-
1
-
-
84892666600
-
The challenge and promise of glycomics
-
COI: 1:CAS:528:DC%2BC2cXhtF2msb8%3D, PID: 24439204
-
Cummings, R. D. & Pierce, J. M. The challenge and promise of glycomics. Chem. Biol. 21, 1–15 (2014).
-
(2014)
Chem. Biol.
, vol.21
, pp. 1-15
-
-
Cummings, R.D.1
Pierce, J.M.2
-
2
-
-
85014440279
-
Biological roles of glycans
-
COI: 1:CAS:528:DC%2BC1cXhsVSisLY%3D, PID: 27558841
-
Varki, A. Biological roles of glycans. Glycobiology 27, 3–49 (2017).
-
(2017)
Glycobiology
, vol.27
, pp. 3-49
-
-
Varki, A.1
-
3
-
-
84862728161
-
Vertebrate protein glycosylation: diversity, synthesis and function
-
COI: 1:CAS:528:DC%2BC38XovFyktLs%3D, PID: 22722607
-
Moremen, K. W., Tiemeyer, M. & Nairn, A. V. Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13, 448–462 (2012).
-
(2012)
Nat. Rev. Mol. Cell Biol.
, vol.13
, pp. 448-462
-
-
Moremen, K.W.1
Tiemeyer, M.2
Nairn, A.V.3
-
4
-
-
85040782404
-
Expression system for structural and functional studies of human glycosylation enzymes
-
COI: 1:CAS:528:DC%2BC2sXhvFyrsr7P, PID: 29251719
-
Moremen, K. W. et al. Expression system for structural and functional studies of human glycosylation enzymes. Nat. Chem. Biol. 14, 156–162 (2018).
-
(2018)
Nat. Chem. Biol.
, vol.14
, pp. 156-162
-
-
Moremen, K.W.1
-
5
-
-
49449087287
-
Glycosyltransferases: structures, functions, and mechanisms
-
COI: 1:CAS:528:DC%2BD1cXos1ekurY%3D, PID: 18518825
-
Lairson, L. L., Henrissat, B., Davies, G. J. & Withers, S. G. Glycosyltransferases: structures, functions, and mechanisms. Annu. Rev. Biochem. 77, 521–555 (2008).
-
(2008)
Annu. Rev. Biochem.
, vol.77
, pp. 521-555
-
-
Lairson, L.L.1
Henrissat, B.2
Davies, G.J.3
Withers, S.G.4
-
6
-
-
84891763855
-
The carbohydrate-active enzymes database (CAZy) in 2013
-
COI: 1:CAS:528:DC%2BC2cXoslWn, PID: 24270786
-
Lombard, V., Golaconda Ramulu, H., Drula, E., Coutinho, P. M. & Henrissat, B. The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 42, D490–D495 (2014).
-
(2014)
Nucleic Acids Res.
, vol.42
, pp. D490-D495
-
-
Lombard, V.1
Golaconda Ramulu, H.2
Drula, E.3
Coutinho, P.M.4
Henrissat, B.5
-
7
-
-
0024322304
-
The allosteric transition of glycogen phosphorylase
-
COI: 1:CAS:528:DyaL1MXlsV2ntb8%3D, PID: 2770867
-
Barford, D. & Johnson, L. N. The allosteric transition of glycogen phosphorylase. Nature 340, 609–616 (1989).
-
(1989)
Nature
, vol.340
, pp. 609-616
-
-
Barford, D.1
Johnson, L.N.2
-
8
-
-
84901830981
-
The Cosmc connection to the Tn antigen in cancer
-
PID: 24643043
-
Ju, T., Aryal, R. P., Kudelka, M. R., Wang, Y. & Cummings, R. D. The Cosmc connection to the Tn antigen in cancer. Cancer Biomark. 14, 63–81 (2014).
-
(2014)
Cancer Biomark.
, vol.14
, pp. 63-81
-
-
Ju, T.1
Aryal, R.P.2
Kudelka, M.R.3
Wang, Y.4
Cummings, R.D.5
-
9
-
-
77950459311
-
-
(eds. Varki, A, Cummings, R.D., Esko, J.D. et al.), Cold Spring Harbor, NY
-
Rini, J.M. & Esko, J.D. in Essentials of Glycobiology (eds. Varki, A, Cummings, R.D., Esko, J.D. et al.) 65–75 (Cold Spring Harbor, NY, 2015).
-
(2015)
Essentials of Glycobiology
, pp. 65-75
-
-
Rini, J.M.1
Esko, J.D.2
-
10
-
-
84974715560
-
The biochemistry of O-GlcNAc transferase: which functions make it essential in mammalian cells?
-
COI: 1:CAS:528:DC%2BC28XpvV2ksr8%3D, PID: 27294441
-
Levine, Z. G. & Walker, S. The biochemistry of O-GlcNAc transferase: which functions make it essential in mammalian cells? Annu. Rev. Biochem. 85, 631–657 (2016).
-
(2016)
Annu. Rev. Biochem.
, vol.85
, pp. 631-657
-
-
Levine, Z.G.1
Walker, S.2
-
11
-
-
85058061655
-
Cryo-EM is uncovering the mechanism of eukaryotic protein N-glycosylation
-
COI: 1:CAS:528:DC%2BC1cXitlKlsrfL, PID: 30450807
-
Bai, L. & Li, H. Cryo-EM is uncovering the mechanism of eukaryotic protein N-glycosylation. FEBS J. 286, 1638–1644 (2019).
