-
1
-
-
77952563903
-
Selenoproteins-what unique properties can arise with selenocysteine in place of cysteine?
-
Arner ES. 2010. Selenoproteins-what unique properties can arise with selenocysteine in place of cysteine? Exp Cell Res. 316:1296-1303.
-
(2010)
Exp Cell Res
, vol.316
, pp. 1296-1303
-
-
Arner, E.S.1
-
2
-
-
0034010855
-
Two homologues encoding human UDP-glucose: Glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity
-
DOI 10.1021/bi9916473
-
Arnold SM, Fessler LI, Fessler JH, Kaufman RJ. 2000. Two homologues encoding human UDP-glucose: Glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity. Biochemistry. 39:2149-2163. (Pubitemid 30130063)
-
(2000)
Biochemistry
, vol.39
, Issue.9
, pp. 2149-2163
-
-
Arnold, S.M.1
Fessler, L.I.2
Fessler, J.H.3
Kaufman, R.J.4
-
3
-
-
0242321979
-
The noncatalytic portion of human udp-glucose: Glycoprotein glucosyltransferase i confers udp-glucose binding and transferase function to the catalytic domain
-
DOI 10.1074/jbc.M305800200
-
Arnold SM, Kaufman RJ. 2003. The noncatalytic portion of human UDP-glucose: Glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain. J Biol Chem. 278:43320-43328. (Pubitemid 37345953)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.44
, pp. 43320-43328
-
-
Arnold, S.M.1
Kaufman, R.J.2
-
4
-
-
80355143396
-
The two Caenorhabditis elegans UDP-glucose: Glycoprotein glucosyltransferase homologues have distinct biological functions
-
Buzzi LI, Simonetta SH, Parodi AJ, Castro OA. 2011. The two Caenorhabditis elegans UDP-glucose: Glycoprotein glucosyltransferase homologues have distinct biological functions. PLoS One. 6:e27025.
-
(2011)
PLoS One.
, vol.6
-
-
Buzzi, L.I.1
Simonetta, S.H.2
Parodi, A.J.3
Castro, O.A.4
-
5
-
-
0037422614
-
UDP-Glc: Glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
-
DOI 10.1073/pnas.262661199
-
Caramelo JJ, Castro OA, Alonso LG, De Prat-Gay G, Parodi AJ. 2003. UDP-Glc: Glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proc Natl Acad Sci USA. 100:86-91. (Pubitemid 36078034)
-
(2003)
Proceedings of the National Academy of Sciences of the United States of America
, vol.100
, Issue.1
, pp. 86-91
-
-
Caramelo, J.J.1
Castro, O.A.2
Alonso, L.G.3
De Prat-Gay, G.4
Parodi, A.J.5
-
6
-
-
8544242762
-
The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates
-
DOI 10.1074/jbc.M408404200
-
Caramelo JJ, Castro OA, de Prat-Gay G, Parodi AJ. 2004. The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates. J Biol Chem. 279:46280-46285. (Pubitemid 39491623)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.44
, pp. 46280-46285
-
-
Caramelo, J.J.1
Castro, O.A.2
De Prat-Gay, G.3
Parodi, A.J.4
-
7
-
-
77952583769
-
UDP-GlC: Glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control
-
D'Alessio C, Caramelo JJ, Parodi AJ. 2010. UDP-GlC: Glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol. 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
-
8
-
-
0037245727
-
N-linked glycans direct the cotranslational folding pathway of Influenza hemagglutinin
-
DOI 10.1016/S1097-2765(02)00821-3
-
Daniels R, Kurowski B, Johnson AE, Hebert DN. 2003. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell. 11:79-90. (Pubitemid 36126592)
-
(2003)
Molecular Cell
, vol.11
, Issue.1
, pp. 79-90
-
-
Daniels, R.1
Kurowski, B.2
Johnson, A.E.3
Hebert, D.N.4
-
9
-
-
33645635000
-
NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family
-
DOI 10.1074/jbc.M511386200
-
Ferguson AD, Labunskyy VM, Fomenko DE, Arac D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. 2006. NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxinlike family. J Biol Chem. 281:3536-3543. (Pubitemid 43845970)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.6
, pp. 3536-3543
-
-
Ferguson, A.D.1
Labunskyy, V.M.2
Fomenko, D.E.3
Arac, D.4
Chelliah, Y.5
Amezcua, C.A.6
Rizo, J.7
Gladyshev, V.N.8
Deisenhofer, J.9
-
10
-
-
0028150802
-
Purification to homogeneity of UDP-glucose: Glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
-
Fernandez FS, Trombetta SE, Hellman U, Parodi AJ. 1994. Purification to homogeneity of UDP-glucose: Glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme for Saccharomyces cerevisiae. J Biol Chem. 269:30701-30706. (Pubitemid 24376560)
-
(1994)
Journal of Biological Chemistry
, vol.269
, Issue.48
, pp. 30701-30706
-
-
Fernandez, F.S.1
Trombetta, S.E.2
Hellman, U.3
Parodi, A.J.4
-
11
-
-
77952037973
-
Deficiency in the 15-kDa selenoprotein inhibits tumorigenicity and metastasis of colon cancer cells
-
Irons R, Tsuji PA, Carlson BA, Ouyang P, Yoo MH, Xu XM, Hatfield DL, Gladyshev VN, Davis CD. 2010. Deficiency in the 15-kDa selenoprotein inhibits tumorigenicity and metastasis of colon cancer cells. Cancer Prev Res (Phila). 3:630-639.
