-
1
-
-
0343373375
-
1H-nuclear magnetic resonance spectroscopy as a tool on the structural analysis of carbohydrates related to glycoproteins
-
1H-nuclear magnetic resonance spectroscopy as a tool on the structural analysis of carbohydrates related to glycoproteins. Adv. Carbohydr. Chem. Biochem. 1983, 41, 209-374.
-
(1983)
Adv. Carbohydr. Chem. Biochem.
, vol.41
, pp. 209-374
-
-
Vliegenthart, J.F.G.1
Dornald, L.2
Halveek, H.V.3
-
2
-
-
75749134145
-
N-glycan structures: Recognition and processing in the ER
-
Aebi, M.; Bernasconi, R.; Clerc, S.; Molinari, M. N-glycan structures: Recognition and processing in the ER. Trends Biochem. Sci. 2010, 35, 74-82.
-
(2010)
Trends Biochem. Sci.
, vol.35
, pp. 74-82
-
-
Aebi, M.1
Bernasconi, R.2
Clerc, S.3
Molinari, M.4
-
3
-
-
84862851683
-
Molecular and structural basis for N-glycan-dependent determination of glycoprotein fates in cells
-
Kamiya, Y.; Satoh, T.; Kato, K. Molecular and structural basis for N-glycan-dependent determination of glycoprotein fates in cells. Biochim. Biophys. Acta 2012, 1820, 1327-1337.
-
(2012)
Biochim. Biophys. Acta
, vol.1820
, pp. 1327-1337
-
-
Kamiya, Y.1
Satoh, T.2
Kato, K.3
-
4
-
-
35048842895
-
Structural views of glycoprotein-fate determination in cells
-
Kato, K.; Kamiya, Y. Structural views of glycoprotein-fate determination in cells. Glycobiology 2007, 17, 1031-1044.
-
(2007)
Glycobiology
, vol.17
, pp. 1031-1044
-
-
Kato, K.1
Kamiya, Y.2
-
5
-
-
70349855203
-
Glycoprotein folding, quality control and ER-associated degradation
-
Lederkremer, G.Z. Glycoprotein folding, quality control and ER-associated degradation. Curr. Opin. Struct. Biol. 2009, 19, 515-523.
-
(2009)
Curr. Opin. Struct. Biol.
, vol.19
, pp. 515-523
-
-
Lederkremer, G.Z.1
-
6
-
-
22544467505
-
More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle
-
Deprez, P.; Gautschi, M.; Helenius, A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol. Cell 2005, 19, 183-195.
-
(2005)
Mol. Cell
, vol.19
, pp. 183-195
-
-
Deprez, P.1
Gautschi, M.2
Helenius, A.3
-
7
-
-
0019332339
-
Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
-
Grinna, L.S.; Robbins, P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 1980, 255, 2255-2258.
-
(1980)
J. Biol. Chem.
, vol.255
, pp. 2255-2258
-
-
Grinna, L.S.1
Robbins, P.W.2
-
8
-
-
84877713668
-
Specificity of Processing α-glucosidase I is guided by the substrate conformation: Crystallographic and in silico studies
-
Barker, M.K.; Rose, D.R. Specificity of Processing α-glucosidase I is guided by the substrate conformation: Crystallographic and in silico studies. J. Biol. Chem. 2013, 288, 13563-13574.
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 13563-13574
-
-
Barker, M.K.1
Rose, D.R.2
-
9
-
-
0029078838
-
N-alkylated nitrogen-in-the-ring sugars: Conformational basis of inhibition of glycosidases and HIV-1 replication
-
Asano, N.; Kizu, H.; Oseki, K.; Tomioka, E.; Matsui, K.; Okamoto, M.; Baba, M. N-alkylated nitrogen-in-the-ring sugars: Conformational basis of inhibition of glycosidases and HIV-1 replication. J. Med. Chem. 1995, 38, 2349-2356.
-
(1995)
J. Med. Chem.
, vol.38
, pp. 2349-2356
-
-
Asano, N.1
Kizu, H.2
Oseki, K.3
Tomioka, E.4
Matsui, K.5
Okamoto, M.6
Baba, M.7
-
10
-
-
0032560488
-
α-glucosidase inhibitors as potential broad based anti-viral agents
-
Mehta, A.; Zitzmann, N.; Rudd, P.M.; Block, T.M.; Dwek, R.A. α-glucosidase inhibitors as potential broad based anti-viral agents. FEBS Lett. 1998, 430, 17-22.
-
(1998)
FEBS Lett.
, vol.430
, pp. 17-22
-
-
Mehta, A.1
Zitzmann, N.2
Rudd, P.M.3
Block, T.M.4
Dwek, R.A.5
-
11
-
-
33947303039
-
Glucosidase inhibitors as antiviral agents for hepatitis B and C
-
Durantel, D.; Alotte, C.; Zoulim, F. Glucosidase inhibitors as antiviral agents for hepatitis B and C. Curr. Opin. Investig. Drugs 2007, 8, 125-129.
-
(2007)
Curr. Opin. Investig. Drugs
, vol.8
, pp. 125-129
-
-
Durantel, D.1
Alotte, C.2
Zoulim, F.3
-
12
-
-
77952583769
-
UDP-GlC:Glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control
-
D'Alessio, C.; Caramelo, J.J.; Parodi, A.J. UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control. Semin. Cell Dev. Biol. 2010, 21, 491-499.
-
(2010)
Semin. Cell Dev. Biol.