-
(2019)
FEBS J.
, vol.286
, pp. 1638-1644
-
-
Bai, L.1
Li, H.2
-
12
-
-
84995426440
-
Structure and protein-protein interactions of human UDP-glucuronosyltransferases
-
COI: 1:CAS:528:DC%2BC1cXhtlWntbo%3D, PID: 27822186
-
Fujiwara, R., Yokoi, T. & Nakajima, M. Structure and protein-protein interactions of human UDP-glucuronosyltransferases. Front. Pharmacol. 7, 388 (2016).
-
(2016)
Front. Pharmacol.
, vol.7
, pp. 388
-
-
Fujiwara, R.1
Yokoi, T.2
Nakajima, M.3
-
13
-
-
0035967864
-
Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I
-
COI: 1:CAS:528:DC%2BD3MXksFSrs78%3D, PID: 11419947
-
Ramakrishnan, B. & Qasba, P. K. Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I. J. Mol. Biol. 310, 205–218 (2001).
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 205-218
-
-
Ramakrishnan, B.1
Qasba, P.K.2
-
14
-
-
42949090427
-
Structure and function of β-1,4-galactosyltransferase
-
COI: 1:CAS:528:DC%2BD1cXkvFelsbc%3D, PID: 18393823
-
Qasba, P. K., Ramakrishnan, B. & Boeggeman, E. Structure and function of β-1,4-galactosyltransferase. Curr. Drug Targets 9, 292–309 (2008).
-
(2008)
Curr. Drug Targets
, vol.9
, pp. 292-309
-
-
Qasba, P.K.1
Ramakrishnan, B.2
Boeggeman, E.3
-
15
-
-
0036019552
-
Crystal structure of β1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site
-
COI: 1:CAS:528:DC%2BD38XktlCksLY%3D, PID: 12051854
-
Ramakrishnan, B., Balaji, P. V. & Qasba, P. K. Crystal structure of β1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site. J. Mol. Biol. 318, 491–502 (2002).
-
(2002)
J. Mol. Biol.
, vol.318
, pp. 491-502
-
-
Ramakrishnan, B.1
Balaji, P.V.2
Qasba, P.K.3
-
16
-
-
84946779761
-
High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner
-
COI: 1:CAS:528:DC%2BC2MXhslyrtrnP, PID: 26374898
-
Gagnon, S. M. et al. High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner. J. Biol. Chem. 290, 27040–27052 (2015).
-
(2015)
J. Biol. Chem.
, vol.290
, pp. 27040-27052
-
-
Gagnon, S.M.1
-
17
-
-
84951759208
-
Novel UDP-GalNAc derivative structures provide insight into the donor specificity of human blood group glycosyltransferase
-
COI: 1:CAS:528:DC%2BC2MXitV2is7nM, PID: 26527682
-
Wagner, G. K., Pesnot, T., Palcic, M. M. & Jørgensen, R. Novel UDP-GalNAc derivative structures provide insight into the donor specificity of human blood group glycosyltransferase. J. Biol. Chem. 290, 31162–31172 (2015).
-
(2015)
J. Biol. Chem.
, vol.290
, pp. 31162-31172
-
-
Wagner, G.K.1
Pesnot, T.2
Palcic, M.M.3
Jørgensen, R.4
-
18
-
-
31144449168
-
Structures and mechanisms of glycosyltransferases
-
COI: 1:CAS:528:DC%2BD28XksVymtA%3D%3D, PID: 16037492
-
Breton, C., Snajdrová, L., Jeanneau, C., Koca, J. & Imberty, A. Structures and mechanisms of glycosyltransferases. Glycobiology 16, 29R–37R (2006).
-
(2006)
Glycobiology
, vol.16
, pp. 29R-37R
-
-
Breton, C.1
Snajdrová, L.2
Jeanneau, C.3
Koca, J.4
Imberty, A.5
-
19
-
-
80053157756
-
Structural insights into the mechanism of protein O-fucosylation
-
COI: 1:CAS:528:DC%2BC3MXhtleisLjM, PID: 21966509
-
Lira-Navarrete, E. et al. Structural insights into the mechanism of protein O-fucosylation. PLoS One 6, e25365 (2011).
-
(2011)
PLoS One
, vol.6
-
-
Lira-Navarrete, E.1
-
20
-
-
85021122264
-
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1
-
COI: 1:CAS:528:DC%2BC2sXotVOltLw%3D, PID: 28530709
-
Li, Z. et al. Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1. Nat. Chem. Biol. 13, 757–763 (2017).
-
(2017)
Nat. Chem. Biol.
, vol.13
, pp. 757-763
-
-
Li, Z.1
-
21
-
-
85028455278
-
Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism
-
COI: 1:CAS:528:DC%2BC2sXhtl2gu7%2FP, PID: 28670741
-
Urbanowicz, B. R. et al. Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism. Plant J. 91, 931–949 (2017).
-
(2017)
Plant J.
, vol.91
, pp. 931-949
-
-
Urbanowicz, B.R.1
-
22
-
-
84945290553
-
Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism
-
COI: 1:CAS:528:DC%2BC2MXhsFeiu7bK, PID: 26414444
-
Yu, H. et al. Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. Nat. Chem. Biol. 11, 847–854 (2015).