-
(2010)
Cancer Prev Res (Phila).
, vol.3
, pp. 630-639
-
-
Irons, R.1
Tsuji, P.A.2
Carlson, B.A.3
Ouyang, P.4
Yoo, M.H.5
Xu, X.M.6
Hatfield, D.L.7
Gladyshev, V.N.8
Davis, C.D.9
-
12
-
-
84870050270
-
Reconstructed glycan profile for evaluation of operating status of the endoplasmic reticulum glycoprotein quality control
-
Iwamoto S, Isoyama M, Hirano M, Yamaya K, Ito Y, Matsuo I, Totani K. 2013. Reconstructed glycan profile for evaluation of operating status of the endoplasmic reticulum glycoprotein quality control. Glycobiology. 23:121-131.
-
(2013)
Glycobiology.
, vol.23
, pp. 121-131
-
-
Iwamoto, S.1
Isoyama, M.2
Hirano, M.3
Yamaya, K.4
Ito, Y.5
Matsuo, I.6
Totani, K.7
-
13
-
-
84860802199
-
Chemical synthesis of intentionally misfolded homogeneous glycoprotein: A unique approach for the study of glycoprotein quality control
-
Izumi M, Makimura Y, Dedola S, Seko A, Kanamori A, Sakono M, Ito Y, Kajihara Y. 2012. Chemical synthesis of intentionally misfolded homogeneous glycoprotein: A unique approach for the study of glycoprotein quality control. J Am Chem Soc. 134:7238-7241.
-
(2012)
J Am Chem Soc.
, vol.134
, pp. 7238-7241
-
-
Izumi, M.1
Makimura, Y.2
Dedola, S.3
Seko, A.4
Kanamori, A.5
Sakono, M.6
Ito, Y.7
Kajihara, Y.8
-
14
-
-
80053001930
-
Roles of the 15-kDa selenoprotein (Sep15) in redox homeostasis and cataract development revealed by the analysis of Sep 15 knockout mice
-
Kasaikina MV, Fomenko DE, Labunskyy VM, Lachke SA, Qiu W, Moncaster JA, Zhang J, Wojnarowicz MW, Jr, Natarajan SK, Malinouski M, et al. 2011. Roles of the 15-kDa selenoprotein (Sep15) in redox homeostasis and cataract development revealed by the analysis of Sep 15 knockout mice. J Biol Chem. 286:33203-33212.
-
(2011)
J Biol Chem.
, vol.286
, pp. 33203-33212
-
-
Kasaikina, M.V.1
Fomenko, D.E.2
Labunskyy, V.M.3
Lachke, S.A.4
Qiu, W.5
Moncaster, J.A.6
Zhang, J.7
Wojnarowicz Jr., M.W.8
Natarajan, S.K.9
Malinouski, M.10
-
15
-
-
84880101535
-
Top-down chemoenzymatic approach to a high-mannose-Type glycan library: Synthesis of a common precursor and its enzymatic trimming
-
Koizumi A, Matsuo I, Takatani M, Seko A, Hachisu M, Takeda Y, Ito Y. 2013. Top-down chemoenzymatic approach to a high-mannose-Type glycan library: Synthesis of a common precursor and its enzymatic trimming. Angew Chem Int Ed. 52:7426-7431.