, vol.21
, pp. 491-499
-
-
D'Alessio, C.1
Caramelo, J.J.2
Parodi, A.J.3
-
13
-
-
33845969527
-
Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans
-
Totani, K.; Ihara, Y.; Matsuo, I.; Ito, Y. Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans. J. Biol. Chem. 2006, 281, 31502-31508.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 31502-31508
-
-
Totani, K.1
Ihara, Y.2
Matsuo, I.3
Ito, Y.4
-
14
-
-
39049105287
-
Effects of macromolecular crowding on glycoprotein processing enzymes
-
Totani, K.; Ihara, Y.; Matsuo, I.; Ito, Y. Effects of macromolecular crowding on glycoprotein processing enzymes. J. Am. Chem. Soc. 2008, 130, 2101-2107.
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 2101-2107
-
-
Totani, K.1
Ihara, Y.2
Matsuo, I.3
Ito, Y.4
-
15
-
-
0035807024
-
Quaternary and domain structure of glycoprotein processing glucosidase II
-
Trombetta, E.S.; Fleming, K.G.; Helenius, A. Quaternary and domain structure of glycoprotein processing glucosidase II. Biochemistry 2001, 40, 10717-10722.
-
(2001)
Biochemistry
, vol.40
, pp. 10717-10722
-
-
Trombetta, E.S.1
Fleming, K.G.2
Helenius, A.3
-
16
-
-
70249110040
-
Sugar-binding activity of the MRH domain in the ER α-glucosidase II beta subunit is important for efficient glucose trimming
-
Hu, D.; Kamiya, Y.; Totani, K.; Kamiya, D.; Kawasaki, N.; Yamaguchi, D.; Matsuo, I.; Matsumoto, N.; Ito, Y.; Kato, K.; et al. Sugar-binding activity of the MRH domain in the ER α-glucosidase II beta subunit is important for efficient glucose trimming. Glycobiology 2009, 19, 1127-1135.
-
(2009)
Glycobiology
, vol.19
, pp. 1127-1135
-
-
Hu, D.1
Kamiya, Y.2
Totani, K.3
Kamiya, D.4
Kawasaki, N.5
Yamaguchi, D.6
Matsuo, I.7
Matsumoto, N.8
Ito, Y.9
Kato, K.10
-
17
-
-
84878756888
-
Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum
-
Olson, L.J.; Orsi, R.; Alculumbre, S.G.; Peterson, F.C.; Stigliano, I.D.; Parodi, A.J.; D'Alessio, C.; Dahms, N.M. Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum. J. Biol. Chem. 2013, 288, 16460-16475.
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 16460-16475
-
-
Olson, L.J.1
Orsi, R.2
Alculumbre, S.G.3
Peterson, F.C.4
Stigliano, I.D.5
Parodi, A.J.6
D'Alessio, C.7
Dahms, N.M.8
-
18
-
-
78650250452
-
Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation
-
Satoh, T.; Chen, Y.; Hu, D.; Hanashima, S.; Yamamoto, K.; Yamaguchi, Y. Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation. Mol. Cell 2010, 40, 905-916.
-
(2010)
Mol. Cell
, vol.40
, pp. 905-916
-
-
Satoh, T.1
Chen, Y.2
Hu, D.3
Hanashima, S.4
Yamamoto, K.5
Yamaguchi, Y.6
-
19
-
-
44849102178
-
Getting in and out from calnexin/calreticulin cycles
-
Caramelo, J.J.; Parodi, A.J. Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 2008, 283, 10221-10225.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 10221-10225
-
-
Caramelo, J.J.1
Parodi, A.J.2
-
20
-
-
77749326886
-
Sophisticated modes of sugar recognition by intracellular lectins involved in quality control of glycoproteins
-
Powell, G., McCabe, O. , Eds.; Nova Science Publisher: New York, NY, USA
-
Kamiya, Y.; Kamiya, D.; Urade, R.; Suzuki, T.; Kato, K. Sophisticated modes of sugar recognition by intracellular lectins involved in quality control of glycoproteins. In Glycobiology Research Trends; Powell, G., McCabe, O., Eds.; Nova Science Publisher: New York, NY, USA, 2009; pp. 27-40.
-
(2009)
Glycobiology Research Trends
, pp. 27-40
-
-
Kamiya, Y.1
Kamiya, D.2
Urade, R.3
Suzuki, T.4
Kato, K.5
-
21
-
-
0034799402
-
The structure of calnexin, an ER chaperone involved in quality control of protein folding
-
Schrag, J.D.; Bergeron, J.J.; Li, Y.; Borisova, S.; Hahn, M.; Thomas, D.Y.; Cygler, M. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 2001, 8, 633-644.
-
(2001)
Mol. Cell
, vol.8
, pp. 633-644
-
-
Schrag, J.D.1
Bergeron, J.J.2
Li, Y.3
Borisova, S.4
Hahn, M.5
Thomas, D.Y.6
Cygler, M.7
-
22
-
-
78649641361
-
Structural basis of carbohydrate recognition by calreticulin
-
Kozlov, G.; Pocanschi, C.L.; Rosenauer, A.; Bastos-Aristizabal, S.; Gorelik, A.; Williams, D.B.; Gehring, K. Structural basis of carbohydrate recognition by calreticulin. J. Biol. Chem. 2010, 285, 38612-38620.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 38612-38620
-
-
Kozlov, G.1
Pocanschi, C.L.2
Rosenauer, A.3
Bastos-Aristizabal, S.4
Gorelik, A.5
Williams, D.B.6
Gehring, K.7
-
23
-
-
79952663496
-
X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism
-
Chouquet, A.; Païdassi, H.; Ling, W.L.; Frachet, P.; Houen, G.; Arland, G.J.; Gaboriaud, F. X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism. PLoS One 2011, 6, e17886.