-
(2015)
Nat. Chem. Biol.
, vol.11
, pp. 847-854
-
-
Yu, H.1
-
23
-
-
84905366680
-
Substrate-guided front-face reaction revealed by combined structural snapshots and metadynamics for the polypeptide N-acetylgalactosaminyltransferase 2
-
COI: 1:CAS:528:DC%2BC2cXhtVantrbL
-
Lira-Navarrete, E. et al. Substrate-guided front-face reaction revealed by combined structural snapshots and metadynamics for the polypeptide N-acetylgalactosaminyltransferase 2. Angew. Chem. Int. Edn Engl. 53, 8206–8210 (2014).
-
(2014)
Angew. Chem. Int. Edn Engl.
, vol.53
, pp. 8206-8210
-
-
Lira-Navarrete, E.1
-
24
-
-
84938976766
-
A native ternary complex trapped in a crystal reveals the catalytic mechanism of a retaining glycosyltransferase
-
Albesa-Jové, D. et al. A native ternary complex trapped in a crystal reveals the catalytic mechanism of a retaining glycosyltransferase. Angew. Chem. Int. Edn Engl. 54, 9898–9902 (2015).
-
(2015)
Angew. Chem. Int. Edn Engl.
, vol.54
, pp. 9898-9902
-
-
Albesa-Jové, D.1
-
25
-
-
85031726299
-
Structural snapshots of α-1,3-galactosyltransferase with native substrates: insight into the catalytic mechanism of retaining glycosyltransferases
-
Albesa-Jové, D., Sainz-Polo, M. A., Marina, A. & Guerin, M. E. Structural snapshots of α-1,3-galactosyltransferase with native substrates: insight into the catalytic mechanism of retaining glycosyltransferases. Angew. Chem. Int. Edn Engl. 56, 14853–14857 (2017).
-
(2017)
Angew. Chem. Int. Edn Engl.
, vol.56
, pp. 14853-14857
-
-
Albesa-Jové, D.1
Sainz-Polo, M.A.2
Marina, A.3
Guerin, M.E.4
-
26
-
-
77952024581
-
Crystal structure of the catalytic domain of Drosophila beta1,4-galactosyltransferase-7
-
COI: 1:CAS:528:DC%2BC3cXlslSqtrw%3D, PID: 20236943
-
Ramakrishnan, B. & Qasba, P. K. Crystal structure of the catalytic domain of Drosophila beta1,4-galactosyltransferase-7. J. Biol. Chem. 285, 15619–15626 (2010).
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 15619-15626
-
-
Ramakrishnan, B.1
Qasba, P.K.2
-
27
-
-
84957894741
-
Recent structural and mechanistic insights into protein O-GalNAc glycosylation
-
COI: 1:CAS:528:DC%2BC28XisVWru7k%3D, PID: 26862189
-
Hurtado-Guerrero, R. Recent structural and mechanistic insights into protein O-GalNAc glycosylation. Biochem. Soc. Trans. 44, 61–67 (2016).
-
(2016)
Biochem. Soc. Trans.
, vol.44
, pp. 61-67
-
-
Hurtado-Guerrero, R.1
-
28
-
-
84957900542
-
The reaction mechanism of retaining glycosyltransferases
-
PID: 26862188
-
Ardèvol, A., Iglesias-Fernández, J., Rojas-Cervellera, V. & Rovira, C. The reaction mechanism of retaining glycosyltransferases. Biochem. Soc. Trans. 44, 51–60 (2016).
-
(2016)
Biochem. Soc. Trans.
, vol.44
, pp. 51-60
-
-
Ardèvol, A.1
Iglesias-Fernández, J.2
Rojas-Cervellera, V.3
Rovira, C.4
-
29
-
-
84947419831
-
QM/MM studies reveal how substrate-substrate and enzyme-substrate interactions modulate retaining glycosyltransferases catalysis and mechanism
-
PID: 26415846
-
Gómez, H., Mendoza, F., Lluch, J. M. & Masgrau, L. QM/MM studies reveal how substrate-substrate and enzyme-substrate interactions modulate retaining glycosyltransferases catalysis and mechanism. Adv. Protein Chem. Struct. Biol. 100, 225–254 (2015).
-
(2015)
Adv. Protein Chem. Struct. Biol.
, vol.100
, pp. 225-254
-
-
Gómez, H.1
Mendoza, F.2
Lluch, J.M.3
Masgrau, L.4
-
30
-
-
84881007618
-
Geometric attributes of retaining glycosyltransferase enzymes favor an orthogonal mechanism
-
COI: 1:CAS:528:DC%2BC3sXht12mt7%2FL, PID: 23936487
-
Schuman, B., Evans, S. V. & Fyles, T. M. Geometric attributes of retaining glycosyltransferase enzymes favor an orthogonal mechanism. PLoS One 8, e71077 (2013).
-
(2013)
PLoS One
, vol.8
-
-
Schuman, B.1
Evans, S.V.2
Fyles, T.M.3
-
31
-
-
85046261666
-
Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite
-
COI: 1:CAS:528:DC%2BC1cXhvVGht7vM, PID: 29666272
-
Kadirvelraj, R. et al. Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite. Proc. Natl Acad. Sci. USA 115, 4637–4642 (2018).
