請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75155
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Hann-chang Hsiung | en |
dc.contributor.author | 熊漢昌 | zh_TW |
dc.date.accessioned | 2021-07-01T08:12:01Z | - |
dc.date.available | 2021-07-01T08:12:01Z | - |
dc.date.issued | 2000 | |
dc.identifier.citation | Archer, S. N. and Hirano, J. (1998) Rod opsin sequence in the John Dory: Further evidence for the spectral tuning of rhodopsin. Journal of Fish Biology 52, 209-212. Archer, S. N. and Hirano, J. (1996) Absorbance spectra and molecular structure of the blue-sensitive rod visual pigment in the conger eel (Conger conger). Proceedings of the Royal Society of London B 263, 761-767. Archer, S. N. and Hirano, J. (1997) Opsin sequences of the rod visual pigments in two species of Poeciliid fish. Journal of Fishery Biology 51, 215-219. Archer, S. N., Hope, A. and Partridge, J. C. (1995) The molecular basis for the green-blue sensitive shift in the rod visual pigments of the European eel. Proceedings of the Royal Society of London B 262, 289-295. Archer, S. N. and Lythgoe, J. N. (1990) The visual pigments basis for cone polymorphism in the guppy, Poecilia reticulata. Vision Research 30, 225-233. Archer, S. N., Lythgoe, J. N. and Hall, L. (1992) Rod opsin cDNA sequence from the sand goby (Pomatoschistus minutus) compared with those of other vertebrates. Proceedings of the Royal Society of London B 248, 19-25. Asenjo, A. B., Rim, J. and Oprian, D. (1994) Molecular determinants of human red/green color discrimination. Neuron 12, 1131-1138. Baehr, W, Falk, J. D., Bugra, K., Trianthaafyllos, J. T. and McGinnis, J. F. (1988) Isolation and analysis of the mouse opsin gene. Federation of European Biochemical Societies Letters 238, 253-256. Baiwin, J. M. (1993) The probable arrangement of the helices in G protein- coupled receptors. The EMBO Journal 12, 1693-1703. Batni, S., Scalzetti, L., Moody, S. A. and Knox, B. E. (1996) Characterization of the Xenopus rhodopsin gene. The Journal of Biological Chemistry 271, 3179- 3186. Baylor, D. A., Lythgoe, R. J. and Tansley, K. (1936) Some new forms of visua1 purple found in deep-sea fish, with a note on the visual cells of origin. Proceedings of the Royal Society of London B 816, 95-113. Beatty, D. D. (1984) Visual pigments and the labile scoptopic visual system of fish. Vision Research 24, 1563-1573. Best, A. C. and Nicol, J. A. (1980) Eyeshine in fishes. A review of ocular reflectors. Canadian Journal of Zoology 58, 945-956 Bowmaker, J. K., Astell, S., Hunt, D. M. and Mollon, J. D. (1991) Photosensitive and photostable pigments in the retinae of Old World monkey. Journal of Experimental Biology 156, 1-19. Bowmaker, J. K. and Kunz, Y. W. (1987) Ultraviolet receptors, tetrachromatic colour vision and retinal mosiacs in the brown trout (Salmo trutta): age dependent change. Vision Research 27,2102-2108. Brown, A. J. H., Perry, S. J., Saunders, S. E. and Burke, J. F. (1999). Extender PCR: A method for the isolation of sequences regulating gene expression from genomic DNA. BioTechniques 26, 804-806. Bowmaker, J. K., Thorpe, A and Douglas, R. H. (1991) Ultraviolet-sensitive cones in the goldfish. Vison Research 31,349-352. Bridges, C. D. B. (1972) The rhodopsin-porphyropsin visual system. In Dartnall, H. J. A. (Ed.), Handbook of sensory physiology, VII/1 417-480 Berlin: Springer. Chang, B. S. W, Crandall, K. A., Carulli, J. P. and Hartyl, D. L. (1995) Opsin phylogeny and evolution: A model for blue shifts