-
(2011)
PLoS One
, vol.6
, pp. e17886
-
-
Chouquet, A.1
Païdassi, H.2
Ling, W.L.3
Frachet, P.4
Houen, G.5
Arland, G.J.6
Gaboriaud, F.7
-
24
-
-
78149238000
-
Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain
-
Kozlov, G.; Bastos-Aristizabal, S.; Maattanen, P.; Rosenauer, A.; Zheng, F.; Killikelly, A.; Trempe, J.F.; Thomas, D.Y.; Gehring, K. Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. J. Biol. Chem. 2010, 285, 35551-35557.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 35551-35557
-
-
Kozlov, G.1
Bastos-Aristizabal, S.2
Maattanen, P.3
Rosenauer, A.4
Zheng, F.5
Killikelly, A.6
Trempe, J.F.7
Thomas, D.Y.8
Gehring, K.9
-
25
-
-
12144291328
-
Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system
-
Pollock, S.; Kozlov, G.; Pelletier, M.F.; Trempe, J.F.; Jansen, G.; Sitnikov, D.; Bergeron, J.J.; Gehring, K.; Ekiel, I.; Thomas, D.Y. Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system. EMBO J. 2004, 23, 1020-1029.
-
(2004)
EMBO J.
, vol.23
, pp. 1020-1029
-
-
Pollock, S.1
Kozlov, G.2
Pelletier, M.F.3
Trempe, J.F.4
Jansen, G.5
Sitnikov, D.6
Bergeron, J.J.7
Gehring, K.8
Ekiel, I.9
Thomas, D.Y.10
-
26
-
-
84907810734
-
PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin
-
Sakono, M.; Seko, A.; Takeda, Y.; Ito, Y. PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin. Biochem. Biophys. Res. Commun. 2014, 452, 27-31.
-
(2014)
Biochem. Biophys. Res. Commun.
, vol.452
, pp. 27-31
-
-
Sakono, M.1
Seko, A.2
Takeda, Y.3
Ito, Y.4
-
27
-
-
34948911583
-
Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36
-
Satoh, T.; Cowieson, N.P.; Hakamata, W.; Ideo, H.; Fukushima, K.; Kurihara, M.; Kato, R.; Yamashita, K.; Wakatsuki, S. Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36. J. Biol. Chem. 2007, 282, 28246-28255.
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 28246-28255
-
-
Satoh, T.1
Cowieson, N.P.2
Hakamata, W.3
Ideo, H.4
Fukushima, K.5
Kurihara, M.6
Kato, R.7
Yamashita, K.8
Wakatsuki, S.9
-
28
-
-
84880070996
-
Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII)
-
Zheng, C.; Page, R.C.; Das, V.; Nix, J.C.; Wigren, E.; Misra, S.; Zhang, B. Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII). J. Biol. Chem. 2013, 288, 20499-20509.
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 20499-20509
-
-
Zheng, C.1
Page, R.C.2
Das, V.3
Nix, J.C.4
Wigren, E.5
Misra, S.6
Zhang, B.7
-
29
-
-
84896861605
-
Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36
-
Satoh, T.; Suzuki, K.; Yamaguchi, T.; Kato, K. Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36. PLoS One 2014, 9, e87963.
-
(2014)
PLoS One
, vol.9
, pp. e87963
-
-
Satoh, T.1
Suzuki, K.2
Yamaguchi, T.3
Kato, K.4
-
30
-
-
0742322956
-
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation
-
Taylor, S.C.; Ferguson, A.D.; Bergeron, J.J.; Thomas, D.Y. The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation. Nat. Struct. Mol. Biol. 2004, 11, 128-134.
-
(2004)
Nat. Struct. Mol. Biol.
, vol.11
, pp. 128-134
-
-
Taylor, S.C.1
Ferguson, A.D.2
Bergeron, J.J.3
Thomas, D.Y.4
-
31
-
-
65249184983
-
The recognition motif of the glycoprotein-folding sensor enzyme UDP-Glc:Glycoprotein glucosyltransferase
-
Totani, K.; Ihara, Y.; Tsujimoto, T.; Matsuo, I.; Ito, Y. The recognition motif of the glycoprotein-folding sensor enzyme UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 2009, 48, 2933-2940.
-
(2009)
Biochemistry
, vol.48
, pp. 2933-2940
-
-
Totani, K.1
Ihara, Y.2
Tsujimoto, T.3
Matsuo, I.4
Ito, Y.5
-
32
-
-
0037422614
-
UDP-Glc:Glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
-
Caramelo, J.J.; Castro, O.A.; Alonso, L.G.; de Prat-Gay, G.; Parodi, A.J. UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proc. Natl. Acad. Sci. USA 2003, 100, 86-91.
-
(2003)
Proc. Natl. Acad. Sci. USA
, vol.100
, pp. 86-91
-
-
Caramelo, J.J.1
Castro, O.A.2
Alonso, L.G.3
De Prat-Gay, G.4
Parodi, A.J.5
-
33
-
-
84922143124
-
Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: Crystal structure of third thioredoxin-like domain of UDP-glucose:Glycoprotein glucosyltransferase
-
Zhu, T.; Satoh, T.; Kato, K. Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: Crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase. Sci. Rep. 2014, 4, 7322, doi:10.1038/srep07322.
