オルニチンデカルボキシラーゼ (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "オルニチンデカルボキシラーゼ" in Japanese language version.

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22nih.gov

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13doi.org

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1rcsb.org

8,838^th place

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1sourceforge.net

1,669^th place

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1ulg.ac.be

7,875^th place

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1escholarship.org

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doi.org

“Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases”. Structure 7 (5): 567–81. (May 1999). doi:10.1016/S0969-2126(99)80073-2. PMID 10378276.
“Characterization of the reaction mechanism for Trypanosoma brucei ornithine decarboxylase by multiwavelength stopped-flow spectroscopy”. Biochemistry 36 (49): 15147–55. (December 1997). doi:10.1021/bi971652b. PMID 9398243.
PDB: 1d7k; “Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding”. J. Mol. Biol. 295 (1): 7–16. (January 2000). doi:10.1006/jmbi.1999.3331. PMID 10623504. ; rendered via PyMOL.
“The ornithine decarboxylase gene is essential for cell survival during early murine development”. Mol. Cell. Biol. 21 (19): 6549–58. (October 2001). doi:10.1128/MCB.21.19.6549-6558.2001. PMC 99801. PMID 11533243.
“Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate”. EMBO J. 22 (7): 1488–96. (April 2003). doi:10.1093/emboj/cdg158. PMC 152902. PMID 12660156.
“Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination”. Mol. Cell 5 (2): 403–10. (February 2000). doi:10.1016/S1097-2765(00)80435-9. PMID 10882081.
“A proteasome howdunit: the case of the missing signal”. Cell 101 (4): 341–4. (May 2000). doi:10.1016/S0092-8674(00)80843-0. PMID 10830160.
“The ornithine decarboxylase gene is a transcriptional target of c-Myc”. Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7804–8. (August 1993). doi:10.1073/pnas.90.16.7804. PMC 47231. PMID 8356088.
“Polyamines and cancer: old molecules, new understanding”. Nat. Rev. Cancer 4 (10): 781–92. (October 2004). doi:10.1038/nrc1454. PMID 15510159.
“A definitive role of ornithine decarboxylase in photocarcinogenesis”. Am. J. Pathol. 159 (3): 885–92. (September 2001). doi:10.1016/S0002-9440(10)61764-6. PMC 1850478. PMID 11549581.
“Comparison of androgen regulation of ornithine decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent kidney and accessory sex organs”. Endocrinology 130 (3): 1131–44. (March 1992). doi:10.1210/en.130.3.1131. PMID 1537280.
“Ornithine decarboxylase induction and polyamine synthesis in the kindling of seizures: the effect of alpha-difluoromethylornithine”. Epilepsy Res. 11 (1): 3–7. (1992). doi:10.1016/0920-1211(92)90015-L. PMID 1563337.
“Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis”. Amino Acids 33 (2): 359–66. (August 2007). doi:10.1007/s00726-007-0537-9. PMID 17610127.

escholarship.org

“Polyamines and cancer: old molecules, new understanding”. Nat. Rev. Cancer 4 (10): 781–92. (October 2004). doi:10.1038/nrc1454. PMID 15510159.

nih.gov

pubmed.ncbi.nlm.nih.gov

“Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases”. Structure 7 (5): 567–81. (May 1999). doi:10.1016/S0969-2126(99)80073-2. PMID 10378276.
“Characterization of the reaction mechanism for Trypanosoma brucei ornithine decarboxylase by multiwavelength stopped-flow spectroscopy”. Biochemistry 36 (49): 15147–55. (December 1997). doi:10.1021/bi971652b. PMID 9398243.
PDB: 1d7k; “Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding”. J. Mol. Biol. 295 (1): 7–16. (January 2000). doi:10.1006/jmbi.1999.3331. PMID 10623504. ; rendered via PyMOL.
“The ornithine decarboxylase gene is essential for cell survival during early murine development”. Mol. Cell. Biol. 21 (19): 6549–58. (October 2001). doi:10.1128/MCB.21.19.6549-6558.2001. PMC 99801. PMID 11533243.
“Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate”. EMBO J. 22 (7): 1488–96. (April 2003). doi:10.1093/emboj/cdg158. PMC 152902. PMID 12660156.
“Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination”. Mol. Cell 5 (2): 403–10. (February 2000). doi:10.1016/S1097-2765(00)80435-9. PMID 10882081.
“A proteasome howdunit: the case of the missing signal”. Cell 101 (4): 341–4. (May 2000). doi:10.1016/S0092-8674(00)80843-0. PMID 10830160.
“The ornithine decarboxylase gene is a transcriptional target of c-Myc”. Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7804–8. (August 1993). doi:10.1073/pnas.90.16.7804. PMC 47231. PMID 8356088.
“Polyamines and cancer: old molecules, new understanding”. Nat. Rev. Cancer 4 (10): 781–92. (October 2004). doi:10.1038/nrc1454. PMID 15510159.
“A definitive role of ornithine decarboxylase in photocarcinogenesis”. Am. J. Pathol. 159 (3): 885–92. (September 2001). doi:10.1016/S0002-9440(10)61764-6. PMC 1850478. PMID 11549581.
“Role of asbestos and active oxygen species in activation and expression of ornithine decarboxylase in hamster tracheal epithelial cells”. Cancer Res. 51 (1): 167–73. (January 1991). PMID 1846307.
“Comparison of androgen regulation of ornithine decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent kidney and accessory sex organs”. Endocrinology 130 (3): 1131–44. (March 1992). doi:10.1210/en.130.3.1131. PMID 1537280.
“Development of difluoromethylornithine (DFMO) as a chemoprevention agent”. Clin. Cancer Res. 5 (5): 945–51. (May 1999). PMID 10353725.
“Ornithine decarboxylase induction and polyamine synthesis in the kindling of seizures: the effect of alpha-difluoromethylornithine”. Epilepsy Res. 11 (1): 3–7. (1992). doi:10.1016/0920-1211(92)90015-L. PMID 1563337.
“Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis”. Amino Acids 33 (2): 359–66. (August 2007). doi:10.1007/s00726-007-0537-9. PMID 17610127.

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

rcsb.org

PDB: 1d7k; “Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding”. J. Mol. Biol. 295 (1): 7–16. (January 2000). doi:10.1006/jmbi.1999.3331. PMID 10623504. ; rendered via PyMOL.

sourceforge.net

pymol.sourceforge.net

PDB: 1d7k; “Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding”. J. Mol. Biol. 295 (1): 7–16. (January 2000). doi:10.1006/jmbi.1999.3331. PMID 10623504. ; rendered via PyMOL.

ulg.ac.be

orbi.ulg.ac.be

“The ornithine decarboxylase gene is essential for cell survival during early murine development”. Mol. Cell. Biol. 21 (19): 6549–58. (October 2001). doi:10.1128/MCB.21.19.6549-6558.2001. PMC 99801. PMID 11533243.