Białko von Hippla-Lindaua (Polish Wikipedia)

Analysis of information sources in references of the Wikipedia article "Białko von Hippla-Lindaua" in Polish language version.

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cancerres.aacrjournals.org

Shiao, YH, Resau JH, Nagashima K, Anderson LM, Ramakrishna G. The von Hippel-Lindau tumor suppressor targets to mitochondria. „Cancer Res”. 60. 11, s. 2816-2819, 2000. PMID: 20306593.
Bindra, RS, Vasselli, JR, Stearman, R, Linehan, WM, Klausner, RD. VHL-mediated hypoxia regulation of cyclin D1 in renal carcinoma cells. „Cancer Res”. 62. 11, s. 3014-3019, 2002. PMID: 12036906.
Zatyka, M, da Silva, NF, Clifford, SC, Morris, MR, Wiesener,MS, Eckardt, KU, Houlston, RS, Richards, FM, Latif, F, Maher, ER. Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease. „Cancer Res”. 62. 13, s. 3803-11, 2002. PMID: 12097293.
Gao J, Naglich JG, Laidlaw J, Whaley JM, Seizinger BR, Kley N. Cloning and characterization of a mouse gene with homology to the human von Hippel-Lindau disease tumor suppressor gene: implications for the potential organization of the human von Hippel-Lindau disease gene. „Cancer Res”. 55. 4, s. 743-747, 1995. PMID: 7850784.

asm.org

mcb.asm.org

Mukhopadhyay, D, Knebelmann, B, Cohen, HT, Ananth, S, Sukhatme, VP. The von Hippel-Lindau tumor suppressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity. „Mol Cell Biol”. 17, s. 5629-5639, 1997. PMID: 97415639.
Hergovich, A, Lisztwan, J, Thoma, CR, Wirbelauer, C, Barry, RE, Krek, W. Priming-dependent phosphorylation and regulation of the tumor suppressor pVHL by glycogen synthase kinase 3. „Mol Cell Biol”. 26. 15, s. 5784-96, 2006. PMID: 16847331.

cambridge.org

journals.cambridge.org

Richards, FM. Molecular pathology of von Hippel-Lindau disease and the VHL tumor supressor gene. „Expert Reviews in Molecular Medicine”, 2001.

genesdev.org

Kamura, T, Conrad, MN, Yan, Q, Conaway, RC, Conaway, JW. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. „Genes Dev”. 13, s. 2928-2933, 1999.

jbc.org

Pal, S, Claffey, KP, Dvorak, HF, Mukhopadhyay, D. The von Hippel-Lindau gene product inhibits vascular permeability factor/ vascular endothelial growth factor expression in renal cell carcinoma by blocking protein kinase C pathways. „J Biol Chem”. 272, s. 27509-27512, 1997. PMID: 98010573.
Li, Z, Na, X, Wang, D, Schoen, SR, Messing, EM, Wu, G. Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. „J Biol Chem”. 277. 7, s. 4656-4662, 2002. PMID: 11739384.
Datta, K, Nambudripad, R, Pal, S, Zhou, M, Cohen, HT, Mukhopadhyay, D. Inhibition of insulin-like growth factor-I-mediated cell signaling by the von Hippel-Lindau gene product in renal cancer. „J Biol Chem”. 275. 27. s. 20700-20706. PMID: 10748176.
Gunaratnam, L, Morley, M, Franovic, A, de Paulsen, N, Mekhail, K, Parolin, DA, Nakamura, E, Lorimer, IA, Lee, S. Hypoxia inducible factor activates the transforming growth factor-alpha/epidermal growth factor receptor growth stimulatory pathway in VHL^(-/-) renal cell carcinoma cells. „J Biol Chem”. 278. 45, s. 44966-44974, 2003. PMID: 12944410.

nature.com

Adryan, B, Decker, HJ, Papas, TS, Hsu, T. Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila. „Oncogene”. 19. 24, s. 2803-2811, 200. PMID: 10851083.