-
(2018)
Proc. Natl Acad. Sci. USA
, vol.115
, pp. 4637-4642
-
-
Kadirvelraj, R.1
-
32
-
-
33745246850
-
X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues
-
COI: 1:CAS:528:DC%2BD28Xmt1yku7s%3D, PID: 16769084
-
Gordon, R. D. et al. X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues. J. Mol. Biol. 360, 67–79 (2006).
-
(2006)
J. Mol. Biol.
, vol.360
, pp. 67-79
-
-
Gordon, R.D.1
-
33
-
-
33748756443
-
X-ray crystal structure of leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism
-
COI: 1:CAS:528:DC%2BD28XovF2jtrY%3D, PID: 16829524
-
Pak, J. E. et al. X-ray crystal structure of leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism. J. Biol. Chem. 281, 26693–26701 (2006).
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 26693-26701
-
-
Pak, J.E.1
-
34
-
-
82555168211
-
Structural and mechanistic characterization of leukocyte-type core 2 β1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase
-
COI: 1:CAS:528:DC%2BC3MXhsFKls7bN, PID: 22056345
-
Pak, J. E., Satkunarajah, M., Seetharaman, J. & Rini, J. M. Structural and mechanistic characterization of leukocyte-type core 2 β1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase. J. Mol. Biol. 414, 798–811 (2011).
-
(2011)
J. Mol. Biol.
, vol.414
, pp. 798-811
-
-
Pak, J.E.1
Satkunarajah, M.2
Seetharaman, J.3
Rini, J.M.4
-
35
-
-
84883579401
-
The structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycans
-
COI: 1:CAS:528:DC%2BC3sXhtlKrsLnM, PID: 23999306
-
Kuhn, B. et al. The structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycans. Acta Crystallogr. D Biol. Crystallogr. 69, 1826–1838 (2013).
-
(2013)
Acta Crystallogr. D Biol. Crystallogr.
, vol.69
, pp. 1826-1838
-
-
Kuhn, B.1
-
36
-
-
84889053976
-
Enzymatic basis for N-glycan sialylation: structure of rat α2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation
-
COI: 1:CAS:528:DC%2BC3sXhvVKnsbrP, PID: 24155237
-
Meng, L. et al. Enzymatic basis for N-glycan sialylation: structure of rat α2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation. J. Biol. Chem. 288, 34680–34698 (2013).
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 34680-34698
-
-
Meng, L.1
-
37
-
-
70350770831
-
Structural insight into mammalian sialyltransferases
-
COI: 1:CAS:528:DC%2BD1MXht1Cmu7%2FO, PID: 19820709
-
Rao, F. V. et al. Structural insight into mammalian sialyltransferases. Nat. Struct. Mol. Biol. 16, 1186–1188 (2009).
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 1186-1188
-
-
Rao, F.V.1
-
38
-
-
84938750981
-
Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation
-
COI: 1:CAS:528:DC%2BC2MXhtFKrsrbP, PID: 26192331
-
Volkers, G. et al. Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation. Nat. Struct. Mol. Biol. 22, 627–635 (2015).
-
(2015)
Nat. Struct. Mol. Biol.
, vol.22
, pp. 627-635
-
-
Volkers, G.1
-
39
-
-
85045085634
-
Structural basis for the initiation of glycosaminoglycan biosynthesis by human xylosyltransferase 1
-
COI: 1:CAS:528:DC%2BC1cXotFejtbo%3D, PID: 29681470
-
Briggs, D. C. & Hohenester, E. Structural basis for the initiation of glycosaminoglycan biosynthesis by human xylosyltransferase 1. Structure 26, 801–809.e3 (2018).
-
(2018)
Structure
, vol.26
, pp. 801-809
-
-
Briggs, D.C.1
Hohenester, E.2
-
40
-
-
85052108452
-
Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
-
PID: 30140003
-
Nagae, M. et al. Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V. Nat. Commun. 9, 3380 (2018).
-
(2018)
Nat. Commun.
, vol.9
-
-
Nagae, M.1
-
41
-
-
84995376581
-
Structure of Arabidopsis thaliana FUT1 reveals a variant of the GT-B class fold and provides insight into xyloglucan fucosylation
-
COI: 1:CAS:528:DC%2BC2sXktlWmsbs%3D, PID: 27637560
-
Rocha, J. et al. Structure of Arabidopsis thaliana FUT1 reveals a variant of the GT-B class fold and provides insight into xyloglucan fucosylation. Plant Cell 28, 2352–2364 (2016).
-
(2016)
Plant Cell
, vol.28
, pp. 2352-2364
-
-
Rocha, J.1
-
42
-
-
84957678805
-
A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2
-
PID: 26854667
-
Valero-González, J. et al. A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2. Nat. Chem. Biol. 12, 240–246 (2016).
-
(2016)
Nat. Chem. Biol.
, vol.12
, pp. 240-246
-
-
Valero-González, J.1
-
43
-
-
85026726254
-
Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1)
-
COI: 1:CAS:528:DC%2BC28XitVWmsrfF, PID: 28775322
-
Li, Z. et al. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8, 185 (2017).
-
(2017)
Nat. Commun.