-
(2014)
Sci. Rep.
, vol.4
, pp. 7322
-
-
Zhu, T.1
Satoh, T.2
Kato, K.3
-
34
-
-
27844454857
-
A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:Glycoprotein glucosyltransferase
-
Labunskyy, V.M.; Ferguson, A.D.; Fomenko, D.E.; Chelliah, Y.; Hatfield, D.L.; Gladyshev, V.N. A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase. J. Biol. Chem. 2005, 280, 37839-37845.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 37839-37845
-
-
Labunskyy, V.M.1
Ferguson, A.D.2
Fomenko, D.E.3
Chelliah, Y.4
Hatfield, D.L.5
Gladyshev, V.N.6
-
35
-
-
84898948025
-
Both isoforms of human UDP-glucose:Glycoprotein glucosyltransferase are enzymatically active
-
Takeda, Y.; Seko, A.; Hachisu, M.; Daikoku, S.; Izumi, M.; Koizumi, A.; Fujikawa, K.; Kajihara, Y.; Ito, Y. Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are enzymatically active. Glycobiology 2014, 24, 344-350.
-
(2014)
Glycobiology
, vol.24
, pp. 344-350
-
-
Takeda, Y.1
Seko, A.2
Hachisu, M.3
Daikoku, S.4
Izumi, M.5
Koizumi, A.6
Fujikawa, K.7
Kajihara, Y.8
Ito, Y.9
-
36
-
-
27744467536
-
Sugar-binding properties of VIP36, an intracellular animal lectin operating as a cargo receptor
-
Kamiya, Y.; Yamaguchi, Y.; Takahashi, N.; Arata, Y.; Kasai, K.I.; Ihara, Y.; Matsuo, I.; Ito, Y.; Yamamoto, K.; Kato, K. Sugar-binding properties of VIP36, an intracellular animal lectin operating as a cargo receptor. J. Biol. Chem. 2005, 280, 37178-37182.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 37178-37182
-
-
Kamiya, Y.1
Yamaguchi, Y.2
Takahashi, N.3
Arata, Y.4
Kasai, K.I.5
Ihara, Y.6
Matsuo, I.7
Ito, Y.8
Yamamoto, K.9
Kato, K.10
-
37
-
-
38349136210
-
Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36
-
Kamiya, Y.; Kamiya, D.; Yamamoto, K.; Nyfeler, B.; Hauri, H.P.; Kato, K. Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J. Biol. Chem. 2008, 283, 1857-1861.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 1857-1861
-
-
Kamiya, Y.1
Kamiya, D.2
Yamamoto, K.3
Nyfeler, B.4
Hauri, H.P.5
Kato, K.6
-
38
-
-
0023733211
-
Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
-
Schweizer, A.; Fransen, J.A.; Bachi, T.; Ginsel, L.; Hauri, H.P. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 1988, 107, 1643-1653.
-
(1988)
J. Cell Biol.
, vol.107
, pp. 1643-1653
-
-
Schweizer, A.1
Fransen, J.A.2
Bachi, T.3
Ginsel, L.4
Hauri, H.P.5
-
39
-
-
34248997838
-
N-glycan structure dictates extension of protein folding or onset of disposal
-
Molinari, M. N-glycan structure dictates extension of protein folding or onset of disposal. Nat. Chem. Biol. 2007, 3, 313-320.
-
(2007)
Nat. Chem. Biol.
, vol.3
, pp. 313-320
-
-
Molinari, M.1
-
40
-
-
84868583210
-
Subcellular localization of ERGIC-53 under endoplasmic reticulum stress condition
-
Qin, S.Y.; Kawasaki, N.; Hu, D.; Tozawa, H.; Matsumoto, N.; Yamamoto, K. Subcellular localization of ERGIC-53 under endoplasmic reticulum stress condition. Glycobiology 2012, 22, 1709-1720.
-
(2012)
Glycobiology
, vol.22
, pp. 1709-1720
-
-
Qin, S.Y.1
Kawasaki, N.2
Hu, D.3
Tozawa, H.4
Matsumoto, N.5
Yamamoto, K.6
-
41
-
-
0038532576
-
The role of glucosidase II and endomannosidase in glucose trimming of asparagine-liked oligosaccharides
-
Roth, J.; Ziak, M.; Zuber, C. The role of glucosidase II and endomannosidase in glucose trimming of asparagine-liked oligosaccharides. Biochimie 2003, 85, 287-294.
-
(2003)
Biochimie
, vol.85
, pp. 287-294
-
-
Roth, J.1
Ziak, M.2
Zuber, C.3
-
42
-
-
0021891884
-
Assembly of asparagine-liked oligosaccharides
-
Kornfeld, R.; Kornfeld, S. Assembly of asparagine-liked oligosaccharides. Annu. Rev. Biochem. 1985, 54, 631-664.
-
(1985)
Annu. Rev. Biochem.
, vol.54
, pp. 631-664
-
-
Kornfeld, R.1
Kornfeld, S.2
-
43
-
-
0032586737
-
Man α1-2 Man α-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition
-
Moothoo, D.N.; Canan, B.; Field, R.A.; Naismith, J.H. Man α1-2 Man α-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition. Glycobiology 1999, 9, 539-545.
