ライフサイエンスコーパス: glucosaminidase

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1 , whereas R3 is located at the N-terminus of glucosaminidase.

2 er subsequent treatment with N-acetyl-beta-D-glucosaminidase.

3 anced by the chemical inhibition of N-acetyl-glucosaminidase.

4 N-acetyl glucosaminidase, a specific tubular injury marker, was s

5 lationship between urinary N-acetyl-beta-(D)-glucosaminidase activity (NAG) and kidney injury molecul

6 glitazone normalized urinary N-acetyl-beta-D-glucosaminidase activity, a marker for renal proximal tu

7 plasma creatinine, urinary N-acetyl-beta-(d)-glucosaminidase activity, kidney injury molecule 1, and

8 detect the preformed enzymes N-acetyl-beta-D-glucosaminidase, alpha-D-galactosidase, beta-D-galactosi

9 Antigens (glucosaminidase, an ABC transporter lipoprotein, a conse

10 ther urinary markers such as N-acetyl-beta-D-glucosaminidase and beta2-microglobulin.

11 preceding the appearance of N-acetyl-beta-D-glucosaminidase and beta2-microglobulin.

12 periplasmic (HexA and HexB) N-acetyl-beta-D-glucosaminidases and one cytoplasmic (HexC) N-acetyl-bet

13 e to N-acetlyneuraminidase and beta-N-acetyl glucosaminidase, and minimally sensitive to beta-N-acety

14 nidase and its isoenzyme A, N-acetyl-alpha-D-glucosaminidase, beta-galactosidase, beta-glucuronidase,

15 reviously in B. subtilis, differing from the glucosaminidase function that is apparent in B. cereus/B

16 Endo-beta-N-glucosaminidase H (EndoH) treatment of gp120-Fc under co

17 ween the urinary activity of N-acetyl-beta-D-glucosaminidase (NAG) and cardiovascular risk has been a

18 im-1 to BUN, SCr and urinary N-acetyl-beta-D-glucosaminidase (NAG) as predictors of kidney tubular da

19 was measured by immunoblot, N-acetyl-beta-d-glucosaminidase (NAG) by enzyme measurement, alpha1-micr

20 idney injury molecule-1 (KIM-1) and N-acetyl glucosaminidase (NAG) corresponding to the progression a

21 vely associated with urinary N-acetyl beta-d-glucosaminidase (NAG) levels but not microalbumin levels

22 ular injury (increased urine N-acetyl-beta-D-glucosaminidase (NAG) levels) after its use was sought i

23 lanine aminopeptidase (AAP), N-acetyl-beta-d-glucosaminidase (NAG), and creatinine.

24 activity of beta-glucosidase (BG), N-acetyl-glucosaminidase (NAG), and peroxidase in two soils that

25 he p.Ile403Thr variant in the alpha-N-acetyl-glucosaminidase (NAGLU) gene segregates with the disease

26 (OGT) and O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase (OGA), mediate addition and removal, res

27 lglucosamine-1-phosphodiester alpha-N-acetyl glucosaminidase), presumably due to a block in transit o

28 A major lytic enzymatic activity was a glucosaminidase, probably YaaH, that cleaved between N-a

29 an was not detected, and it is proposed that glucosaminidase products were previously misidentified a

30 pH had little effect on N-acetyl-beta-glucosaminidase release from primary granules.

31 d 775 to generate a pro-peptide, amidase and glucosaminidase, respectively.

32 ons of beta2-microglobulin and N-acetyl-beta-glucosaminidase rose significantly (P=0.03 for both incr

33 e repeat domains direct pro-Atl, amidase and glucosaminidase to a specific receptor at the equatorial

34 mined the mechanism that directs amidase and glucosaminidase to the cell division site on the staphyl

35 of beta-D-galactosidases and N-acetyl-beta-D-glucosaminidases to obtain core glycopeptides.

36 Urinary albumin and N-acetyl-beta-D-glucosaminidase was significantly increased on day 8 com

37 s and one cytoplasmic (HexC) N-acetyl-beta-D-glucosaminidase were demonstrated.

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