in wavelength regulation. Molecualr Phylogenetic Evolution 4,31-43. Chen, S., Wang, Q. -L., Nie, Z., Sun, H., Lennon, G., Copeland, N. G., Gilbert, D. J., Jenkins, N. A. and Zack, D. J. (1997) Crx, a novel Otx-like pairedhomeodomain protein, binds to and transactivates photoreceptor cell-specific genes. Neuron 19, 10 17-1030. Clarke, G. L. (1936) On the depth at which fishes can see. Ecology 17, 452-456. Cohen, J. L. (1991) Adaptations for scotopic vision in the lemon shark (Negaprion brevirostris). Journal of Expenmental Zoology 5, 76-84. Crescitelli, F. (1991) Adaptations of visual pigments to the photic environment of the deep-sea. Journal of Experimental Zoology 5, 66-75. Crescitelli, F., McFafl-Ngai, M. and Horwitz, J. (1985) The visual pigment sensivitity hypothesis: further evidence from fishes of varying habitats. Journal of Comparative Physiology A 157, 323-333. Crisan, D. and Mattson, J. C. (1993) Retrospective DNA analysis using fixed tissue speicmens. DNA and Cell Biology 12,455-464. Denton, E. J., Gilpin-Brown, J. B. and Wright, P. G. (1970) On the ‘filters’ in the photophores of mesopelagic fish and on a fish emitting red light and especially sensitive to red light. Journal of Physiology (London) 208,72-73. Denton, E. J., Herring, P. J., Widder, E. A., Latz, M. F. and Case, J. F. (1985) The roles of filters in the photophores of oceanicanimals and their relation to vision in the oceanic environment. Proceedings of the Royal Society of London B 225, 63-97. Douglas, R. H. and Partridge, J. C. (1997) On the visual pigments of deep-sea fish. Journal of Fish Biology 50, 68-85. Douglas, R. H., Partridge, J. C. and Hope, A. J. (1995) Visual and lenticular pigments in the eyes of demersal deep-sea fishes. 177, Journal of Comparative Physiology A 111-122. Dratz, E. A. and Hargrave, P A. (1983) The structure of rhodopsin and the outer segment disc membrane. Trends in Biochemical Science 8, 128-13 1. Dubeau, L., Chandler, L. A., Gralow J. R., Nicholz, P. W. and Jones, P. A. (1986) Southern blot analysis of DNA extracted from formalin-fixed pathology specimens. Cancer Research 46, 2964-2969. Fasick, J. I and Robinson, P R. (1998) Mechanism of spectral tuning in the dolphin visual pigments. Biochemistry 37,433-438. Fernandez, H. R. C. (1978) Visual pigments of bioluminescent and non- bioluminescent deep-sea fishes. Vision Research 18, 589-592. Fey, M. F., Piikington, S. P., Summer, C. and Wainscoat, J. S. (1987) Molecular diagnosis of haematological disorders using DNA from stored bone marrow slides. Br. J. Haematol. 67,489-492. Fitzgibbon, J., Hope, A. J., Slobodyanyuk, S. J., Bellingham, J., Bowmaker, J. K. and Hunt, D. M. (1995) The rhodopsin-encoding gene of bony fish lacks introns. Gene 164, 273-277. Fukuda, M. N., Papermaster, D. P. and Hargrave, P. A (1979) Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near NH2 terminus. Journal of Biological Chemistry 254, 820 1-8207. Goelz, S. E., Hamilton, S. R. and Vogeistein, B. (1985) Purification of DNA from formaldehyde fixed and paraffin embedded human tissue. Biophysical and Biophysical Research Communication2. 