-
(1999)
Glycobiology
, vol.9
, pp. 539-545
-
-
Moothoo, D.N.1
Canan, B.2
Field, R.A.3
Naismith, J.H.4
-
44
-
-
0038278822
-
Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex
-
Zhang, B.; Cunningham, M.A.; Nichols, W.C.; Bernat, J.A.; Seligsohn, U.; Pipe, S.W.; McVey, J.H.; Schulte-Overberg, U.; de Bosch, N.B.; Ruiz-Saez, A.; et al. Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex. Nat. Genet 2003, 34, 220-225.
-
(2003)
Nat. Genet
, vol.34
, pp. 220-225
-
-
Zhang, B.1
Cunningham, M.A.2
Nichols, W.C.3
Bernat, J.A.4
Seligsohn, U.5
Pipe, S.W.6
McVey, J.H.7
Schulte-Overberg, U.8
De Bosch, N.B.9
Ruiz-Saez, A.10
-
45
-
-
61849174315
-
Recent developments in the understanding of the combined deficiency of FV and FVIII
-
Zhang, B. Recent developments in the understanding of the combined deficiency of FV and FVIII. Br. J. Haematol. 2009, 145, 15-23.
-
(2009)
Br. J. Haematol.
, vol.145
, pp. 15-23
-
-
Zhang, B.1
-
46
-
-
21844438479
-
LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway
-
Zhang, B.; Kaufman, R.J.; Ginsburg, D. LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J. Biol. Chem. 2005, 280, 25881-25886.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 25881-25886
-
-
Zhang, B.1
Kaufman, R.J.2
Ginsburg, D.3
-
47
-
-
33749510461
-
Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex
-
Nyfeler, B.; Zhang, B.; Ginsburg, D.; Kaufman, R.J.; Hauri, H.P. Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex. Traffic 2006, 7, 1473-1481.
-
(2006)
Traffic
, vol.7
, pp. 1473-1481
-
-
Nyfeler, B.1
Zhang, B.2
Ginsburg, D.3
Kaufman, R.J.4
Hauri, H.P.5
-
48
-
-
77749233842
-
Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency
-
Nishio, M.; Kamiya, Y.; Mizushima, T.; Wakatsuki, S.; Sasakawa, H.; Yamamoto, K.; Uchiyama, S.; Noda, M.; McKay, A.R.; Fukui, K.; et al. Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency. Proc. Natl. Acad. Sci. USA 2010, 107, 4034-4039.
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 4034-4039
-
-
Nishio, M.1
Kamiya, Y.2
Mizushima, T.3
Wakatsuki, S.4
Sasakawa, H.5
Yamamoto, K.6
Uchiyama, S.7
Noda, M.8
McKay, A.R.9
Fukui, K.10
-
49
-
-
76749118043
-
Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII
-
Wigren, E.; Bourhis, J.M.; Kursula, I.; Guy, J.E.; Lindqvist, Y. Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII. FEBS Lett. 2010, 584, 878-882.
-
(2010)
FEBS Lett.
, vol.584
, pp. 878-882
-
-
Wigren, E.1
Bourhis, J.M.2
Kursula, I.3
Guy, J.E.4
Lindqvist, Y.5
-
50
-
-
84882768894
-
Regulation of Mac-2BP secretion is mediated by its N-glycan binding to ERGIC-53
-
Chen, Y.; Hojo, S.; Matsumoto, N.; Yamamoto, K. Regulation of Mac-2BP secretion is mediated by its N-glycan binding to ERGIC-53. Glycobiology 2013, 23, 904-916.
-
(2013)
Glycobiology
, vol.23
, pp. 904-916
-
-
Chen, Y.1
Hojo, S.2
Matsumoto, N.3
Yamamoto, K.4
-
51
-
-
84887868167
-
The intracellular cargo receptor ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles
-
Klaus, J.P.; Eisenhauer, P.; Russo, J.; Mason, A.B.; Do, D.; King, B.; Taatjes, D.; Cornillez-Ty, C.; Boyson, J.E.; Thali, M.; et al. The intracellular cargo receptor ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles. Cell Host Microbe 2013, 14, 522-534.
-
(2013)
Cell Host Microbe
, vol.14
, pp. 522-534
-
-
Klaus, J.P.1
Eisenhauer, P.2
Russo, J.3
Mason, A.B.4
Do, D.5
King, B.6
Taatjes, D.7
Cornillez-Ty, C.8
Boyson, J.E.9
Thali, M.10
-
52
-
-
0034980520
-
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast
-
Jakob, C.A.; Bodmer, D.; Spirig, U.; Battig, P.; Marcil, A.; Dignard, D.; Bergeron, J.J.; Thomas, D.Y.; Aebi, M. Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep. 2001, 2, 423-430.
-
(2001)
EMBO Rep.
, vol.2
, pp. 423-430
-
-
Jakob, C.A.1
Bodmer, D.2
Spirig, U.3
Battig, P.4
Marcil, A.5
Dignard, D.6
Bergeron, J.J.7
Thomas, D.Y.8
Aebi, M.9
-
53
-
-
0034981027
-
A novel ER α-mannosidase-like protein accelerates ER-associated degradation
-
Hosokawa, N.; Wada, I.; Hasegawa, K.; Yorihuzi, T.; Tremblay, L.O.; Herscovics, A.; Nagata, K. A novel ER α-mannosidase-like protein accelerates ER-associated degradation. EMBO Rep. 2001, 2, 415-422.
-
(2001)
EMBO Rep.