-
(2013)
Angew Chem Int Ed.
, vol.52
, pp. 7426-7431
-
-
Koizumi, A.1
Matsuo, I.2
Takatani, M.3
Seko, A.4
Hachisu, M.5
Takeda, Y.6
Ito, Y.7
-
17
-
-
0035805615
-
Association between the 15-kDa selenoprotein and UDP-glucose: Glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells
-
Korotkov KV, Kumaraswamy E, Zhou Y, Hatfield DL, Gladyshev VN. 2001. Association between the 15-kDa selenoprotein and UDP-glucose: Glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. J Biol Chem. 276:15330-15336.
-
(2001)
J Biol Chem.
, vol.276
, pp. 15330-15336
-
-
Korotkov, K.V.1
Kumaraswamy, E.2
Zhou, Y.3
Hatfield, D.L.4
Gladyshev, V.N.5
-
18
-
-
27844454857
-
A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose: Glycoprotein glucosyltransferase
-
DOI 10.1074/jbc.M508685200
-
Labunskyy VM, Ferguson AD, Fomenko DE, Chelliah Y, Hatfield DL, Gladyshev VN. 2005. A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose: Glycoprotein glucosyltransferase. J Biol Chem. 280:37839-37845. (Pubitemid 41642395)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.45
, 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
-
19
-
-
33847008259
-
The Sep15 protein family: Roles in disulfide bond formation and quality control in the endoplasmic reticulum
-
Labunskyy VM, Hatfield DL, Gladyshev VN. 2007. The Sep15 protein family: Roles in disulfide bond formation and quality control in the endoplasmic reticulum. IUBMB Life. 59:1-5.
-
(2007)
IUBMB Life.
, vol.59
, pp. 1-5
-
-
Labunskyy, V.M.1
Hatfield, D.L.2
Gladyshev, V.N.3
-
20
-
-
69749100361
-
Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses
-
Labunskyy VM, Yoo MH, Hatfield DL, Gladyshev VN. 2009. Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses. Biochemistry. 48:8458-8465.
-
(2009)
Biochemistry.
, vol.48
, pp. 8458-8465
-
-
Labunskyy, V.M.1
Yoo, M.H.2
Hatfield, D.L.3
Gladyshev, V.N.4
-
21
-
-
70349855203
-
Glycoprotein folding, quality control and ER-Associated degradation
-
Lederkremer GZ. 2009. Glycoprotein folding, quality control and ER-Associated degradation. Curr Opin Struct Biol. 19:515-523.
-
(2009)
Curr Opin Struct Biol.
, vol.19
, pp. 515-523
-
-
Lederkremer, G.Z.1
-
22
-
-
33745940580
-
Comprehensive synthesis of ER related high-mannose-Type sugar chains by convergent strategy
-
DOI 10.1016/j.tet.2006.06.045, PII S0040402006009756
-
Matsuo I, Totani K, Tatami A, Ito Y. 2006. Comprehensive synthesis of ER related high-mannose-Type sugar chains by convergent strategy. Tetrahedron. 62:8262-8277. (Pubitemid 44062635)
-
(2006)
Tetrahedron
, vol.62
, Issue.35
, pp. 8262-8277
-
-
Matsuo, I.1
Totani, K.2
Tatami, A.3
Ito, Y.4
-
23
-
-
0037467411
-
Synthesis of monoglucosylated high-mannose-Type dodecasaccharide, a putative ligand for molecular chaperone, calnexin, and calreticurin
-
DOI 10.1021/ja021288q
-
Matsuo I, Wada M, Manabe S, Yamaguchi Y, Otake K, Kato K, Ito Y. 2003. Synthesis of monoglucosylated high-mannose-Type dodecasaccharide, a putative ligand for molecular chaperone, calnexin, and calreticulin. J Am Chem Soc. 125:3402-3403. (Pubitemid 36512394)
-
(2003)
Journal of the American Chemical Society
, vol.125
, Issue.12
, pp. 3402-3403
-
-
Matsuo, I.1
Wada, M.2
Manabe, S.3
Yamaguchi, Y.4
Otake, K.5
Kato, K.6
Ito, Y.7
-
24
-
-
84886822755
-
Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT)
-
Prados MB, Caramelo JJ, Miranda SE. 2013. Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: Glycoprotein glucosyltransferase (UGGT). Biochim Biophys Acta. 1833:3368-3374.
