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101.
Tomoshiro Takeda Osamu Ueno Muneaki Samejima Takeshi Ohtani 《Journal of plant research》1985,98(4):393-411
Two hundred and twenty species of 38 genera in the Cyperaceae from Australia were examined for the possible occurrence of the C4 photosynthesis and the anatomical features of leaves and culms. The Kranz type of anatomy and the carbon isotope ratios typical of C4 plants were found in 84 species in the following six genera of four tribes belonging to subfamily Cyperoideae:Bulbostylis, Crosslandia, andFimbristylis (Fimbristylideae);Lipocarpha (Lipocarpheae);Cyperus (Cypereae);Rhynchospora (Rhynchosporeae). The anatomical observation revealed that the C4 species possessed any one of the three Kranz anatomical types found by previous investigators. It was suggested that in the Cyperaceae the C4 syndrome evolved independently within several taxa of the subfamily. The relative distribution of C3 and C4 species of the Cyperaceae in Australia was investigated by use of floristic data. It was recognized that the C4 species dominated in the northern part of the continent which was characterized by tropical and subtropical savannas and hot dry areas with summer rainfall, and the C3 species in the southern part, which contained temperate areas and mediterranean climatic areas with winter rainfall. 相似文献
102.
103.
Sumitomo Shinichiro Tatemoto Yukihiro Fukui Shin Nakamura Taka-aki Fukushima Shoji Ito Nobuyuki Mori Masahiko 《Virchows Archiv. B, Cell pathology including molecular pathology》1985,49(1):395-399
Virchows Archiv B Cell Pathology - Paget cells from cases of mammary and extramammary Paget’s disease were examined for carcinoembryonic antigen (CEA) and CEA-related antigens by the... 相似文献
104.
Isolation and physical mapping of temperature-sensitive mutants defective in heat-shock induction of proteins in Escherichia coli 总被引:25,自引:0,他引:25
Summary Mutants of Escherichia coli K12 that are partially or totally defective in induction of major heat-shock proteins and cannot grow at high temperature (42° C) were isolated by localized mutagenesis. These mutants carry a single mutation in the gene htpR (formerly hin) located at min 76 on the E. coli genetic map. Some mutants exhibit delayed (partial) induction of heat-shock proteins or require a higher temperature for induction than the wild type, whereas others are not induced under any of these conditions. The maximum temperature that allows growth varies among different mutants and is correlated with the residual induction capacity. Temperature-resistant revertants obtained from each mutant are fully or partially recovered in heat-shock induction. These results indicate that the inability of htpR mutants to grow at high temperature is due to the defect in heat-shock induction. In addition, a couple of mutants was found that produce significantly higher amounts of heat-shock proteins even at 30° C.The htpR gene has been cloned into plasmid pBR322 using the above mutants, and was localized to a DNA segment of 1.6 kilobase pairs. The mutants harboring certain palsmids that carry a part of htpR produce temperature-resistant recombinants at high frequency. This permits further localization of mutations within the htpR gene. Analysis of proteins encoded by each of the recombinant plasmids including the one carrying a previously isolated amber mutation (htpR165) led to the identification of a protein with an apparent molecular weight of about 36,000 daltons as the htpR gene product. 相似文献
105.
Identification of the secY (prlA) gene product involved in protein export in Escherichia coli 总被引:17,自引:0,他引:17
Koreaki Ito 《Molecular & general genetics : MGG》1984,197(2):204-208
Summary The gene secY (or prlA) is essential for protein export across the cytoplasmic membrane of Escherichia coli. The protein product of secY has been identified using the gene cloned under the control of the pL promoter of phage in combination with the maxicell system. The protein was found to have some unusual properties. First, it is important not to heat the protein at 100°C in the SDS sample buffer for its subsequent detection by gel electrophoresis. Second, migration of the protein in SDS-polyacrylamide gel electrophoresis is variable depending on the gel compositions. Gels with stronger sieving effect give higher apparent molecular weights. These properties are similar to those of hydrophobic proteins of the cytoplasmic membrane, such as the lactose permease. Finally, a major fraction of the protein synthesized from the overproducing plasmid is degraded rapidly in vivo. The altered protein from the secY24 mutant gene is even more unstable. These results provide information which is basic for the dissection of the protein export machinery of the bacterial cell. 相似文献
106.