nih.gov

ncbi.nlm.nih.gov

Model utworzony na podstawie danych z Min JH, Yang, H, Ivan, M, Gertler, F, Kaelin Jr, WG, Pavletich, NP. Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling. „Science”. 296. 5574, s. 1886-1889, 2002. PMID: 12004076. (PDBid=1LM8), przy wykorzystaniu MBT Protein Workshop.
Seizinger BR, Rouleau GA, Ozelius LJ, Lane AH, Farmer GE, Lamiell JM, Haines J, Yuen JW, Collins D, Majoor-Krakauer D, et al. Von Hippel-Lindau disease maps to the region of chromosome 3 associated with renal cell carcinoma. „Nature”. 332. 6161, s. 268-269, 1988. PMID: 2894613.
Latif, F, Tory, K, Gnarra, J, Yao, M, Duh, FM, Orcutt, ML, Stackhouse, T, Kuzmin, I, Modi, W, Geil, L, et al. Identification of the von Hippel-Lindau disease tumor suppressor gene. „Science”. 260. 5112, s. 1235, 1993. PMID: 8493574.
Schoenfeld, A, Davidowitz, EJ, Burk, RD. A second major native von Hippel-Lindau gene product, initiated from an internal translation start site, functions as a tumor suppressor. „Proc Nat Acad Sci”. 95, s. 8817-8822, 1998. PMID: 9671762.
Iliopoulos, O, Kibel, A, Gray, S, Kaelin, WG, Jr. Tumour suppression by the human von Hippel-Lindau gene product. „Nature Medicine”. 1, s. 822-826, 1995. PMID: 7585187.
Iliopoulos, O, Onh, M, Kaelin, WG, Jr. pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation. „Proc Natl Acad Sci USA”. 95, s. 11661-11666, 1998. PMID: 9751722.
Hergovich, A, Lisztwan, J, Barry, R, Ballschmieter, P, Krek, W. Regulation of microtubule stability by the von Hippel-Lindau tumour supressor protein pVHL. „Natl Cell Biol”. 5, s. 64-70, 2003. PMID: 12510195.
Shiao, YH, Resau JH, Nagashima K, Anderson LM, Ramakrishna G. The von Hippel-Lindau tumor suppressor targets to mitochondria. „Cancer Res”. 60. 11, s. 2816-2819, 2000. PMID: 20306593.
Richards, FM, Schofield, PN, Fleming, S, Maher, ER. Expression of the von Hippel-Lindau disease tumor supressor gene during human embryogenesis. „Hum Mol Genet”. 5, s. 639-644, 1996. PMID: 8733131.
Renbaum, P, Duh, FM, Latif, F, Zbar, B, Lerman, MI, Kuzmin, I. Isolation and characterization of the full-length 3' untranslated region of the human von Hippel-Lindau tumor suppressor gene. „Human Genetics”. 98. 9, s. 666-671, 1996. PMID: 8931697.
Kessler, PM. Expression of the Von Hippel-Lindau tumor suppressor gene, VHL, in human fetal kidney and during mouse embryogenesis. „Mol Med”. 1, s. 457-466, 1995. PMID: 96091369.
Kibel, A, Iliopoulos, O, DeCaprio, JA, Kaelin, WG. Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C. „Science”. 269. 5229, s. 1400-1401, 1995. PMID: 7660130.
Pause A, Lee, S, Worrell, RA, Chen, DY, Burgess, WH, Linehan, WM, Klausner, RD. The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins. „Proc Natl Acad Sci U S A”. 94. 6, s. 2156-2161, 1997. PMID: 9122164.
Baek, JH, Liu, YV, McDonald, KR, Wesley, JB, Hubbi, ME, Byun, H, Semenza, GL. SSAT2 is an essential component of the Ubiquitin ligase complex that regulates HIF-1alpha. „J Biol Chem”. Epub, 2007. PMID: 17558023.
Maxwell, PH, Wiesener, MS, Chang, GW, Clifford, SC, Vaux, EC, Cockman, ME, Wykoff, CC, Pugh, CW, Maher, ER, Ratcliffe, PJ. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. „Nature”. 399. 6733, s. 271-275, 1999. PMID: 10353251.
Ohh, M, Yauch, RL, Lonergan, KM, Whaley, JM, Stemmer-Rachamimov, AO, Louis, DN, Gavin, BJ, Kley, N, Kaelin, WG, Iliopoulos, O. The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix. „Mol Cell”. 1. 7, s. 959-968, 1998. PMID: 9651579.
Mukhopadhyay, D, Knebelmann, B, Cohen, HT, Ananth, S, Sukhatme, VP. The von Hippel-Lindau tumor suppressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity. „Mol Cell Biol”. 17, s. 5629-5639, 1997. PMID: 97415639.
Okuda, H, Saitoh, K, Hirai, S, Iwai, K, Takaki, Y, Baba, M, Minato, N, Ohno, S, Shuin, T. The von Hippel-Lindau tumor suppressor protein mediates ubiquitination of activated atypical protein kinase C. „J Biol Chem”. 276. 47, s. 43611-43617, 2001. PMID: 11574546.
Pal, S, Claffey, KP, Dvorak, HF, Mukhopadhyay, D. The von Hippel-Lindau gene product inhibits vascular permeability factor/ vascular endothelial growth factor expression in renal cell carcinoma by blocking protein kinase C pathways. „J Biol Chem”. 272, s. 27509-27512, 1997. PMID: 98010573.
