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The forest EF per capita kept a steady status, while the forest production footprint (FPF) and forest export footprint (FEF) decreased.
      
Effect of Export-Specific Cytoplasmic Chaperone, Protein SecB, on Secretion of Escherichia coli Alkaline Phosphatase
      
Secretion increases in the presence of this chaperone at 30°C, which is the most favorable for the interaction of SecB with the export-initiation domain found previously in the N-terminal region of the mature enzyme.
      
This interaction most likely occurs in the region of the export domain, which is located close to the signal peptide and in complex with a translocational ATPase-protein SecA.
      
Study of Interaction of Export Initiation Domain of Escherichia coli Mature Alkaline Phosphatase with Membrane Phospholipids dur
      
The gene encodes an export signal peptide characteristic for periplasmic redox proteins.
      
Karyopherins bind to their cargoes via recognition of nuclear localization signal (NLS) for nuclear import or nuclear export signal (NES) for export to form a transport complex.
      
GAPDS was shown to lack the sequence similar to the atypical nuclear export signal motif (NES) of the somatic isoenzyme GAPD.
      
The use of the system clipboard allows one to export the results of analysis into Word and Excel, and to call external programs via the Internet.
      
Export-specific chaperone SecB and translocational ATPase SecA catalyze the cytoplasmic steps of Sec-dependent secretion in Escherichia coli.
      
The cytoplasmic step of posttranslational secretion in Escherichia coli is catalyzed by export-specific chaperone SecB and translocational ATPase SecA.
      
In contrast to Nrf2, ProTα escaped Keap1-dependent ubiquitination, proteasomal degradation, and export from the nucleus.
      
Export of metabolites by the proteins of the DMT and RhtB families and its possible role in intercellular communication
      
These proteins are involved in the export of amino acids, purines, and other metabolites from the cell.
      
The functional diversities of associated and free-living bacterial communities were additionally compared using BIOLOG GN microplates to reveal the possible export of Microcystis-attached bacteria into ambient water.
      
Export of the subunits is mediated by the periplasmic chaperone Caf1M.
      
These genes are orthologous to the sbrgene of Drosophilaand control mRNA export from the nucleus to the cytoplasm.
      
The sbrgene of Drosophila melanogasterbelongs to the NXF(nuclear export factor) family responsible for the mRNA transport from nucleus to cytoplasm.
      
The presence of DK2 in the culture broth of mutant bacteria, connected to its export in the environment, was established.
      
During salt adaptation, cyanobacterial cells accumulate osmoprotectors, export excessive Na+ with the help of Na+/H+ antiporters, and actively absorb K+ with the help of K+-transporting systems.
      
 

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