, vol.2
, pp. 415-422
-
-
Hosokawa, N.1
Wada, I.2
Hasegawa, K.3
Yorihuzi, T.4
Tremblay, L.O.5
Herscovics, A.6
Nagata, K.7
-
54
-
-
0034651605
-
Crystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control
-
Vallée, F.; Lipari, F.; Yip, P.; Sleno, B.; Herscovics, A.; Howell, P.L. Crystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control. EMBO J. 2000, 19, 581-588.
-
(2000)
EMBO J.
, vol.19
, pp. 581-588
-
-
Vallée, F.1
Lipari, F.2
Yip, P.3
Sleno, B.4
Herscovics, A.5
Howell, P.L.6
-
55
-
-
0034731519
-
Structural basis for catalysis and inhibition of N-glycan processing class I α1,2-mannosidases
-
Vallée, F.; Karaveg, K.; Herscovics, A.; Moremen, K.W.; Howell, P.L. Structural basis for catalysis and inhibition of N-glycan processing class I α1,2-mannosidases. J. Biol. Chem. 2000, 275, 41287-41298.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 41287-41298
-
-
Vallée, F.1
Karaveg, K.2
Herscovics, A.3
Moremen, K.W.4
Howell, P.L.5
-
56
-
-
23844499082
-
Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) α-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control
-
Karaveg, K.; Moremen, K.W. Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) α-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J. Biol. Chem. 2005, 280, 29837-29848.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 29837-29848
-
-
Karaveg, K.1
Moremen, K.W.2
-
57
-
-
18144419652
-
Mechanism of class 1 (glycosylhydrolase family 47) α-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control
-
Karaveg, K.; Siriwardena, A.; Tempel, W.; Liu, Z.J.; Glushka, J.; Wang, B.C.; Moremen, K.W. Mechanism of class 1 (glycosylhydrolase family 47) α-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J. Biol. Chem. 2005, 280, 16197-16207.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 16197-16207
-
-
Karaveg, K.1
Siriwardena, A.2
Tempel, W.3
Liu, Z.J.4
Glushka, J.5
Wang, B.C.6
Moremen, K.W.7
-
58
-
-
33646928455
-
EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming
-
Hirao, K.; Natsuka, Y.; Tamura, T.; Wada, I.; Morito, D.; Natsuka, S.; Romero, P.; Sleno, B.; Tremblay, L.O.; Herscovics, A.; et al. EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming. J. Biol. Chem. 2006, 281, 9650-9658.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 9650-9658
-
-
Hirao, K.1
Natsuka, Y.2
Tamura, T.3
Wada, I.4
Morito, D.5
Natsuka, S.6
Romero, P.7
Sleno, B.8
Tremblay, L.O.9
Herscovics, A.10
-
59
-
-
13244265787
-
A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation
-
Olivari, S.; Galli, C.; Alanen, H.; Ruddock, L.; Molinari, M. A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation. J. Biol. Chem. 2005, 280, 2424-2428.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 2424-2428
-
-
Olivari, S.1
Galli, C.2
Alanen, H.3
Ruddock, L.4
Molinari, M.5
-
60
-
-
57749083532
-
Defining the glycan destruction signal for endoplasmic reticulum-associated degradation
-
Quan, E.M.; Kamiya, Y.; Kamiya, D.; Denic, V.; Weibezahn, J.; Kato, K.; Weissman, J.S. Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol. Cell 2008, 32, 870-877.
-
(2008)
Mol. Cell
, vol.32
, pp. 870-877
-
-
Quan, E.M.1
Kamiya, Y.2
Kamiya, D.3
Denic, V.4
Weibezahn, J.5
Kato, K.6
Weissman, J.S.7
-
61
-
-
59849119398
-
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
-
Clerc, S.; Hirsch, C.; Oggier, D.M.; Deprez, P.; Jakob, C.; Sommer, T.; Aebi, M. Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J. Cell Biol. 2009, 184, 159-172.
-
(2009)
J. Cell Biol.
, vol.184
, pp. 159-172
-
-
Clerc, S.1
Hirsch, C.2
Oggier, D.M.3
Deprez, P.4
Jakob, C.5
Sommer, T.6
Aebi, M.7
-
62
-
-
67650535999
-
Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
-
Hosokawa, N.; Kamiya, Y.; Kamiya, D.; Kato, K.; Nagata, K. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J. Biol. Chem. 2009, 284, 17061-17068.
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 17061-17068
-
-
Hosokawa, N.1
Kamiya, Y.2
Kamiya, D.3
Kato, K.4
Nagata, K.5
-
63
-
-
77952811195
-
EDEM1 accelerates the trimming of α1,2-linked mannose on the C branch of N-glycans
-
Hosokawa, N.; Tremblay, L.O.; Sleno, B.; Kamiya, Y.; Wada, I.; Nagata, K.; Kato, K.; Herscovics, A. EDEM1 accelerates the trimming of α1,2-linked mannose on the C branch of N-glycans. Glycobiology 2010, 20, 567-575.
-
(2010)
Glycobiology
, vol.20
, pp. 567-575
-
-
Hosokawa, N.1
Tremblay, L.O.2
Sleno, B.3
Kamiya, Y.4
Wada, I.5
Nagata, K.6
Kato, K.7
Herscovics, A.8
-
64
-
-
84905987689
-
EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step
-
Ninagawa, S.; Okada, T.; Sumitomo, Y.; Kamiya, Y.; Kato, K.; Horimoto, S.; Ishikawa, T.; Takeda, S.; Sakuma, T.; Yamamoto, T.; et al. EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step. J. Cell Biol. 2014, 206, 347-356.
