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981.
Barbara Schimmer Saskia Luttikholt Jeannine LA Hautvast Elisabeth AM Graat Piet Vellema Yvonne THP van Duynhoven 《BMC veterinary research》2011,7(1):1-14
Background
Highly pathogenic avian influenza (HPAI) viruses have had devastating effects on poultry industries worldwide, and there is concern about the potential for HPAI outbreaks in the poultry industry in Great Britain (GB). Critical to the potential for HPAI to spread between poultry premises are the connections made between farms by movements related to human activity. Movement records of catching teams and slaughterhouse vehicles were obtained from a large catching company, and these data were used in a simulation model of HPAI spread between farms serviced by the catching company, and surrounding (geographic) areas. The spread of HPAI through real-time movements was modelled, with the addition of spread via company personnel and local transmission.Results
The model predicted that although large outbreaks are rare, they may occur, with long distances between infected premises. Final outbreak size was most sensitive to the probability of spread via slaughterhouse-linked movements whereas the probability of onward spread beyond an index premises was most sensitive to the frequency of company personnel movements.Conclusions
Results obtained from this study show that, whilst there is the possibility that HPAI virus will jump from one cluster of farms to another, movements made by catching teams connected fewer poultry premises in an outbreak situation than slaughterhouses and company personnel. The potential connection of a large number of infected farms, however, highlights the importance of retaining up-to-date data on poultry premises so that control measures can be effectively prioritised in an outbreak situation. 相似文献982.
Gille A Wenzel-Seifert K Doughty MB Seifert R 《The Journal of biological chemistry》2003,278(10):7822-7828
Xanthine nucleotide-selective small GTP-binding proteins with an Asp/Asn mutation are valuable for the analysis of individual GTP-binding proteins in complex systems. Similar applications can be devised for heterotrimeric G-proteins. However, Asp/Asn mutants of Galpha(o), Galpha(11), and Galpha(16) were inactive. An additional Gln/Leu mutation in the catalytic site, reducing GTPase activity and increasing GDP affinity, was required to generate xanthine nucleotide-selective unspecified G-protein alpha-subunit (Galpha). Our study aim was to generate xanthine nucleotide-selective mutants of Galpha(s), the stimulatory G-protein of adenylyl cyclase. The short splice variant of Galpha(s) (Galpha(sS)) possesses higher GDP affinity than the long splice variant (Galpha(sL)). Nucleoside 5'-[gamma-thio]triphosphates (NTPgammaSs) and nucleoside 5'-[beta,gamma-imido]triphosphates effectively activated a Galpha(sS) mutant with a D280N exchange (Galpha(sS)-N280), whereas nucleotides activated a Galpha(sL) mutant with a D295N exchange (Galpha(sL)-N295) only weakly. The Gln/Leu mutation enhanced Galpha(sL)-N295 activity. NTPgammaSs activated Galpha(sS)-N280 and a Galpha(sL) mutant with a Q227L and D295N exchange (Galpha(sL)-L227/N295) with similar potencies, whereas xanthosine 5'-triphosphate and xanthosine 5'-[beta,gamma-imido]triphosphate were more potent than GTP and guanosine 5'-[beta,gamma-imido]triphosphate, respectively. Galpha(sS)-N280 interacted with the beta(2)-adrenoreceptor and exhibited high-affinity XTPase activity. Collectively, (i) Galpha(sS)-N280 is the first functional xanthine nucleotide-selective Galpha with the Asp/Asn mutation alone; (ii) sufficiently high GDP affinity is crucial for Galpha Asp/Asn mutant function; (iii) with nucleoside 5'-triphosphates and nucleoside 5'-[beta,gamma-imido]triphosphates, Galpha(s)-N280 and Galpha(sL)-L227/N295 exhibit xanthine nucleotide selectivity, whereas NTPgammaSs sterically perturb the catalytic site of Galpha and annihilate xanthine selectivity. 相似文献
983.