, vol.8
-
-
Li, Z.1
-
44
-
-
85047290208
-
Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of α-dystroglycan
-
COI: 1:CAS:528:DC%2BC28Xht1yls7bF, PID: 27493216
-
Kuwabara, N. et al. Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of α-dystroglycan. Proc. Natl Acad. Sci. USA 113, 9280–9285 (2016).
-
(2016)
Proc. Natl Acad. Sci. USA
, vol.113
, pp. 9280-9285
-
-
Kuwabara, N.1
-
45
-
-
2542420721
-
Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1
-
COI: 1:CAS:528:DC%2BD2cXjvF2ruro%3D, PID: 14993226
-
Kakuda, S. et al. Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1. J. Biol. Chem. 279, 22693–22703 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 22693-22703
-
-
Kakuda, S.1
-
46
-
-
0034602394
-
Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I
-
COI: 1:CAS:528:DC%2BD3cXotFWlt7o%3D, PID: 10946001
-
Pedersen, L. C. et al. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J. Biol. Chem. 275, 34580–34585 (2000).
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 34580-34585
-
-
Pedersen, L.C.1
-
47
-
-
44349178127
-
ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes
-
COI: 1:CAS:528:DC%2BD1cXkt1alu70%3D, PID: 18192272
-
Alfaro, J. A. et al. ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes. J. Biol. Chem. 283, 10097–10108 (2008).
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 10097-10108
-
-
Alfaro, J.A.1
-
48
-
-
85048025637
-
Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers
-
COI: 1:CAS:528:DC%2BC1cXhtlygsr3P, PID: 29784804
-
Culbertson, A. T., Ehrlich, J. J., Choe, J. Y., Honzatko, R. B. & Zabotina, O. A. Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers. Proc. Natl Acad. Sci. USA 115, 6064–6069 (2018).
-
(2018)
Proc. Natl Acad. Sci. USA
, vol.115
, pp. 6064-6069
-
-
Culbertson, A.T.1
Ehrlich, J.J.2
Choe, J.Y.3
Honzatko, R.B.4
Zabotina, O.A.5
-
49
-
-
0012784535
-
Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
-
COI: 1:CAS:528:DC%2BD3sXjtVShsbo%3D, PID: 12562774
-
Pedersen, L. C. et al. Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. J. Biol. Chem. 278, 14420–14428 (2003).
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 14420-14428
-
-
Pedersen, L.C.1
-
50
-
-
84870347565
-
Structural snapshots of the reaction coordinate for O-GlcNAc transferase
-
COI: 1:CAS:528:DC%2BC38XhsFOmt7fI, PID: 23103939
-
Lazarus, M. B. et al. Structural snapshots of the reaction coordinate for O-GlcNAc transferase. Nat. Chem. Biol. 8, 966–968 (2012).
-
(2012)
Nat. Chem. Biol.
, vol.8
, pp. 966-968
-
-
Lazarus, M.B.1
-
51
-
-
32244440192
-
Dystroglycan: from biosynthesis to pathogenesis of human disease
-
COI: 1:CAS:528:DC%2BD28Xhs1eit7Y%3D, PID: 16410545
-
Barresi, R. & Campbell, K. P. Dystroglycan: from biosynthesis to pathogenesis of human disease. J. Cell Sci. 119, 199–207 (2006).
-
(2006)
J. Cell Sci.
, vol.119
, pp. 199-207
-
-
Barresi, R.1
Campbell, K.P.2
-
52
-
-
84936755861
-
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane
-
COI: 1:CAS:528:DC%2BC28Xhs1OqurzO, PID: 25882296
-
Yoshida-Moriguchi, T. & Campbell, K. P. Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane. Glycobiology 25, 702–713 (2015).
-
(2015)
Glycobiology
, vol.25
, pp. 702-713
-
-
Yoshida-Moriguchi, T.1
Campbell, K.P.2
-
53
-
-
85031935329
-
Recent advancements in understanding mammalian O-mannosylation
-
COI: 1:CAS:528:DC%2BC1cXhvFentbvF, PID: 28810660
-
Sheikh, M. O., Halmo, S. M. & Wells, L. Recent advancements in understanding mammalian O-mannosylation. Glycobiology 27, 806–819 (2017).
-
(2017)
Glycobiology
, vol.27
, pp. 806-819
-
-
Sheikh, M.O.1
Halmo, S.M.2
Wells, L.3
-
54
-
-
47749085112
-
Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site
-
COI: 1:CAS:528:DC%2BD1cXovVOjtrg%3D, PID: 18599462
-
Shah, N., Kuntz, D. A. & Rose, D. R. Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site. Proc. Natl Acad. Sci. USA 105, 9570–9575 (2008).
-
(2008)
Proc. Natl Acad. Sci. USA
, vol.105
, pp. 9570-9575
-
-
Shah, N.1
Kuntz, D.A.2
Rose, D.R.3
-
55
-
-
85006176207
-
Sialylation of N-glycans: mechanism, cellular compartmentalization and function
-
COI: 1:CAS:528:DC%2BC28XitVylt7fE, PID: 27975143
-
Bhide, G. P. & Colley, K. J. Sialylation of N-glycans: mechanism, cellular compartmentalization and function. Histochem. Cell Biol. 147, 149–174 (2017).
-
(2017)
Histochem. Cell Biol.