130, 118-126. Gouras, P., Kjeldbye, H. and Zack, D. J. (1994) Reporter gene expression in cones in transgenic mice carrying bovine rhodopsin promoter/lacZ transgenes. Visual Neuroscience 11, 1227-1231. Hargrave, P A. (1977) The amino-terminal tryptic peptide of bovine rhodopsin. A glycopeptide containing two sites of oligosaccharide attachment. Biochimica et Biophysica Acta 492, 83-94. Harosi, F. I. and Hashimoto, Y. (1983) Ultraviolet visual pigment in a vertebrate: a tetrachromatic cone system in the dace. Science 222, 1021-1023. Herring, P. J. (1983) The spectral characteristics of luminous marine organisms. Proceedings of the Royal Society of London B 220, 183-217. Hope, A. J., Partridge, J. C. Dulai, K. S. and Hunt, D. M. (1997) Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes. Proceedings of the Royal Society of London B 264, 155-163. Hunt, D. M., Fitzgibbon, J. Sloboldyanyuk, S. J. and Bowmaker, J. K. (1996) Spectral tuning and molecualr evolution of rod visual pigments in the species flock of cottoid fish in Lake Baikal. Vision Research 26, 1217-1224. Inoue, H., Nojima, H. and Okayama, H. (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96,23-28. Jerlov, N. G. (1976) Marine potics. Elserier Scientific: Amsterdam. Johnson, R L., Grant, K. B., Zankel, T. C., Boehm, M. F., Merbs, S. L., Nathans, J. and Nakanishi, K. (1993) Cloning and expression of goldfish opsin sequences. Biochemistry 32, 208-214. Kampa, E. M. (1970) Underwater daylight and moonlight measurements in the Eastern North Atlantic. Journal of the Marine Biological Association of thetion of DNA from formaldehyde fixed and paraffin embedded human tissue. Biochemical and United Kingdom 50, 391-420. Kamik, S. S. and Khorana, H. G. (1990) Journal of Biological Chemistry 265, 17520-17524. Kamik, S. S., Sakmar, T. P, Chen, H. -B. and Khorana, H. G. (1988) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proceedings of the National Academy Science of the United States of America 85, 8459-8463. Knox, B. E., Schlueter, C., Sanger, B. M., Green, C. B. and Besharse, J. C. (1998) Transgene exrepssion in Xenopus rods. Federation of European Biochemical Societies Letters 423, 117-121. Kumar, R., Chen, S., Scheurer; D., Wang, Q. L., Duh, E., Sung, C. H., Rehemtulla, A., Swqroop, A., Adler, R. and Zack, D. J. (1996) The bZIP transcription factor Nrl stimulates rhodopsin promoter activity in primary retinal cell cultures. The Journal of Biological Chemistry 271,29612-29618. Latz, M. I., Frank, T. M.and Case, J. F. (1988) Spectral composition of bioluminescence of epipelagic organisms from the Sargasso sea. Marine Biology 98,441-446. Lem, J., Applebury, M. L., Falk, J. D., Flannery, J. G. and Simon, M. I. (1991) Tissue-specific and developmental regulation of rod opsin chimeric genes in transgenic mice. Neuron 6,201-210. Liang, C. J., Yamashits, K. Muellenberg, C. G., Shichi, H. and Kobata, A. (1979) Journal of Biological Chemistry 254,6414-6418. Lim, J., Chang, J. L. and Tsai, H. J. (1997) A second type of rhodopsin cDNA from the common carp (Cyprinus carpio). Biochimica et Biophysica acta 1352, 8-12. Locket, N. A. (1977) Adaptations to the deep-sea environment. In Handbook of sensory physiology, vol. VII/5, pp. 67-192. Berlin: Springer-Verlag. Locket, N. A. (1992) Problems of deep foveas. Australia and New Zealand Journal of Ophthalmology 20, 28 1-295. Loew, E. R. and Dartnall, H. J. A. (1976) Vitamin A1/A2-based visual pigment mixtures in cones of the rudd. Vision Research 16, 891-896. Lythgoe, J. N. (1972) The Ecology of Vision. Oxford: Clarendon Press. McFarland, W. N. and Loew, E. R. (1994) Ultraviolet visual pigments in marme fishes of the family Pomacentridae. Vision Research 34, 1393-3396. Merbs, S. L. and Nathans, J. (1993) Role of hydroxyl-bearing amino acids in differentially tuning the absorption spectra of the human red and green cone