-
(2014)
J. Cell Biol.
, vol.206
, pp. 347-356
-
-
Ninagawa, S.1
Okada, T.2
Sumitomo, Y.3
Kamiya, Y.4
Kato, K.5
Horimoto, S.6
Ishikawa, T.7
Takeda, S.8
Sakuma, T.9
Yamamoto, T.10
-
65
-
-
79959357020
-
A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum
-
Gauss, R.; Kanehara, K.; Carvalho, P.; Ng, D.T.; Aebi, M. A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum. Mol. Cell 2011, 42, 782-793.
-
(2011)
Mol. Cell
, vol.42
, pp. 782-793
-
-
Gauss, R.1
Kanehara, K.2
Carvalho, P.3
Ng, D.T.4
Aebi, M.5
-
66
-
-
0028198111
-
How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
-
Helenius, A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 1994, 5, 253-265.
-
(1994)
Mol. Biol. Cell
, vol.5
, pp. 253-265
-
-
Helenius, A.1
-
67
-
-
77949889295
-
The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation
-
Mikami, K.; Yamaguchi, D.; Tateno, H.; Hu, D.; Qin, S.Y.; Kawasaki, N.; Yamada, M.; Matsumoto, N.; Hirabayashi, J.; Ito, Y.; et al. The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation. Glycobiology 2010, 20, 310-321.
-
(2010)
Glycobiology
, vol.20
, pp. 310-321
-
-
Mikami, K.1
Yamaguchi, D.2
Tateno, H.3
Hu, D.4
Qin, S.Y.5
Kawasaki, N.6
Yamada, M.7
Matsumoto, N.8
Hirabayashi, J.9
Ito, Y.10
-
68
-
-
47749109897
-
A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal
-
Bernasconi, R.; Pertel, T.; Luban, J.; Molinari, M. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal. J. Biol. Chem. 2008, 283, 16446-16454.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 16446-16454
-
-
Bernasconi, R.1
Pertel, T.2
Luban, J.3
Molinari, M.4
-
69
-
-
40249088336
-
OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
-
Christianson, J.C.; Shaler, T.A.; Tyler, R.E.; Kopito, R.R. OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 2008, 10, 272-282.
-
(2008)
Nat. Cell Biol.
, vol.10
, pp. 272-282
-
-
Christianson, J.C.1
Shaler, T.A.2
Tyler, R.E.3
Kopito, R.R.4
-
71
-
-
84875364799
-
Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant
-
Fujimori, T.; Kamiya, Y.; Nagata, K.; Kato, K.; Hosokawa, N. Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant. FEBS J. 2013, 280, 1563-1575.
-
(2013)
FEBS J.
, vol.280
, pp. 1563-1575
-
-
Fujimori, T.1
Kamiya, Y.2
Nagata, K.3
Kato, K.4
Hosokawa, N.5
-
72
-
-
84907829386
-
Characterization of the Grp94/OS-9 chaperone-lectin complex
-
Seidler, P.M.; Shinsky, S.A.; Hong, F.; Li, Z.; Cosgrove, M.S.; Gewirth, D.T. Characterization of the Grp94/OS-9 chaperone-lectin complex. J. Mol. Biol. 2014, 426, 3590-3605.
-
(2014)
J. Mol. Biol.
, vol.426
, pp. 3590-3605
-
-
Seidler, P.M.1
Shinsky, S.A.2
Hong, F.3
Li, Z.4
Cosgrove, M.S.5
Gewirth, D.T.6
-
73
-
-
84905275409
-
OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation
-
Dersh, D.; Jones, S.M.; Eletto, D.; Christianson, J.C.; Argon, Y. OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation. Mol. Biol. Cell 2014, 25, 2220-2234.
-
(2014)
Mol. Biol. Cell
, vol.25
, pp. 2220-2234
-
-
Dersh, D.1
Jones, S.M.2
Eletto, D.3
Christianson, J.C.4
Argon, Y.5
-
74
-
-
84858039295
-
Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex
-
Hanna, J.; Schutz, A.; Zimmermann, F.; Behlke, J.; Sommer, T.; Heinemann, U. Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex. J. Biol. Chem. 2012, 287, 8633-8640.
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 8633-8640
-
-
Hanna, J.1
Schutz, A.2
Zimmermann, F.3
Behlke, J.4
Sommer, T.5
Heinemann, U.6
-
75
-
-
84956477144
-
Protein-carbohydrate interaction: Fundamental considerations
-
Ernst, B., Hart, G.W., Sinaÿ, P. Wiley-VCH: Weinhein, Germany
-
Burkhalter, N.F.; Dimick, S.M.; Toone, E.J. Protein-carbohydrate interaction: Fundamental considerations. In Carbohydrates in Chemistry and Biology, Part II; Ernst, B., Hart, G.W., Sinaÿ, P., Eds.; Wiley-VCH: Weinhein, Germany, 2000; Volume 2, pp. 863-914.
-
(2000)
Carbohydrates in Chemistry and Biology, Part II
, vol.2
, pp. 863-914
-
-
Burkhalter, N.F.1
Dimick, S.M.2
Toone, E.J.3
-
76
-
-
85016338076
-
13C labeling in conjunction with high-field nuclear magnetic resonance spectroscopy for comparative conformational analysis of high mannose-type oligosaccharides
-
13C labeling in conjunction with high-field nuclear magnetic resonance spectroscopy for comparative conformational analysis of high mannose-type oligosaccharides. Biomolecules 2013, 3, 108-123.