, vol.147
, pp. 149-174
-
-
Bhide, G.P.1
Colley, K.J.2
-
56
-
-
77449115880
-
Advances in the biology and chemistry of sialic acids
-
COI: 1:CAS:528:DC%2BC3cXhs1yrsQ%3D%3D, PID: 20020717
-
Chen, X. & Varki, A. Advances in the biology and chemistry of sialic acids. ACS Chem. Biol. 5, 163–176 (2010).
-
(2010)
ACS Chem. Biol.
, vol.5
, pp. 163-176
-
-
Chen, X.1
Varki, A.2
-
57
-
-
77956041687
-
The sialome—far more than the sum of its parts
-
COI: 1:CAS:528:DC%2BC3cXhtlGlt77K, PID: 20726801
-
Cohen, M. & Varki, A. The sialome—far more than the sum of its parts. OMICS 14, 455–464 (2010).
-
(2010)
OMICS
, vol.14
, pp. 455-464
-
-
Cohen, M.1
Varki, A.2
-
58
-
-
84921786419
-
Siglec-mediated regulation of immune cell function in disease
-
COI: 1:CAS:528:DC%2BC2cXhsFOksrrM, PID: 25234143
-
Macauley, M. S., Crocker, P. R. & Paulson, J. C. Siglec-mediated regulation of immune cell function in disease. Nat. Rev. Immunol. 14, 653–666 (2014).
-
(2014)
Nat. Rev. Immunol.
, vol.14
, pp. 653-666
-
-
Macauley, M.S.1
Crocker, P.R.2
Paulson, J.C.3
-
59
-
-
0028985664
-
The sialyltransferase “sialylmotif” participates in binding the donor substrate CMP-NeuAc
-
COI: 1:CAS:528:DyaK2MXjtlWqt7Y%3D, PID: 7829476
-
Datta, A. K. & Paulson, J. C. The sialyltransferase “sialylmotif” participates in binding the donor substrate CMP-NeuAc. J. Biol. Chem. 270, 1497–1500 (1995).
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 1497-1500
-
-
Datta, A.K.1
Paulson, J.C.2
-
60
-
-
25144501600
-
The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach
-
COI: 1:CAS:528:DC%2BD2MXlslyrtr4%3D, PID: 15843597
-
Harduin-Lepers, A., Mollicone, R., Delannoy, P. & Oriol, R. The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach. Glycobiology 15, 805–817 (2005).
-
(2005)
Glycobiology
, vol.15
, pp. 805-817
-
-
Harduin-Lepers, A.1
Mollicone, R.2
Delannoy, P.3
Oriol, R.4
-
61
-
-
0034850831
-
The human sialyltransferase family
-
COI: 1:CAS:528:DC%2BD3MXmt1yhsbY%3D, PID: 11530204
-
Harduin-Lepers, A. et al. The human sialyltransferase family. Biochimie 83, 727–737 (2001).
-
(2001)
Biochimie
, vol.83
, pp. 727-737
-
-
Harduin-Lepers, A.1
-
62
-
-
72249094196
-
Metabolism, cell surface organization, and disease
-
PID: 20064370
-
Dennis, J. W., Nabi, I. R. & Demetriou, M. Metabolism, cell surface organization, and disease. Cell 139, 1229–1241 (2009).
-
(2009)
Cell
, vol.139
, pp. 1229-1241
-
-
Dennis, J.W.1
Nabi, I.R.2
Demetriou, M.3
-
63
-
-
0030754637
-
Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene
-
COI: 1:CAS:528:DyaK2sXltFSgtLs%3D, PID: 9235963
-
Buckhaults, P., Chen, L., Fregien, N. & Pierce, M. Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene. J. Biol. Chem. 272, 19575–19581 (1997).
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 19575-19581
-
-
Buckhaults, P.1
Chen, L.2
Fregien, N.3
Pierce, M.4
-
64
-
-
0029911075
-
Transcriptional regulation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma cells (HuCC-T1) is mediated by Ets-1
-
COI: 1:CAS:528:DyaK28XmsV2rtbk%3D, PID: 8900148
-
Kang, R. et al. Transcriptional regulation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma cells (HuCC-T1) is mediated by Ets-1. J. Biol. Chem. 271, 26706–26712 (1996).
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 26706-26712
-
-
Kang, R.1
-
65
-
-
0027196125
-
Purification and characterization of UDP-N-acetylglucosamine: alpha-6-d-mannoside beta 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line
-
COI: 1:CAS:528:DyaK3sXkvV2lsLw%3D, PID: 8393437
-
Gu, J. et al. Purification and characterization of UDP-N-acetylglucosamine: alpha-6-d-mannoside beta 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. J. Biochem. 113, 614–619 (1993).
-
(1993)
J. Biochem.
, vol.113
, pp. 614-619
-
-
Gu, J.1
-
66
-
-
0026760518
-
Purification and characterization of rat kidney UDP-N-acetylglucosamine: α-6-d-mannoside β-1,6-N-acetylglucosaminyltransferase
-
COI: 1:CAS:528:DyaK38Xhs1yksLc%3D, PID: 1531335
-
Shoreibah, M. G., Hindsgaul, O. & Pierce, M. Purification and characterization of rat kidney UDP-N-acetylglucosamine: α-6-d-mannoside β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 267, 2920–2927 (1992).
