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   1 host PPP, augmenting production of NADPH and ribose 5-phosphate.                                     
     2 )G degrees for D-ribose and two species of D-ribose 5-phosphate.                                     
     3 ees for two protonation states of 2'-deoxy-D-ribose 5-phosphate.                                     
     4            The first intermediate forms with ribose 5-phosphate.                                     
     5 ependent hydrolysis of ADP-ribose to AMP and ribose 5-phosphate.                                     
     6 ze the negative charge of the leaving group, ribose 5-phosphate.                                     
     7 d more information as compared to those from ribose 5-phosphate.                                     
     8 NADPH and the essential nucleotide component ribose-5-phosphate.                                     
     9 he nonoxidative pentose phosphate pathway to ribose-5-phosphate.                                     
    10 thesis from 4,5-dimethylphenylenediamine and ribose-5-phosphate.                                     
    11  to the equation: ADP-ribose + H2O --> AMP + ribose-5-phosphate.                                     
    12 ssed in isolation, cleaves ADPR into AMP and ribose-5-phosphate.                                     
    13 e and in the absence of the reaction product ribose 5'-phosphate.                                    
    14 zyme hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.                                    
    15 ed OAADPr to the products AMP and acetylated ribose 5'-phosphate.                                    
    16 his shows that Delta(f)G degrees (2'-deoxy-D-ribose 5-phosphate(2)(-)) - Delta(f)G degrees (D-ribose 
    17 se 5-phosphate(2)(-)) - Delta(f)G degrees (D-ribose 5-phosphate(2)(-)) = 147.86 kJ mol(-1) at 298.15 
    18 at SAICAR (succinylaminoimidazolecarboxamide ribose-5'-phosphate, an intermediate of the de novo puri
  
  
  
  
    23 , identified binding sites for the substrate ribose 5-phosphate and the activator alpha-D-glucose 1,6
  
  
    26 hat interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribo
    27 haride analogues, D-arabinose 5-phosphate, D-ribose 5-phosphate, and 2-deoxy-D-ribose 5-phosphate, we
  
  
    30 reased the conversion of triosephosphates to ribose-5-phosphate, and strongly inhibited the developme
  
    32 lyze the conversion of ribose-1-phosphate to ribose-5-phosphate, enabling the Pi mop to remove large 
    33 edoheptulose 7-phosphate, failure to recycle ribose 5-phosphate for the oxidative PPP, depleted NADPH
  
    35 ltransferases, and catalyzes the transfer of ribose 5-phosphate from alpha-d-5-phosphoribosyl-1-pyrop
    36 bose, glucose, glycerylaldehyde-3-phosphate, ribose-5-phosphate, glucose-6-phosphate, and mannose-6-p
    37 id, form glycosidic linkages with ribose and ribose-5-phosphate in water to produce nucleosides and n
    38  The crystal structure of the complex with D-ribose-5-phosphate indicated that the phosphosugar is bo
  
    40 y enriched [(14)C]orotic acid show that when ribose 5'-phosphate is deleted from substrate orotidine 
    41 s on CAIR and N5-CAIR analogues in which the ribose 5'-phosphate is replaced with a methyl group.    
    42 ventions suggested by this algorithm, genes (ribose 5-phosphate isomerase and ribulose 5-phosphate 3-
    43 t homologs of triose phosphate isomerase and ribose 5-phosphate isomerase B, were necessary, as previ
    44 reas other targets, such as glyoxalase I and ribose 5-phosphate isomerase, detoxify byproducts from g
  
  
    47 inder of the cavity binds the nicotinate and ribose-5'-phosphate moieties, which are nestled within t
  
    49 dent apoptosis through controlling NADPH and ribose 5-phosphate production via the pentose phosphate 
    50 2dR5P), as an alternate substrate, but not D-ribose 5-phosphate (R5P) nor the four carbon analogue D-
    51 n complex with phosphoenolpyruvate (PEP) and ribose 5-phosphate (R5P), and with a bisubstrate inhibit
    52 ite of the PLP synthase subunit, Pdx1, where ribose-5-phosphate (R5P), glyceraldehyde-3-phosphate (G3
  
    54 uperfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribo
    55 of succinyl-5-aminoimidazole-4-carboxamide-1-ribose-5'-phosphate (SAICAR), a metabolite abundant in p
  
    57 ynthase, which catalyzes the attachment of D-ribose-5-phosphate to prealnumycin by formation of the C
    58 is derived from D-fructose 6-phosphate and D-ribose 5-phosphate via a transaldol reaction catalyzed b
    59 -phosphate) and nucleotide metabolism (via D-ribose 5-phosphate) was associated with perturbations in
    60 ribose 5-[(18)O(3)]phosphate and [U-(13)C(5)]ribose 5-phosphate were analyzed by mass spectrometry.  
    61 osphate, D-ribose 5-phosphate, and 2-deoxy-D-ribose 5-phosphate, were separately condensed with (Z)- 
    62 y of 6-PG for oxidative decarboxylation to D-ribose-5-phosphate, which is essential for the utilizati
  
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