Li, Z, Wang, D, Na, X, Schoen, SR, Messing, EM, Wu, G. Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor. „Biochem Biophys Res Commun”. 294. 3, s. 700-709, 2002. PMID: 12056827.
Li, Z, Na, X, Wang, D, Schoen, SR, Messing, EM, Wu, G. Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. „J Biol Chem”. 277. 7, s. 4656-4662, 2002. PMID: 11739384.
Roe, J, Kim, H, Lee, S, Kim, S, Cho, E, Youn, H. p53 Stabilization and Transactivation by a von Hippel-Lindau Protein. „Molecular Cell”. 22. 3. s. 395-405. PMID: 16678111.
Kuznetsova AV, Meller J, Schnell PO, Nash JA, Ignacak ML, Sanchez Y, Conaway JW, Conaway RC, Czyzyk-Krzeska MF. von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination. „Proc Natl Acad Sci U S A”. 100. 5, s. 2706-2711, 2003. PMID: 12604794.
Cohen, HT, Zhou, M, Welsh, AM, Zarghamee, S, Scholz, H, Mukhopadhyay, D, Kishida, T, Zbar, B, Knebelmann, B, Sukhatme, VP. An important von Hippel-Lindau tumor suppressor domain mediates Sp1-binding and self-association. „Biochem Biophys Res Commun”. 266. 1, s. 43-50, 1999. PMID: 10581162.
Iwai, K, Yamanaka, K, Kamura, T, Minato, N, Conaway, RC, Conaway, JW, Klausner, RD, Pause, A. Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex. „Proc Natl Acad Sci U S A”. 96. 22, s. 12436-12441, 1999. PMID: 10535940.
Datta, K, Nambudripad, R, Pal, S, Zhou, M, Cohen, HT, Mukhopadhyay, D. Inhibition of insulin-like growth factor-I-mediated cell signaling by the von Hippel-Lindau gene product in renal cancer. „J Biol Chem”. 275. 27. s. 20700-20706. PMID: 10748176.
Davidowitz, EJ, Schoenfeld, AR, Burk, RD. VHL induces renal cell differentiation and growth arrest through integration of cell-cell and cell-extracellular matrix signaling. „Mol Cell Biol”. 21. 3, s. 865-874, 2001. PMID: 11154273.
Pause, A, Lee, S, Lonergan, KM, Klausner, RD. The von Hippel-Lindau tumor suppressor gene is required for cell cycle exit upon serum withdrawal. „Proc Natl Acad Sci U S A”. 95. 3, s. 993-998, 1998. PMID: 9448273.
Bindra, RS, Vasselli, JR, Stearman, R, Linehan, WM, Klausner, RD. VHL-mediated hypoxia regulation of cyclin D1 in renal carcinoma cells. „Cancer Res”. 62. 11, s. 3014-3019, 2002. PMID: 12036906.
Zatyka, M, da Silva, NF, Clifford, SC, Morris, MR, Wiesener,MS, Eckardt, KU, Houlston, RS, Richards, FM, Latif, F, Maher, ER. Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease. „Cancer Res”. 62. 13, s. 3803-11, 2002. PMID: 12097293.
Gunaratnam, L, Morley, M, Franovic, A, de Paulsen, N, Mekhail, K, Parolin, DA, Nakamura, E, Lorimer, IA, Lee, S. Hypoxia inducible factor activates the transforming growth factor-alpha/epidermal growth factor receptor growth stimulatory pathway in VHL^(-/-) renal cell carcinoma cells. „J Biol Chem”. 278. 45, s. 44966-44974, 2003. PMID: 12944410.
Hergovich, A, Lisztwan, J, Thoma, CR, Wirbelauer, C, Barry, RE, Krek, W. Priming-dependent phosphorylation and regulation of the tumor suppressor pVHL by glycogen synthase kinase 3. „Mol Cell Biol”. 26. 15, s. 5784-96, 2006. PMID: 16847331.
Woodward, ER, Buchberger, A, Clifford, SC, Hurst, LD, Affara, NA, Maher, ER. Comparative sequence analysis of the VHL tumor suppressor gene. „Genomics”. 65. 3. s. 253-265. PMID: 10857749.
Gao J, Naglich JG, Laidlaw J, Whaley JM, Seizinger BR, Kley N. Cloning and characterization of a mouse gene with homology to the human von Hippel-Lindau disease tumor suppressor gene: implications for the potential organization of the human von Hippel-Lindau disease gene. „Cancer Res”. 55. 4, s. 743-747, 1995. PMID: 7850784.
Adryan, B, Decker, HJ, Papas, TS, Hsu, T. Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila. „Oncogene”. 19. 24, s. 2803-2811, 200. PMID: 10851083.
Aso, T, Yamazaki, K, Aigaki, T, Kitajima, S. Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity. „Biochem Biophys Res Commun”. 276. 1, s. 355-361, 2000. PMID: 11006129.
Stebbins, CE, Kaelin, WG, Pavletich, NP. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. „Science”. 284. 5413, s. 455-461, 1999. PMID: 10205047.