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 2920-2927
-
-
Shoreibah, M.G.1
Hindsgaul, O.2
Pierce, M.3
-
67
-
-
79960720473
-
Glycosylation, galectins and cellular signaling
-
COI: 1:CAS:528:DC%2BC3MXps1ejtLs%3D, PID: 21616652
-
Boscher, C., Dennis, J. W. & Nabi, I. R. Glycosylation, galectins and cellular signaling. Curr. Opin. Cell Biol. 23, 383–392 (2011).
-
(2011)
Curr. Opin. Cell Biol.
, vol.23
, pp. 383-392
-
-
Boscher, C.1
Dennis, J.W.2
Nabi, I.R.3
-
68
-
-
33646828699
-
Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2
-
COI: 1:CAS:528:DC%2BD28XivVCnsr4%3D, PID: 16434399
-
Fritz, T. A., Raman, J. & Tabak, L. A. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2. J. Biol. Chem. 281, 8613–8619 (2006).
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 8613-8619
-
-
Fritz, T.A.1
Raman, J.2
Tabak, L.A.3
-
69
-
-
84929208855
-
Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation
-
COI: 1:CAS:528:DC%2BC2MXhtF2lu7%2FL, PID: 25939779
-
Lira-Navarrete, E. et al. Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation. Nat. Commun. 6, 6937 (2015).
-
(2015)
Nat. Commun.
, vol.6
-
-
Lira-Navarrete, E.1
-
70
-
-
85037122538
-
The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences
-
PID: 29208955
-
de Las Rivas, M. et al. The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. Nat. Commun. 8, 1959 (2017).
-
(2017)
Nat. Commun.
, vol.8
-
-
de Las Rivas, M.1
-
71
-
-
84867257213
-
Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeats
-
COI: 1:CAS:528:DC%2BC38XhsVKlsL%2FE, PID: 22872643
-
Takeuchi, H., Kantharia, J., Sethi, M. K., Bakker, H. & Haltiwanger, R. S. Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeats. J. Biol. Chem. 287, 33934–33944 (2012).
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 33934-33944
-
-
Takeuchi, H.1
Kantharia, J.2
Sethi, M.K.3
Bakker, H.4
Haltiwanger, R.S.5
-
72
-
-
33646922955
-
Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats
-
COI: 1:CAS:528:DC%2BD28XjtVSrt70%3D, PID: 16464858
-
Luo, Y., Nita-Lazar, A. & Haltiwanger, R. S. Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats. J. Biol. Chem. 281, 9385–9392 (2006).
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 9385-9392
-
-
Luo, Y.1
Nita-Lazar, A.2
Haltiwanger, R.S.3
-
73
-
-
0032478730
-
Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells
-
COI: 1:CAS:528:DyaK1cXitlOhsbc%3D, PID: 9525914
-
Wang, Y. & Spellman, M. W. Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells. J. Biol. Chem. 273, 8112–8118 (1998).
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 8112-8118
-
-
Wang, Y.1
Spellman, M.W.2
-
74
-
-
85057497162
-
Multiple roles for O-glycans in Notch signalling
-
COI: 1:CAS:528:DC%2BC1cXitlentr7F, PID: 30207383
-
Varshney, S. & Stanley, P. Multiple roles for O-glycans in Notch signalling. FEBS Lett. 592, 3819–3834 (2018).
-
(2018)
FEBS Lett.
, vol.592
, pp. 3819-3834
-
-
Varshney, S.1
Stanley, P.2
-
75
-
-
85051230343
-
Regulation of Notch function by O-glycosylation
-
COI: 1:CAS:528:DC%2BC1MXosFWrtL8%3D, PID: 30030822
-
Harvey, B. M. & Haltiwanger, R. S. Regulation of Notch function by O-glycosylation. Adv. Exp. Med. Biol. 1066, 59–78 (2018).
-
(2018)
Adv. Exp. Med. Biol.
, vol.1066
, pp. 59-78
-
-
Harvey, B.M.1
Haltiwanger, R.S.2
-
76
-
-
85060462431
-
Protein O-fucosylation: structure and function
-
COI: 1:CAS:528:DC%2BC1MXhtFCls74%3D, PID: 30690220
-
Holdener, B. C. & Haltiwanger, R. S. Protein O-fucosylation: structure and function. Curr. Opin. Struct. Biol. 56, 78–86 (2019).
-
(2019)
Curr. Opin. Struct. Biol.
, vol.56
, pp. 78-86
-
-
Holdener, B.C.1
Haltiwanger, R.S.2
-
77
-
-
85060182630
-
Protein O-glucosylation: another essential role of glucose in biology
-
COI: 1:CAS:528:DC%2BC1MXltVeisQ%3D%3D, PID: 30665188
-
Yu, H. & Takeuchi, H. Protein O-glucosylation: another essential role of glucose in biology. Curr. Opin. Struct. Biol. 56, 64–71 (2019).
-
(2019)
Curr. Opin. Struct. Biol.
, vol.56
, pp. 64-71
-
-
Yu, H.1
Takeuchi, H.2
-
78
-
-
85021732344
-
Biological functions of fucose in mammals
-
COI: 1:CAS:528:DC%2BC1cXhvV2nu7vO, PID: 28430973
-
Schneider, M., Al-Shareffi, E. & Haltiwanger, R. S. Biological functions of fucose in mammals. Glycobiology 27, 601–618 (2017).