pigments. Photochemistry and Photobiology 58, 706-710. Morabito, M. A., Yu, X. and Barnstable, C. J. (1991) Characterization of developmentally regulated and retina-specffic nuclear protein binding to a site in the upstream region of the rat opsin gene. The journal of Biological Chemistry 266,9667-9672. Munk, O. (1966) Ocular anatomy of some deep-sea teleosts. In Dana report. pp. 1-62. Copenhagen: Carlsburg Foundation. Nakayama, T. A. and Khorana, H. G. (1991) Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in the bovine rhodopsin. Journal of Biological Chemistry 266,4269-4275. Nathans, J. (1990) Determinants of visual pigment absorbances-role of charged amino acids in the putative transmembrane segments. Biochemistry 29, 937-942. Nathans, J. and Hogness, D. S. (1983) Isolation, sequence analysis and intronexon arrangement of the gene encoding bovine rhodopsin. Cell 34, 807-8 14. Nathans, J. and Hogness, D. S. (1984) Isolation and necleotide sequence of the gene encoding human rhodopsin. Proceedings of the National Academy Science of the United States of America 81, 4851-4855. Neitz, M., Neitz, J. and Jacobs, G. H. (1991) Spectral tuning of pigments underly color vision. Science 252, 97 1-974. Nelson, J. S. (1994) Fishes of the world. 3rd edn. New York: John Wiley. Neumeyer, C. (1992) Tetrachromatic color vision in goldfish: evidence from color mixture experiments. Journal of Comparative Physiology 171, 639-649. Nicol, J. A. C. (1969) Bioluminescence. In: Fish Physiology (W. S. Hoar and D. J. Randall, eds) pp. 355-400. Vol. III, Academic Press, New York. Ovchinnikov, Y. A., Abdulae N. G. and Bogachuk, A. S. (1988) Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitoylated. Federation of European Biochemical Societies Letters 230,1-5. Pankhurst, N. W. (1987) Intraspecific and interspecific changes in retianl morphology among mesopelagic and demersal teleosts from the slope waters of New Zealand. Environmental Biology of Fishes 19,269-280. Pargridge, J. C., Archer, S. N. and Lythgoe, J. N. (1988) Visual pigments in the individual rods of deep-sea fishes. Journal of Comparative Physiology A 162, 543-550. Partridge, J. C., Shand, J., Archer, S. N., Lythgoe, J. N. and van Groningen Luyben, W. A.. H. M. (1989) Interspecific variation in the visual pigments of deep-sea fishes. Journal of Comparative Physiology A 164, 513-529. Partridge, J. C., Archer, S. N. and van Oostrum, J. (1992) Single and multiple visual pigments in deep-sea fishes. Journal of the Marine Biological Association of the United Kingdom 72, 113-130. Partridge, J. C. and Douglas, R. H. (1995) Far-red sensitivity in the deep-sea dragon fish Aristostomias titmanni. Nature 375, 21-22. Provencio, I., Loex E. R. and Foster, R. G. (1992) Vitamin A2-based visual pigments in fully terrestrial vertebrates. Vision Research 12, 2201-2208. Rehemtulla, A., Warwar, R., Kumar, R., Ji, X., Zack, D. J. and Swaroop, A. (1996) The basic motif-leucine zipper transcription factor Nrl can positively regulate rhodopsin gene expression. Proceedings of the National Academy Science of the United States of America 93, 191-195. Robinson, J. Schmitt, E. A. and Dowling, J. (1995) Temporal and spatial patterns of opsin gene expression in zebrafish (Danio rerio). Visual Neuroscience 12, 895-906. Sakamar, T. P, Franke, R. R. and Khorana, G. H. (1989) Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proceedings of the National Academy Science of the United States of America 86, 8309-8313. Sambrook, J., Fritsch, B. F. and