ライフサイエンスコーパス: glucosaminidase

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

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

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

4 ons in the NAGLU gene encoding alfa-N-acetyl-glucosaminidase.

5 lidases, beta-d-glucuronidases, and N-acetyl-glucosaminidases.

6 gulated antigens SAOCOL0486 (a lipoprotein), glucosaminidase (a domain of SACOL1062), and SACOL0688 (

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

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

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

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

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

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

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

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

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

16 -associated lipocalin), NAG (N-acetyl-beta-d-glucosaminidase), and KIM-1 (kidney injury molecule 1),

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

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

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

20 l antibodies against the S. aureus autolysin glucosaminidase (Gmd) domain, and subsequent testing wit

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

22 injury biomarker substudy (NAG [N-acetyl-b-D-glucosaminidase], KIM-1 [kidney injury molecule-1], and

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

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

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

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

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

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

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

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

31 ne aminopeptidase (AAP), and N-acetyl-beta-d-glucosaminidase (NAG).

32 eys to report AKI-associated N-acetyl-beta-D-glucosaminidase (NAG).

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

34 n the gene that encodes the protein N-acetyl-glucosaminidase (NAGLU).

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

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

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

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

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

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

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

42 lactate dehydrogenase (LDH), N -acetyl-beta-glucosaminidase, tissue inhibitor of metalloproteinases-

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

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

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

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

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