What's the difference between ague and agued?

Ague


Definition:

  • (n.) An acute fever.
  • (n.) An intermittent fever, attended by alternate cold and hot fits.
  • (n.) The cold fit or rigor of the intermittent fever; as, fever and ague.
  • (n.) A chill, or state of shaking, as with cold.
  • (v. t.) To strike with an ague, or with a cold fit.

Example Sentences:

  • (1) Aspartylglycosaminuria (AGU) is a hereditary metabolic disorder characterized by slowly progressive mental deterioration from infancy, urinary excretion of large amounts of aspartylglycosamine, and decreased activity of the lysosomal enzyme aspartylglcosamine amido hydrolase in various body tissues and fluids.
  • (2) Correlated morphological and biochemical studies thus definitely establish that AGU is a generalized storage disorder.
  • (3) Aspartylglucosaminuria (AGU) is a lysosomal storage disease due to mutations in the aspartylglucosaminidase (AGA) gene.
  • (4) The polymerase chain reaction was used to amplify the glycosylasparaginase protein coding sequence from the three AGU patients in order to compare them to the normal sequence from a full-length human placenta cDNA clone HPAsn.6 (Fisher, K.J., Tollersrud, O.K., and Aronson, N.N., Jr. (1990) FEBS Lett.
  • (5) The addition of Ser AGC AGU tRNA to an E. coli cell-free protein synthesizing system which contains the endogenous tRNA levels results in up to 100% of the ribosomes translating the MS2 coat gene shifting into the -1 reading frame.
  • (6) Thus, the high prevalence of AGU in the Finnish population is the consequence of a founder effect of one ancient mutation.
  • (7) When the 3' overlapping codon is AGA or AGG, there is no ribosome frameshifting; when it is AGU (read by the same serine tRNA) there is frameshifting, although less efficiently than in the case of AGC.
  • (8) The AGU would not respond directly to questions about the climate science town hall.
  • (9) One neutral and two acidic glycoasparagines were isolated from the urine of patients with aspartylglycosylaminuria (AGU).
  • (10) The truncated AGU protein was neither catalytically active nor processed into mature alpha and beta subunits.
  • (11) AGU patients had significantly reduced serum zinc concentrations.
  • (12) We conclude that the increased serum free dolichol in AGU reflects disturbed lysosomal function and that the decreased free and esterified dolichols in NCLs speak against their presumed primary lysosomal nature.
  • (13) In aspartylglycosaminuria (AGU), a lysosomal storage disorder of glycoprotein degradation, there are some abnormalities in collagen and proteoglycan metabolism.
  • (14) 80%) than those linked to a guanosine nucleoside through the same type of bond (AGU, AGG, AGC, ca.
  • (15) The major known glycosylasparaginase gene defect G488----C, which causes the lysosomal storage disease aspartylglycosaminuria (AGU) in Finland, is located in exon 4.
  • (16) This bacterium contains two isoacceptor threonine tRNAs having anticodon sequences AGU and UGU, both with unmodified first nucleotides.
  • (17) We have earlier reported a single missense mutation (Cys163----Ser) to be responsible for 98% of the AGU alleles in the isolated Finnish population, which contains about 90% of the reported AGU patients.
  • (18) (2) There are two tRNAThr species having anticodons UGU and AGU; the first positions of these anticodons are unmodified.
  • (19) The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
  • (20) Two base changes were found to be common to all three Finnish AGU patients, a G482----A transition that results in an Arg161----Gln substitution and a G488----C transversion that causes Cys163----Ser.

Agued


Definition:

  • (imp. & p. p.) of Ague

Example Sentences:

  • (1) Aspartylglycosaminuria (AGU) is a hereditary metabolic disorder characterized by slowly progressive mental deterioration from infancy, urinary excretion of large amounts of aspartylglycosamine, and decreased activity of the lysosomal enzyme aspartylglcosamine amido hydrolase in various body tissues and fluids.
  • (2) Correlated morphological and biochemical studies thus definitely establish that AGU is a generalized storage disorder.
  • (3) Aspartylglucosaminuria (AGU) is a lysosomal storage disease due to mutations in the aspartylglucosaminidase (AGA) gene.
  • (4) The polymerase chain reaction was used to amplify the glycosylasparaginase protein coding sequence from the three AGU patients in order to compare them to the normal sequence from a full-length human placenta cDNA clone HPAsn.6 (Fisher, K.J., Tollersrud, O.K., and Aronson, N.N., Jr. (1990) FEBS Lett.
  • (5) The addition of Ser AGC AGU tRNA to an E. coli cell-free protein synthesizing system which contains the endogenous tRNA levels results in up to 100% of the ribosomes translating the MS2 coat gene shifting into the -1 reading frame.
  • (6) Thus, the high prevalence of AGU in the Finnish population is the consequence of a founder effect of one ancient mutation.
  • (7) When the 3' overlapping codon is AGA or AGG, there is no ribosome frameshifting; when it is AGU (read by the same serine tRNA) there is frameshifting, although less efficiently than in the case of AGC.
  • (8) The AGU would not respond directly to questions about the climate science town hall.
  • (9) One neutral and two acidic glycoasparagines were isolated from the urine of patients with aspartylglycosylaminuria (AGU).
  • (10) The truncated AGU protein was neither catalytically active nor processed into mature alpha and beta subunits.
  • (11) AGU patients had significantly reduced serum zinc concentrations.
  • (12) We conclude that the increased serum free dolichol in AGU reflects disturbed lysosomal function and that the decreased free and esterified dolichols in NCLs speak against their presumed primary lysosomal nature.
  • (13) In aspartylglycosaminuria (AGU), a lysosomal storage disorder of glycoprotein degradation, there are some abnormalities in collagen and proteoglycan metabolism.
  • (14) 80%) than those linked to a guanosine nucleoside through the same type of bond (AGU, AGG, AGC, ca.
  • (15) The major known glycosylasparaginase gene defect G488----C, which causes the lysosomal storage disease aspartylglycosaminuria (AGU) in Finland, is located in exon 4.
  • (16) This bacterium contains two isoacceptor threonine tRNAs having anticodon sequences AGU and UGU, both with unmodified first nucleotides.
  • (17) We have earlier reported a single missense mutation (Cys163----Ser) to be responsible for 98% of the AGU alleles in the isolated Finnish population, which contains about 90% of the reported AGU patients.
  • (18) (2) There are two tRNAThr species having anticodons UGU and AGU; the first positions of these anticodons are unmodified.
  • (19) The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
  • (20) Two base changes were found to be common to all three Finnish AGU patients, a G482----A transition that results in an Arg161----Gln substitution and a G488----C transversion that causes Cys163----Ser.

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