Ken-ichi Yamamoto Osamu Hirano Yoichi Hara Hiroshi Yoshikawa 《Ichthyological Research》1987,33(4):399-404
A cyprinid fish,Pseudogobio esocinus showed gradual bradycardia at oxygen saturation (%) of less than 29.7±4.6 (1.89±0.29 ml/l of oxygen concentration), surfacing at 14.7±1.3 (0.94±0.09ml/l), drastic decrease of oxygen consumption at less than 14.2±0.8 (0.91 ±0.06ml/l) and asphyxia at 9.7±1.4 (0.62±0.09ml/l). The fish avoided water having low oxygen saturation of less than 54.0± 5.4 (3.38±0.30ml/l), and markedly at less than 26.2±3.4 (1.62±0.16 ml/l). 相似文献
107.
Hideya Hayashi Seiji Ito Teruo Tanaka Manabu Negishi Hideo Kawabe Yokohama Hiromitsu Kikuko Watanabe Osamu Hayaishi 《Prostaglandins & other lipid mediators》1987,33(4)
In view of the recent finding that prostaglandin D2 is stereospecifically converted to 9α,11β-prostaglandin F2, an isomer of prostaglandin F2α, a highly specific and sensitive radioimmunoassay for 9α,11β-prostaglandin F2 was developed and applied to determine the content of this prostaglandin in various rat tissues. Antisera against 9α-11β-prostaglandin F2 were raised in rabbits immunized with the bovine serum albumin conjugate, and [3H]9α,11β-prostaglandin F2 was enzymatically prepared from [3H]prostaglandin D2. The assay detected 9α,11β-prostaglandin F2 over the range of 20 pg to 1 ng, and the antiserum showed less than 0.04% cross-section with prostaglandin F2α, prostaglandin F2β and 9β,11β-prostaglandin F2. To avoid postmortem changes, tissues were frozen in liquid nitrogen immediately after removal. The basal level of 9α,11β-prostaglandin F2 was hardly detectable in various tissues of the rat examined, including spleen, lung, liver and brain; although it was found to be 0.31 ± 0.06 ng/g wet weight in the small intestine. During convulsion induced by pentylenetetrazole, enormous amounts of prostaglandin D2 (ca. 180 ng/g wet weight) and prostaglandin F2α (ca. 70 ng/g) were produced in the brain; however, 9α,11β-prostaglandin F2 was detected neither there nor in the blood. This result demonstrates that the conversion to 9α,11β-prostaglandin F2 is a minor pathway, if one at all, of prostaglandin D2 metabolism in the rat brain. 相似文献
108.
109.
110.
Altered translation initiation factor 2 in the cold-sensitive ssyG mutant affects protein export in Escherichia coli. 总被引:10,自引:0,他引:10
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The Escherichia coli gene secY (pr1A) codes for an integral membrane protein that plays an essential role in protein export. We previously isolated cold-sensitive mutations (ssy) as extragenic suppressors of temperature-sensitive secY24 mutation. Now we show that the ssyG class of mutations are within infB coding for the translation initiation factor IF2. The mutants produce altered forms of IF2 with a cold-sensitive in vitro activity to form a translation initiation complex. The mutation suppresses not only secY24 but also other secretion-defective mutations such as secA51 and rp10215. The beta-galactosidase enzyme activity of the MalE-LacZ 72-47 hybrid protein is strikingly reduced in the ssyG mutant at the permissive high temperature, while the hybrid protein itself is normally synthesized. This effect, which was observed only for the hybrid protein with a functional signal sequence, may result from some alteration in the cellular localization of the protein. These results suggest that IF2 or the translation initiation step can modulate protein export reactions. The isolation of cold-sensitive ssyG mutations in infB provides genetic evidence that IF2 is indeed essential for normal growth of E. coli cells. 相似文献