Maniatis, T. (1989) Molecular Cloning, vol. 2, Cold Spring Harbor Laboratory Press, U.S.A. Su, C. Y, Lim, J. and Tsai, H. J. (1999) Structural characterization and transcriptional pattern of two types of carp rhodopsin gene. Comparative Biochemistry and Physiology part B ,in press. Takao, M., Yasui, A. and Tokunaga, F. (1988) Isolation and sequence determination of the chicken rhodopsin gene. Vision Research 28,471-480. Tamura, T., Hanyu, I. and Niwa, H. (1972) Spectral sensitivity and color vision in Skipjack tuna and related species. Bulletin of the Japanese Seciety of Scientific Fishieries 38, 799-802. Thompson, P. and Findlay, J. B. C. (1984) Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites. Biochemical Journal 220,773-780. Tsai, H. J., Shih, S. R., Kuo, C. M. and Li, L. K. (1994) Molecular cloning of the common carp (Cyprinus carpio) rhodopsin cDNA. Comparative Biochemistry and Physiology Part B 109, 8 1-88. Wald, G. (1936) Carotenoid and the visual cycle. Journal of Gen. Physiology 19, 351-371. Wald, G. (1936) Pigments of the retina. Journal of Gen. Physiology 19, 781-795. Warford, A., Pringle, J. H., Hay, J. Henderson, S. D. and Lander, I. (1988) Southern blot analysis of DNA extracted from formol-saline fixed and paraffin wax embedded tissue. Journal of Pathology 154, 313-320. Weiss, L. and Reinberg, D. (1992) FASEB J. 6, 3300-3309. Whitmore, A. V. and Bowmaker, J. K. (1989) Seasonal variation in cone sensitivity and short-wave absorbing visual pigments in the rudd, Scardinitus erythrophthalamus. Journal of Comparative Physiology A 166, 103-115. Widder, E. A., Latz, M. I. And Case, J. F. (1983) Marine bioluminescence spectra measured with an optical multi-channel detection system. Biological Bulletin 165, 791-810. Widder, E. A., Latz, M. I., Herring , P. J. and Case, J. F. (1984) Far-red bioluminescence from two deep-sea fishes. Science 225, 512-514. Wilden, U. and Kuhn, H. (1982) Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. Biochemistry 3014-3022. Williams, A. J., Hunt, D. M., Bowmaker, J. K. and Mollon, J. D. (1992) The polymorphic photopigments of The marmoset: spectral tuning and genetic basis. EMBO Journal 11, 2039-2045. Yokoyama, R. and Yokoyama, S. (1993) Molecular characterization of a blue visual pigment gene in the fish Astyanax fasciatus. Federation of European Biochemical Societies Letters 334, 27-31. Yu, X., Chung, M., Morabito, M. A. and Barnstable, C. J. (1993) Shared nuclear protein binding sites in the upstream region of the rat rod opsin gene. Biochemical and Biophysical Research Communications 191, 76-82. Zack, D. J., Bennett, J., Wang, Y, Davenport, C., Klaunberg, B., Gearhart, J. and Nathans, J. (1991) Unusual topology of bovine rhodopsin promoter-lacZ fusion gene expression in the transgenic mouse retinas. Neuron 6, 197-199. 馬國欽(1999) Characterization of the regulatory elements of the common carp (Cyprinus carpio) rhodopsin gene. 碩士論文 國立臺灣大學 | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75155 | - |
dc.description.abstract | 視紫質蛋白(Rhodopsin, Rho)位於視網膜的視桿細胞,主要的功能是把外界環境的光線轉換成神經訊息,是脊椎動物感應弱光的主要分子。我們選擇了兩種生活在不同光譜環境的魚類作為實驗材料:第一種是棲息在水深 1000 至 5000 公尺深海的黑龍魚,該處只有微弱的藍光和生物螢光;第二種是大洋迴遊性的鮪魚,其生活在海水的表層。我們利用 extender PCR 的方法複殖了這兩種魚類的 Rho 基因,包括 5 端上游調控序列、 coding region 以及 3 端下游的序列。黑龍魚是第一種完整 Rho 基因被發表的深海魚類。 在Rho胺基酸序列的比對中發現,黑龍魚和鮪魚的 Rho 均保有在結構上或功能上重要、在各物種間均保守的胺基酸。在其影響吸收光譜的胺基酸方面,黑龍魚的 Rho 在第 83 和第 292 位置分別是 asparagine 及 serine,這兩個位置特殊的胺基酸可能造成 Rho 吸收光譜向短波長偏移,適應在深海微弱的藍光;而鮪魚 Rho 在第 83 和第 292 位置則為 aspartate 及 alanine,與其餘水錶層魚類的 Rho 相同。在Rho基因上游調控區域的序列比對中,發現黑龍魚和鮪魚的Rho基因均具有與哺乳動物、鳥類Rho基因 cis-element 相近的 BAT-1 核心序列(GGATTANZ2-5ATTA) (-120 to -90),以及在鯉魚 Rho 基因位於-52 to -46 處其 antisense 那一股的序列與哺乳動物Rho基因的 Ret-4 核心序列同源性極高的 GTAATCC (carp specific element)。然而在哺乳動物、鳥類和鯉魚 Rho 基因之間保守的 NRE element (-75 to -64),黑龍魚和鮪魚 Rho 基因卻只具有其前半段 TGCTGA 的同源;而不具有後半段 CAGCC 的同源。而因 CAGCC 是鯉魚視網膜核蛋白結合的位置,且不被哺乳動物 Nrl 抗體所辨認 (馬,1999),故推論魚類和哺乳動物結合在NRE上的核蛋白可能不盡相同,且作用在不同的位置上。 | zh_TW |