A. terreus isolates isolated from some bakery products, corn and rice were found to be able to produce territrems. 90% of theA. terreus isolated from bakery products were able to produce territrem A, with a mean of 0.09 ppm, while 80% ofA. terreus isolates produce territrem B with a mean of 0.24 ppm. On the other hand 31.8% of the isolates ofA. terreus from corn were able to produce territrem A with a mean of 0.44 ppm. ConcerningA. terreus isolates from rice, 66.7% were found to produce territrem A, with a mean of 5.28 ppm, and 77.8% of the isolates produced
territrem B with a mean of 1.79 ppm. 相似文献
984.
985.
The effects of the microenvironment and the nature of the limiting nutrient on culture viability and overall MAb productivity were explored using a hybridoma cell line which characteristically produces MAb in the stationary phase. A direct comparison was made of the changes in the metabolic profiles of suspension and PEG-alginate immobilized (0.8 mm beads) batch cultures upon entry into the stationary phase. The shifts in glucose, glutamine, and amino acid metabolism upon entry into the stationary phase were similar for both microenvironments. While the utilization of most nutrients in the stationary phase decreased to below 20% of that in the growth phase, antibody production was not dramatically affected. The immobilized culture did exhibit a 1.5-fold increase in the specific antibody rate over the suspension culture in both the growth and stationary phases. The role of limiting nutrient on MAb production and cell viability was assessed by artificially depleting a specific nutrient to 1% of its control concentration. An exponentially growing population of HB121 cells exposed to these various depletions responded with dramatically different viability profiles and MAb production kinetics. All depletions resulted in growth-arrested cultures and nongrowth-associated MAb production. Depletions in energy sources (glucose, glutamine) or essential amino acids (isoleucine) resulted in either poor viability or low antibody productivity. A phosphate or serum depletion maintained antibody production over at least a six day period with each resulting in a 3-fold higher antibody production rate than in growing batch cultures. These results were translated to a high-density perfusion culture of immobilized cells in the growth-arrested state with continued MAb expression for 20 days at a specific rate equal to that observed in the phosphate- and serum-depleted batch cultures. 相似文献
986.
987.
Michelle I Portugal Adriane R Todeschini Cristiana S de Lima Carlos AM Silva Ronaldo Mohana-Borges Tom HM Ottenhoff Lucia Mendonça-Previato Jose O Previato Maria CV Pessolani 《BMC microbiology》2008,8(1):75
Background
The histone-like Hlp protein is emerging as a key component in mycobacterial pathogenesis, being involved in the initial events of host colonization by interacting with laminin and glycosaminoglycans (GAGs). In the present study, nuclear magnetic resonance (NMR) was used to map the binding site(s) of Hlp to heparan sulfate and identify the nature of the amino acid residues directly involved in this interaction. 相似文献988.
Most of the detailed mechanisms that have been established for the molecular biological processes that mediate recombination, repair and replication of DNA have come from studies of the Escherichia coli paradigm. The human specific pathogens, Neisseria gonorrhoeae and N. meningitidis, are Gram-negative bacteria that have some molecular processes that are similar to E. coli and others that appear to be divergent. We propose that the pathogenic Neisseriae have evolved a specialized collection of molecular mechanisms to adapt to life limited to human hosts. In this MicroReview, we explore what is known about the basic processes of DNA repair, DNA recombination (genetic exchange and pilin variation) and DNA replication in these human specific pathogens. 相似文献
989.
Wuelton M Monteiro Fernando FA Val André M Siqueira Gabriel P Franca Vanderson S Sampaio Gisely C Melo Anne CG Almeida Marcelo AM Brito Henry M Peixoto Douglas Fuller Quique Bassat Gustavo AS Romero Oliveira Maria Regina F Lacerda Marcus Vinícius G 《Memórias do Instituto Oswaldo Cruz》2014,109(5):553-568
990.