20 (17): 6300–7. doi:10.1128/MCB.20.17.6300-6307.2000. PMC 86104. PMID 10938106.
  15. ^ a b Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG, Melchior F, Hengst L, Slingerland JM (January 2003). "CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis". Mol. Biol. Cell. 14 (1): 201–13. doi:10.1091/mbc.E02-06-0319. PMC 140238. PMID 12529437.
  16. ^ a b Rosner M, Hengstschläger M (November 2004). "Tuberin binds p27 and negatively regulates its interaction with the SCF component Skp2". J. Biol. Chem. 279 (47): 48707–15. doi:10.1074/jbc.M405528200. PMID 15355997.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  17. ^ Youn CK, Cho HJ, Kim SH, Kim HB, Kim MH, Chang IY, Lee JS, Chung MH, Hahm KS, You HJ (February 2005). "Bcl-2 expression suppresses mismatch repair activity through inhibition of E2F transcriptional activity". Nat. Cell Biol. 7 (2): 137–47. doi:10.1038/ncb1215. PMID 15619620.
  18. ^ Porter LA, Kong-Beltran M, Donoghue DJ (September 2003). "Spy1 interacts with p27Kip1 to allow G1/S progression". Mol. Biol. Cell. 14 (9): 3664–74. doi:10.1091/mbc.E02-12-0820. PMC 196558. PMID 12972555.
  19. ^ a b Law BK, Chytil A, Dumont N, Hamilton EG, Waltner-Law ME, Aakre ME, Covington C, Moses HL (December 2002). "Rapamycin potentiates transforming growth factor beta-induced growth arrest in nontransformed, oncogene-transformed, and human cancer cells". Mol. Cell. Biol. 22 (23): 8184–98. doi:10.1128/mcb.22.23.8184-8198.2002. PMC 134072. PMID 12417722.
  20. ^ Yeh CT, Lu SC, Chao CH, Chao ML (May 2003). "Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-associated protein phosphatase by a truncated KAP mutant". Biochem. Biophys. Res. Commun. 305 (2): 311–4. doi:10.1016/s0006-291x(03)00757-5. PMID 12745075.
  21. ^ Hannon GJ, Casso D, Beach D (March 1994). "KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases". Proc. Natl. Acad. Sci. U.S.A. 91 (5): 1731–5. doi:10.1073/pnas.91.5.1731. PMC 43237. PMID 8127873.
  22. ^ a b Harper JW, Adami GR, Wei N, Keyomarsi K, Elledge SJ (November 1993). "The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases". Cell. 75 (4): 805–16. doi:10.1016/0092-8674(93)90499-g. PMID 8242751.
  23. ^ Wang H, Iakova P, Wilde M, Welm A, Goode T, Roesler WJ, Timchenko NA (October 2001). "C/EBPalpha arrests cell proliferation through direct inhibition of Cdk2 and Cdk4". Mol. Cell. 8 (4): 817–28. doi:10.1016/s1097-2765(01)00366-5. PMID 11684017.
  24. ^ Sweeney C, Murphy M, Kubelka M, Ravnik SE, Hawkins CF, Wolgemuth DJ, Carrington M (January 1996). "A distinct cyclin A is expressed in germ cells in the mouse". Development. 122 (1): 53–64. PMID 8565853.
  25. ^ Yang R, Morosetti R, Koeffler HP (March 1997). "Characterization of a second human cyclin A that is highly expressed in testis and in several leukemic cell lines". Cancer Res. 57 (5): 913–20. PMID 9041194.
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  31. ^ Mayer C, Zhao J, Yuan X, Grummt I (February 2004). "mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability". Genes Dev. 18 (4): 423–34. doi:10.1101/gad.285504. PMC 359396. PMID 15004009.
  32. ^ Boudrez A, Beullens M, Groenen P, Van Eynde A, Vulsteke V, Jagiello I, Murray M, Krainer AR, Stalmans W, Bollen M (August 2000). "NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry". J. Biol. Chem. 275 (33): 25411–7. doi:10.1074/jbc.M001676200. PMID 10827081.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  33. ^ Henneke G, Koundrioukoff S, Hübscher U (July 2003). "Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation". Oncogene. 22 (28): 4301–13. doi:10.1038/sj.onc.1206606. PMID 12853968.
  34. ^ Méndez J, Zou-Yang XH, Kim SY, Hidaka M, Tansey WP, Stillman B (March 2002). "Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication". Mol. Cell. 9 (3): 481–91. doi:10.1016/s1097-2765(02)00467-7. PMID 11931757.
  35. ^ a b Yam CH, Ng RW, Siu WY, Lau AW, Poon RY (January 1999). "Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2". Mol. Cell. Biol. 19 (1): 635–45. doi:10.1128/mcb.19.1.635. PMC 83921. PMID 9858587.
  36. ^ Ono T, Kitaura H, Ugai H, Murata T, Yokoyama KK, Iguchi-Ariga SM, Ariga H (October 2000). "TOK-1, a novel p21Cip1-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase". J. Biol. Chem. 275 (40): 31145–54. doi:10.1074/jbc.M003031200. PMID 10878006.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  37. ^ a b Cheng A, Kaldis P, Solomon MJ (November 2000). "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms". J. Biol. Chem. 275 (44): 34744–9. doi:10.1074/jbc.M006210200. PMID 10934208.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  38. ^ Leng X, Noble M, Adams PD, Qin J, Harper JW (April 2002). "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Mol. Cell. Biol. 22 (7): 2242–54. doi:10.1128/mcb.22.7.2242-2254.2002. PMC 133692. PMID 11884610.
  39. ^ Lacy S, Whyte P (May 1997). "Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes". Oncogene. 14 (20): 2395–406. doi:10.1038/sj.onc.1201085. PMID 9188854.
  40. ^ Marti A, Wirbelauer C, Scheffner M, Krek W (May 1999). "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation". Nat. Cell Biol. 1 (1): 14–9. doi:10.1038/8984. PMID 10559858.

Further reading

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[edit]


Category:Cell cycle Category:Proteins Category:EC 2.7.11

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