Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 218,250,877 papers from all fields of science
Search
Sign In
Create Free Account
amadoriase
Known as:
FAOD enzyme
, amadoriase II
, fructosyl amino acid oxidase
National Institutes of Health
Create Alert
Alert
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2015
Highly Cited
2015
Formation of active inclusion bodies induced by hydrophobic self-assembling peptide GFIL8
Xu Wang
,
Bihong Zhou
,
Weike Hu
,
Qing Zhao
,
Zhanglin Lin
Microbial Cell Factories
2015
Corpus ID: 16336457
BackgroundIn the last few decades, several groups have observed that proteins expressed as inclusion bodies (IBs) in bacteria…
Expand
2011
2011
Streamlined protein expression and purification using cleavable self-aggregating tags
L. Xing
,
Wei Wu
,
Bihong Zhou
,
Zhanglin Lin
Microbial Cell Factories
2011
Corpus ID: 2099698
BackgroundRecombinant protein expression and purification remains a fundamental issue for biotechnology. Recently we found that…
Expand
Highly Cited
2008
Highly Cited
2008
The Role of the Amadori Product in the Complications of Diabetes
V. Monnier
,
D. Sell
,
Z. Dai
,
I. Nemet
,
F. Collard
,
Jianye Zhang
Annals of the New York Academy of Sciences
2008
Corpus ID: 1628741
Strong evidence has emerged in recent years in support of an association between advanced glycation and the complications of…
Expand
2007
2007
Studies on the effect of Amadoriase from Aspergillus fumigatus on peptide and protein glycation in vitro.
E. Capuano
,
F. Fedele
,
+7 authors
V. Fogliano
Journal of Agricultural and Food Chemistry
2007
Corpus ID: 32807482
Amadoriase I is a fructosyl amine oxidase from Aspergillus fumigatus that catalyzes the oxidation of Amadori products (APs…
Expand
2001
2001
Kinetic studies, mechanism, and substrate specificity of amadoriase I from Aspergillus sp.
X. Wu
,
B. Palfey
,
V. Mossine
,
V. Monnier
Biochemistry
2001
Corpus ID: 22085636
Amadoriase is a flavoenzyme that catalyzes the oxidative deglycation of Amadori products (fructosyl amino acids or aliphatic…
Expand
2000
2000
Cloning of amadoriase I isoenzyme from Aspergillus sp.: evidence of FAD covalently linked to Cys342.
X. Wu
,
M. Takahashi
,
S. Chen
,
V. Monnier
Biochemistry
2000
Corpus ID: 25854257
Amadoriases are a novel class of FAD enzymes which catalyze the oxidative deglycation of glycated amino acids to yield…
Expand
1999
1999
Production of fungal fructosyl amino acid oxidase useful for diabetic diagnosis in the peroxisome of Candida boidinii
Y. Sakai
,
Hiroyuki Yoshida
,
+4 authors
N. Kato
FEBS Letters
1999
Corpus ID: 27475516
Highly Cited
1997
Highly Cited
1997
Isolation, Purification, and Characterization of Amadoriase Isoenzymes (Fructosyl Amine-oxygen Oxidoreductase EC 1.5.3) from Aspergillus sp.*
M. Takahashi
,
M. Pischetsrieder
,
V. Monnier
Journal of Biological Chemistry
1997
Corpus ID: 45596886
Four “amadoriase” enzyme fractions, which oxidatively degrade glycated low molecular weight amines and amino acids under…
Expand
Highly Cited
1997
Highly Cited
1997
Molecular Cloning and Expression of Amadoriase Isoenzyme (Fructosyl Amine:Oxygen Oxidoreductase, EC 1.5.3) from Aspergillus fumigatus *
M. Takahashi
,
M. Pischetsrieder
,
V. Monnier
Journal of Biological Chemistry
1997
Corpus ID: 34085012
Amadoriase is an enzyme catalyzing the oxidative deglycation of Amadori products to yield corresponding amino acids, glucosone…
Expand
Highly Cited
1996
Highly Cited
1996
Primary structures of fungal fructosyl amino acid oxidases and their application to the measurement of glycated proteins.
N. Yoshida
,
Y. Sakai
,
+4 authors
N. Kato
European Journal of Biochemistry
1996
Corpus ID: 25427492
Fructosyl amino acid oxidase (FAOD), which is active toward model compounds of the glycated proteins in blood, N epsilon…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE