n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime and deoxyglucose

n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime has been researched along with deoxyglucose in 2 studies

Compound Research Comparison

Studies (n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime)	Trials (n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime)	Recent Studies (post-2010) (n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime)	Studies (deoxyglucose)	Trials (deoxyglucose)	Recent Studies (post-2010) (deoxyglucose)
88	0	36	11,426	171	1,375

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Lee, W; Park, SY; Ryu, J	1
Davies, GJ; Gloster, TM; He, Y; Macauley, MS; Stubbs, KA; Vocadlo, DJ	1

Other Studies

2 other study(ies) available for n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime and deoxyglucose

Article	Year
O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes. Experimental & molecular medicine, 2005, Jun-30, Volume: 37, Issue:3 Topics: Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Deoxyglucose; Glucose Transporter Type 5; Glycosylation; Immunoprecipitation; Insulin Receptor Substrate Proteins; Insulin Resistance; Male; Monosaccharide Transport Proteins; Oximes; Phenylcarbamates; Phosphoproteins; Phosphorylation; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-akt; Rats; Rats, Sprague-Dawley; Subcellular Fractions	2005
Inhibition of O-GlcNAcase using a potent and cell-permeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes. Chemistry & biology, 2010, Sep-24, Volume: 17, Issue:9 Topics: 3T3-L1 Cells; Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Deoxyglucose; Enzyme Inhibitors; Humans; Indolizines; Insulin; Insulin Receptor Substrate Proteins; Insulin Resistance; Mice; Oximes; Phenylcarbamates; Phosphorylation; Proto-Oncogene Proteins c-akt	2010

Article

Year

O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes.

Experimental & molecular medicine, 2005, Jun-30, Volume: 37, Issue:3

Topics: Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Deoxyglucose; Glucose Transporter Type 5; Glycosylation; Immunoprecipitation; Insulin Receptor Substrate Proteins; Insulin Resistance; Male; Monosaccharide Transport Proteins; Oximes; Phenylcarbamates; Phosphoproteins; Phosphorylation; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-akt; Rats; Rats, Sprague-Dawley; Subcellular Fractions

2005

Inhibition of O-GlcNAcase using a potent and cell-permeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes.

Chemistry & biology, 2010, Sep-24, Volume: 17, Issue:9

Topics: 3T3-L1 Cells; Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Deoxyglucose; Enzyme Inhibitors; Humans; Indolizines; Insulin; Insulin Receptor Substrate Proteins; Insulin Resistance; Mice; Oximes; Phenylcarbamates; Phosphorylation; Proto-Oncogene Proteins c-akt

2010