-
(2013)
Biomolecules
, vol.3
, pp. 108-123
-
-
Kamiya, Y.1
Yanagi, K.2
Kitajima, T.3
Yamaguchi, T.4
Chiba, Y.5
Kato, K.6
-
77
-
-
84877596270
-
Terminal spin labeling of a high-mannose-type oligosaccharide for quantitative NMR analysis of its dynamic conformation
-
Yamaguchi, T.; Kamiya, Y.; Choo, Y.-M.; Yamamoto, S.; Kato, K. Terminal spin labeling of a high-mannose-type oligosaccharide for quantitative NMR analysis of its dynamic conformation. Chem. Lett. 2013, 42, 544-546.
-
(2013)
Chem. Lett.
, vol.42
, pp. 544-546
-
-
Yamaguchi, T.1
Kamiya, Y.2
Choo, Y.-M.3
Yamamoto, S.4
Kato, K.5
-
78
-
-
0025349114
-
Primary sequence dependence of conformation in oligomannose oligosaccharides
-
Wooten, E.W.; Bazzo, R.; Edge, C.J.; Zamze, S.; Dwek, R.A.; Rademacher, T.W. Primary sequence dependence of conformation in oligomannose oligosaccharides. Eur. Biophys. J. 1990, 18, 139-148.
-
(1990)
Eur. Biophys. J.
, vol.18
, pp. 139-148
-
-
Wooten, E.W.1
Bazzo, R.2
Edge, C.J.3
Zamze, S.4
Dwek, R.A.5
Rademacher, T.W.6
-
79
-
-
0036462598
-
Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling
-
Wormald, M.R.; Petrescu, A.J.; Pao, Y.L.; Glithero, A.; Elliott, T.; Dwek, R.A. Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling. Chem. Rev. 2002, 102, 371-386.
-
(2002)
Chem. Rev.
, vol.102
, pp. 371-386
-
-
Wormald, M.R.1
Petrescu, A.J.2
Pao, Y.L.3
Glithero, A.4
Elliott, T.5
Dwek, R.A.6
-
80
-
-
0028041189
-
Molecular dynamics simulations of high-mannose oligosaccharides
-
Balaji, P.V.; Qasba, P.K.; Rao, V.S. Molecular dynamics simulations of high-mannose oligosaccharides. Glycobiology 1994, 4, 497-515.
-
(1994)
Glycobiology
, vol.4
, pp. 497-515
-
-
Balaji, P.V.1
Qasba, P.K.2
Rao, V.S.3
-
81
-
-
0030839727
-
The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding
-
Petrescu, A.J.; Butters, T.D.; Reinkensmeier, G.; Petrescu, S.; Platt, F.M.; Dwek, R.A.; Wormald, M.R. The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 1997, 16, 4302-4310.
-
(1997)
EMBO J.
, vol.16
, pp. 4302-4310
-
-
Petrescu, A.J.1
Butters, T.D.2
Reinkensmeier, G.3
Petrescu, S.4
Platt, F.M.5
Dwek, R.A.6
Wormald, M.R.7
-
82
-
-
84912051180
-
Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation
-
Zhang, Y.; Yamaguchi, T.; Satoh, T.; Yagi-Utsumi, M.; Kamiya, Y.; Sakae, Y.; Okamoto, Y.; Kato, K. Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation. Adv. Exp. Med. Biol. 2015, 842, 217-230.
-
(2015)
Adv. Exp. Med. Biol.
, vol.842
, pp. 217-230
-
-
Zhang, Y.1
Yamaguchi, T.2
Satoh, T.3
Yagi-Utsumi, M.4
Kamiya, Y.5
Sakae, Y.6
Okamoto, Y.7
Kato, K.8
-
83
-
-
84964257784
-
Paramagnetism-assisted nuclear magnetic resonance analysis of dynamic conformations and interactions of oligosaccharides
-
Taniguchi, N., Endo, T., Hart, G.W., Seeberger, P., Wong, C.-H., Eds.; Springer: Tokyo, Japan in press
-
Yamaguchi, T.; Kato, K. Paramagnetism-assisted nuclear magnetic resonance analysis of dynamic conformations and interactions of oligosaccharides. In Glycoscience: Biology and Medicine; Taniguchi, N., Endo, T., Hart, G.W., Seeberger, P., Wong, C.-H., Eds.; Springer: Tokyo, Japan, 2014, in press, doi:10.1007/978-4-431-54836-2-101-1.
-
(2014)
Glycoscience: Biology and Medicine
-
-
Yamaguchi, T.1
Kato, K.2
-
84
-
-
84922189307
-
Exploration of conformational spaces of high-mannose-type oligosaccharides by an NMR-validated simulation
-
Yamaguchi, T.; Sakae, Y.; Zhang, Y.; Yamamoto, S.; Okamoto, Y.; Kato, K. Exploration of conformational spaces of high-mannose-type oligosaccharides by an NMR-validated simulation. Angew. Chem. Int. Ed. 2014, 53, 10941-10944.
-
(2014)
Angew. Chem. Int. Ed.
, vol.53
, pp. 10941-10944
-
-
Yamaguchi, T.1
Sakae, Y.2
Zhang, Y.3
Yamamoto, S.4
Okamoto, Y.5
Kato, K.6
|