Gnarra, JR, Ward, JM, Porter, FD, Wagner, JR, Devor, DE, Grinberg, A, Emmert-Buck, MR, Westphal, H, Klausner, RD, Linehan, WM. Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice. „Proc Natl Acad Sci U S A”. 94, s. 9102-9107, 1997. PMID: 97404355.
Shuin, T, Yamasaki, I, Tamura, K, Okuda, H, Furihata, M, Ashida, S. Von Hippel-Lindau disease: molecular pathological basis, clinical criteria, genetic testing, clinical features of tumors and treatment. „Japanese Journal of Clinical Oncology”. 36. 6, s. 337-343, 2006. PMID: 16818478.
Vortmeyer, AO, et al. Allelic deletion and mutation of the von Hippel-Lindau (VHL) tumor suppressor gene in pancreatic microcystic adenomas. „Am J Pathol”. 151, s. 951-956, 1997. PMID: 97468663.
Vortmeyer, AO, et al. Somatic von Hippel-Lindau gene mutations detected in sporadic endolymphatic sac tumors. „Cancer Res”. 60, s. 5963-5965, 2000. PMID: 20535963.
Hoebeeck J, Vandesompele J, Nilsson H, De Preter K, Van Roy N, De Smet E, Yigit N, De Paepe A, Laureys G, Påhlman S, Speleman F. The von Hippel-Lindau tumor suppressor gene expression level has prognostic value in neuroblastoma. „Int J Cancer”. 119 (3), s. 624-629, 2006. PMID: 16506218.
AttiyehA. EF AttiyehA. i inni, Chromosome 1p and 11q deletions and outcome in neuroblastoma., „The New England journal of medicine”, 353 (21), 2005, s. 2243-53, PMID: 16306521 .
W nawiasie podano alternatywną numerację – przez pewien czas niejasne było który kodon genu jest pierwszy; część badaczy numerowało nukleotydy i aminokwasy VHL od pierwszego kodonu sklonowanego cDNA (GenBank Accesion No L15409), obecnie wiadomo, że znajdującego się 71 kodonów przed kodonem start VHL; zobacz Kuzmin, I, Duh, FM, Latif, F, Geil, L, Zbar, B, Lerman, MI. Identification of the promoter of the human von Hippel-Landau disease tumor suppressor gene. „Oncogene”. 10, s. 2185-2194, 1995. PMID: 7784063.
Woodward, ER et al. Genetic predisposition to phaeochromocytoma: analysis of candidate genes GDNF, RET and VHL. „Hum Mol Genet”. 6, s. 1051-1056, 1997. PMID: 97358578.
Crossey, PA, Eng, C, Ginalska-Malinowska, M, Lennard, TW, Wheeler, DC, Ponder, BA, Maher, ER. Molecular genetic diagnosis of von Hippel-Lindau disease in familial phaeochromocytoma. „J Med Genet”. 32, s. 885-886, 1995. PMID: 8592333.
Neumann, HP, Bausch, B, McWhinney, SR, Bender, BU, Gimm, O, Franke, G, Schipper, J, Klisch, J, Altehoefer, C, Zerres, K, Januszewicz, A, Eng, C. Germ-line mutations in nonsyndromic pheochromocytoma. „New Eng J Med”. 346, s. 1459-1466, 2002. PMID: 12000816.
Pastore, Y, Jedlickova, K, Guan, Y, Liu, E, Fahner, J, Hasle, H, Prchal, JF, Prchal, JT. Mutations of von Hippel-Lindau tumor-suppressor gene and congenital polycythemia. „Am J Hum Genet”. 73, s. 412-419, 2003. PMID: 12844285.
Kanno, H, Kondo, K, Ito, S, Yamamoto, I, Fujii, S, Torigoe, S, Sakai, N, Hosaka, M, Shuin, T, Yao, M. Somatic mutations of the von Hippel-Lindau tumor suppressor gene in sporadic central nervous system hemangioblastomas. „Cancer Res”. 54, s. 4845-4847, 1994. PMID: 8069849.
Gilcrease, MZ, Schmidt, L, Zbar, B, Truong, L, Rutledge, M, Wheeler, TM. Somatic von Hippel-Lindau mutation in clear cell papillary cystadenoma of the epididymis. „Hum Path”. 26, s. 1341-1346, 1995. PMID: 8522307.
Brauch, H, Kishida, T, Glavac, D, Chen, F, Pausch, F, Hofler, H, Latif, F, Lerman, MI, Zbar, B, Neumann, HPH. Von Hippel-Lindau (VHL) disease with pheochromocytoma in the Black Forest region of Germany: evidence for a founder effect. „Hum Genet”. 95, s. 551-556, 1995. PMID: 7759077.
Bender, BU, Eng, C, Olschewski, M, Berger, DP, Laubenberger, J, Altehofer, C, Kirste, G, Orszagh, M, van Velthoven, V, Miosczka, H, Schmidt, D, Neumann, HPH. VHL c.505 T-C mutation confers a high age related penetrance but no increased overall mortality. „J Med Genet”. 38, s. 508-514, 2001. PMID: 11483638.
Neumann, HP et al. Consequences of direct genetic testing for germline mutations in the clinical management of families with multiple endocrine neoplasia, type II. „JAMA”. 274,, s. 1149-1151, 1995. PMID: 96011708.
Ritter, MM et al. Isolated familial pheochromocytoma as a variant of von Hippel-Lindau disease. „J Clin Endocrinol Metab”. 81, s. 1035-1037, 1996. PMID: 96368564.

pubmedcentral.nih.gov

Iwai, K, Yamanaka, K, Kamura, T, Minato, N, Conaway, RC, Conaway, JW, Klausner, RD, Pause, A. Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex. „Proc Natl Acad Sci U S A”. 96. 22, s. 12436-12441, 1999. PMID: 10535940.

oup.com

academic.oup.com

Richards, FM, Schofield, PN, Fleming, S, Maher, ER. Expression of the von Hippel-Lindau disease tumor supressor gene during human embryogenesis. „Hum Mol Genet”. 5, s. 639-644, 1996. PMID: 8733131.
Shuin, T, Yamasaki, I, Tamura, K, Okuda, H, Furihata, M, Ashida, S. Von Hippel-Lindau disease: molecular pathological basis, clinical criteria, genetic testing, clinical features of tumors and treatment. „Japanese Journal of Clinical Oncology”. 36. 6, s. 337-343, 2006. PMID: 16818478.

pnas.org

Iliopoulos, O, Onh, M, Kaelin, WG, Jr. pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation. „Proc Natl Acad Sci USA”. 95, s. 11661-11666, 1998. PMID: 9751722.
Kuznetsova AV, Meller J, Schnell PO, Nash JA, Ignacak ML, Sanchez Y, Conaway JW, Conaway RC, Czyzyk-Krzeska MF. von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination. „Proc Natl Acad Sci U S A”. 100. 5, s. 2706-2711, 2003. PMID: 12604794.
Pause, A, Lee, S, Lonergan, KM, Klausner, RD. The von Hippel-Lindau tumor suppressor gene is required for cell cycle exit upon serum withdrawal. „Proc Natl Acad Sci U S A”. 95. 3, s. 993-998, 1998. PMID: 9448273.
Gnarra, JR, Ward, JM, Porter, FD, Wagner, JR, Devor, DE, Grinberg, A, Emmert-Buck, MR, Westphal, H, Klausner, RD, Linehan, WM. Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice. „Proc Natl Acad Sci U S A”. 94, s. 9102-9107, 1997. PMID: 97404355.

sciencedirect.com

Ohh, M, Yauch, RL, Lonergan, KM, Whaley, JM, Stemmer-Rachamimov, AO, Louis, DN, Gavin, BJ, Kley, N, Kaelin, WG, Iliopoulos, O. The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix. „Mol Cell”. 1. 7, s. 959-968, 1998. PMID: 9651579.

umd.be

The UMD central website.

web.archive.org

https://web.archive.org/web/20070929081825/http://194.167.35.168:2200/4DACTION/W_PART_M [dostęp 24 czerwca 2007].
https://web.archive.org/web/20070929081819/http://194.167.35.168:2200/4DACTION/W_DEL_M [dostęp 24 czerwca 2007].