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Caccone A; Moriyama EN; Gleason JM; Nigro L; Powell JR 《Molecular biology and evolution》1996,13(9):1224-1232
Drosophila melanogaster belongs to a closely related group of eight species
collectively known as the melanogaster subgroup; all are native to
sub-Saharan Africa and islands off the east coast of Africa. The
phylogenetic relationships of most species in this subgroup have been well
documented; however, the three most closely related species, D. simulans,
D. sechellia, and D. mauritiana, have remained problematic from a
phylogenetic standpoint as no data set has unambiguously resolved them. We
present new DNA sequence data on the nullo and Serendipity-alpha genes and
combine them with all available nuclear DNA sequence data; the total data
encompass 12 genes and the ITS of rDNA. A methodological problem arose
because nine of the genes had information on intraspecific polymorphisms in
at least one species. We explored the effect of inclusion/exclusion of
polymorphic sites and found that it had very little effect on phylogenetic
inferences, due largely to the fact that 82% of polymorphisms are
autapomorphies (unique to one species). We have also reanalyzed our
previous DNA-DNA hybridization data with a bootstrap procedure. The
combined sequence data set and the DNA-DNA hybridization data strongly
support the sister status of the two island species, D. sechellia and D.
mauritiana. This at least partially resolves what had been a paradox of
parallel evolution in these two species.
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INTRoDUCTIoNlYho1iumrePensL,whiteclover,isaneconomicallyimportantplantspeciesintemperatepastures.Asbrieflyreportedby[1],ithas16pairsofchromosomes(2n=32).Asyet,nodetailedcytologicalexaminationofthisspecies,suchasC-banding,hasbeenrep0rted.Inthelastdecade,thetechnique0fC-bandinghasbeenusedt0examinehighlyrepeatedsequencesinplantchrom0s0mesandhasprovidedausefultoolf0rtheanalysis0fcyt0geneticstructureincr0pplants[2-71.Inplants,thechr0m0s0mall0calizationofhighlyrepeatedDNAsequencesbyinsituhybr… 相似文献
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The period (per) locus has received much attention in molecular evolution
studies because it is one of the best studied "behavioral genes" and
because it offers insight into the evolution of repetitive sequences. We
studied most of the coding region of per in Drosophila willistoni and
confirmed previously observed patterns of conservation and divergence among
distantly related species. Five regions are so highly diverged that they
cannot be aligned, whereas a region encompassing the PAS domain is very
conserved. Structural and nucleotide polymorphism patterns in the
willistoni group are not the same as those observed in previously studied
species. We sequenced the region homologous to the highly polymorphic
threonine-glycine repeat of D. melanogaster in multiple strains of D.
willistoni, as well as in other members of willistoni group, and found an
unusual amount of conservation in this region. However, the next
nonconserved region downstream in the sequence is quite variable and
polymorphic for the number of repeated glycines. The glycine codon usage is
significantly different in this glycine repeat as compared to other parts
of the gene. We were able to plot the directionality of change in the
glycine repeat region onto a phylogeny and find that the addition of
glycines is the general trend with the diversification of the willistoni
group.
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Crystallization of rat cellular retinol binding protein II. Preliminary X-ray data obtained from the apoprotein expressed in Escherichia coli 总被引:1,自引:0,他引:1
J C Sacchettini D Stockhausen E Li L J Banaszak J I Gordon 《The Journal of biological chemistry》1987,262(32):15756-15758
Rat cellular retinol-binding protein II (CRBP II) is a member of a family of cytoplasmic proteins which bind hydrophobic ligands. CRBP II is thought to participate in the intestinal absorption and intracellular metabolism of retinoids. We have previously described the crystallization of a homologous rat intestinal fatty acid-binding protein (I-FABP) isolated from Escherichia coli containing a suitably constructed prokaryotic expression vector (Sacchettini, J. C., Meininger, T. A., Lowe, J. B., Gordon, J. I., and Banaszak, L. J., J. Biol. Chem. 262, 5428-5430). We have now efficiently expressed rat CRBP II in E. coli. The E. coli-derived protein, which does not contain any bound retinoid, has been purified and crystals grown from solutions of polyethylene glycol 4000. Crystals of apo-CRBP II are triclinic, space group P1, a = 36.8 A, b = 64.0 A, c = 30.4 A; alpha = 92.8 degrees, beta = 113.5 degrees, gamma = 90.1 degrees. Each unit cell contains two molecules of the 134-residue apoprotein. X-ray diffraction data suggest that the unit cell parameters of crystalline apo-CRBP II resemble those of I-FABP. Comparison of the tertiary structures of E. coli-derived rat I-FABP and CRBP II should provide insights about how these proteins evolved to bind different hydrophobic ligands. 相似文献