dc.description.abstract | The main function of rhodopsin (Rho) that located in rod cells of retina is to transfer the light of outer environment into nervous signal. Rho is the main molecule to detect the dim light. Two kinds of fish lived in different spectral environments are chosen as the experimental materials. The first one is black dragonfish habitated in the deep sea at depth 1000 to 5000 m, where only weak blue light and bioluminescence exist. The second is tuna lived in the surface of ocean. The extender PCR is employed to clone the Rho genes of the two kinds of fish which included 5’ upstream regulatory region, coding region and 3’ downstream sequences. The black dragonfish is the first deep-sea fish whose Rho gene has been published. From the comparison of the deduced amino acid sequence, it revealed that both tuna and black dragonfish maintain some amino acids of structural or functional importance are conserved among species. The positions 83 and 292 of black dragonfish Rho are asparagine and serine, and the two special amino acids may cause Rho absorption spectrum to shift to short wavelength and adapt to deep-sea weak blue light. For the tuna, the positions 83 and 292 of Rho are aspartate and alanine, are the same as other surface-dwelling fish. From the comparison of Rho gene upstream regulatory region, it revealed that both the Rho genes of tuna and dragonfish have the BAT-1 core sequence (GGATTN2-5ATTA) (-120 to -90) similar to that of mammals and birds. We also found homologous sequences of carp specific element GTAATCC (-52 to -46) which antisense sequences are homologous to the core sequences of Ret-4 in mammals. There are conservative NRE element (-75 to -64) existing between the Rho gene of mammals, birds and carp. However, black dragonfish and tuna have only the former half homologous segment TGCTGA, not the later half segment. Because CAGCC is the binding site of carp nuclear proteins and is not recognized by the Nrl antibodies of mammals (Ma, 1999), hence, it is presumed that nuclear proteins binding on the NRE of fishes and mammals are probably not the same and act on different locations. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:12:01Z (GMT). No. of bitstreams: 0 Previous issue date: 2000 | en |
dc.description.tableofcontents | 中文摘要. . . . . . . . . . . .I Abstract . . . . . . . . . . . .II 前言. . . . . . . . . . . .1 材料與方法. . . . . . . . . . . .7 結果與討論. . . . . . . . . . . .14 參考文獻. . . . . . . . . . . .22 圖表. . . . . . . . . . . .34 | |
dc.language.iso | zh-TW | |
dc.title | 鮪魚與深海性黑龍魚視紫質基因之分子選殖與結構分析 | zh_TW |
dc.title | Molecular cloning and structure analysis of the rhodopsin genes of tuna (Tunnus tonggol) and deep-sea black dragonfish (Idiacanthus antrostmus) | en |
dc.date.schoolyear | 88-2 | |
dc.description.degree | 碩士 | |
dc.relation.page | 47 | |
dc.rights.note | 未授權 | |
dc.contributor.author-dept | 生命科學院 | zh_TW |
dc.contributor.author-dept | 漁業科學研究所 | zh_TW |
顯示於系所單位: | 漁業科學研究所 |
文件中的檔案:
沒有與此文件相關的檔案。
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。