-
(2017)
Glycobiology
, vol.27
, pp. 601-618
-
-
Schneider, M.1
Al-Shareffi, E.2
Haltiwanger, R.S.3
-
79
-
-
84989300287
-
Genetic and biochemical evidence that gastrulation defects in Pofut2 mutants result from defects in ADAMTS9 secretion
-
COI: 1:CAS:528:DC%2BC28XhtVWnsLrK, PID: 27297885
-
Benz, B. A. et al. Genetic and biochemical evidence that gastrulation defects in Pofut2 mutants result from defects in ADAMTS9 secretion. Dev. Biol. 416, 111–122 (2016).
-
(2016)
Dev. Biol.
, vol.416
, pp. 111-122
-
-
Benz, B.A.1
-
80
-
-
77956161127
-
O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation
-
COI: 1:CAS:528:DC%2BC3cXhtFGgs77O, PID: 20637190
-
Du, J. et al. O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation. Dev. Biol. 346, 25–38 (2010).
-
(2010)
Dev. Biol.
, vol.346
, pp. 25-38
-
-
Du, J.1
-
81
-
-
84978760284
-
Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations
-
COI: 1:CAS:528:DC%2BC28Xht1Kmu7rN, PID: 27428513
-
Yu, H. et al. Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations. Nat. Chem. Biol. 12, 735–740 (2016).
-
(2016)
Nat. Chem. Biol.
, vol.12
, pp. 735-740
-
-
Yu, H.1
-
82
-
-
85029741460
-
O-Glycosylation modulates the stability of epidermal growth factor-like repeats and thereby regulates Notch trafficking
-
COI: 1:CAS:528:DC%2BC2sXhsFeqsLjP, PID: 28729422
-
Takeuchi, H. et al. O-Glycosylation modulates the stability of epidermal growth factor-like repeats and thereby regulates Notch trafficking. J. Biol. Chem. 292, 15964–15973 (2017).
-
(2017)
J. Biol. Chem.
, vol.292
, pp. 15964-15973
-
-
Takeuchi, H.1
-
83
-
-
84922945390
-
Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism
-
COI: 1:CAS:528:DC%2BC2MXkslaltA%3D%3D, PID: 25544610
-
Vasudevan, D., Takeuchi, H., Johar, S. S., Majerus, E. & Haltiwanger, R. S. Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism. Curr. Biol. 25, 286–295 (2015).
-
(2015)
Curr. Biol.
, vol.25
, pp. 286-295
-
-
Vasudevan, D.1
Takeuchi, H.2
Johar, S.S.3
Majerus, E.4
Haltiwanger, R.S.5
-
84
-
-
85051271215
-
A perspective on structural and mechanistic aspects of protein O-fucosylation
-
COI: 1:CAS:528:DC%2BC1cXhsVGisb%2FN, PID: 30084393
-
Lira-Navarrete, E. & Hurtado-Guerrero, R. A perspective on structural and mechanistic aspects of protein O-fucosylation. Acta Crystallogr. F Struct. Biol. Commun. 74, 443–450 (2018).
-
(2018)
Acta Crystallogr. F Struct. Biol. Commun.
, vol.74
, pp. 443-450
-
-
Lira-Navarrete, E.1
Hurtado-Guerrero, R.2
-
85
-
-
85040050034
-
Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation
-
COI: 1:CAS:528:DC%2BC1cXhvVGks7s%3D, PID: 29301962
-
Wild, R. et al. Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. Science 359, 545–550 (2018).
-
(2018)
Science
, vol.359
, pp. 545-550
-
-
Wild, R.1
-
86
-
-
85044246798
-
The atomic structure of a eukaryotic oligosaccharyltransferase complex
-
COI: 1:CAS:528:DC%2BC1cXks12nurg%3D, PID: 29466327
-
Bai, L., Wang, T., Zhao, G., Kovach, A. & Li, H. The atomic structure of a eukaryotic oligosaccharyltransferase complex. Nature 555, 328–333 (2018).
-
(2018)
Nature
, vol.555
, pp. 328-333
-
-
Bai, L.1
Wang, T.2
Zhao, G.3
Kovach, A.4
Li, H.5
-
87
-
-
85044041374
-
Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum
-
COI: 1:CAS:528:DC%2BC1cXnt1GhtLk%3D, PID: 29519914
-
Braunger, K. et al. Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum. Science 360, 215–219 (2018).
-
(2018)
Science
, vol.360
, pp. 215-219
-
-
Braunger, K.1
-
88
-
-
77949535720
-
Features and development of Coot
-
COI: 1:CAS:528:DC%2BC3cXksFKisb8%3D, PID: 2852313
-
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010).
-
(2010)
Acta Crystallogr. D Biol. Crystallogr.
, vol.66
, pp. 486-501
-
-
Emsley, P.1
Lohkamp, B.2
Scott, W.G.3
Cowtan, K.4
-
89
-
-
84871746273
-
Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen
-
PID: 23230506
-
Thiyagarajan, N. et al. Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen. Sci. Rep. 2, 940 (2012).
-
(2012)
Sci. Rep.
, vol.2
-
-
Thiyagarajan, N.1
|