-
(2013)
Biochim Biophys Acta.
, vol.1833
, pp. 3368-3374
-
-
Prados, M.B.1
Caramelo, J.J.2
Miranda, S.E.3
-
25
-
-
58249093866
-
Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
-
Ruiz-Canada C, Kelleher DJ, Gilmore R. 2009. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell. 136:272-283.
-
(2009)
Cell.
, vol.136
, pp. 272-283
-
-
Ruiz-Canada, C.1
Kelleher, D.J.2
Gilmore, R.3
-
26
-
-
84867194041
-
Biophysical properties of UDP-glucose: Glycoprotein glucosyltransferase, a folding sensor enzyme in the ER, delineated by synthetic probes
-
Sakono M, Seko A, Takeda Y, Hachisu M, Ito Y. 2012. Biophysical properties of UDP-glucose: Glycoprotein glucosyltransferase, a folding sensor enzyme in the ER, delineated by synthetic probes. Biochem Biophys Res Commun. 426:504-510.
-
(2012)
Biochem Biophys Res Commun.
, vol.426
, pp. 504-510
-
-
Sakono, M.1
Seko, A.2
Takeda, Y.3
Hachisu, M.4
Ito, Y.5
-
27
-
-
84865144708
-
Selenium, selenoproteins and the thyroid gland: Interactions in health and disease
-
Schomburg L. 2012. Selenium, selenoproteins and the thyroid gland: Interactions in health and disease. Nat Rev Endocrinol. 8:160-171.
-
(2012)
Nat Rev Endocrinol.
, vol.8
, pp. 160-171
-
-
Schomburg, L.1
-
28
-
-
0031832906
-
Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-Anilino-1-naphthalene sulfonate (ANS)
-
DOI 10.1016/S0167-4838(98)00038-7, PII S0167483898000387
-
Sirangelo I, Bismuto E, Tavassi S, Irace G. 1998. Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-Anilino-1-naphthalene sulfonate. Biochim Biophys Acta. 1385:69-77. (Pubitemid 28277046)
-
(1998)
Biochimica et Biophysica Acta-Protein Structure and Molecular Enzymology
, vol.1385
, Issue.1
, pp. 69-77
-
-
Sirangelo, I.1
Bismuto, E.2
Tavassi, S.3
Irace, G.4
-
29
-
-
0029126624
-
The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc: Glycoprotein glucosyltransferase
-
Sousa M, Parodi AJ. 1995. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc: Glycoprotein glucosyltransferase. EMBO J. 14:4196-4203.
-
(1995)
EMBO J.
, vol.14
, pp. 4196-4203
-
-
Sousa, M.1
Parodi, A.J.2
-
30
-
-
25844518421
-
Synthetic substrates for an endoplasmic reticulum protein-folding sensor, UDP-glucose: Glycoprotein glucosyltransferase
-
DOI 10.1002/anie.200502723
-
Totani K, Ihara Y, Matsuo I, Koshino H, Ito Y. 2005. Synthetic substrates for an endoplasmic reticulum protein-folding sensor, UDP-glucose: Glycoprotein glucosyltransferase. Angew Chem Int Ed Engl. 44:7950-7954. (Pubitemid 41811716)
-
(2005)
Angewandte Chemie-International Edition
, vol.44
, Issue.48
, pp. 7950-7954
-
-
Totani, K.1
Ihara, Y.2
Matsuo, I.3
Koshino, H.4
Ito, Y.5
-
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. 2009. The recognition motif of the glycoprotein-folding sensor enzyme UDP-Glc: Glycoprotein glucosyltransferase. Biochemistry. 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
-
-
0024468302
-
Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes
-
Trombetta SE, Bosch M, Parodi AJ. 1989. Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes. Biochemistry. 28:8108-8116. (Pubitemid 19252890)
-
(1989)
Biochemistry
, vol.28
, Issue.20
, pp. 8108-8116
-
-
Trombetta, S.E.1
Bosch, M.2
Parodi, A.J.3
-
33
-
-
0029983258
-
A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain
-
DOI 10.1074/jbc.271.11.6241
-
Whitley P, Nilsson IM, von Heijne G. 1996. A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain. J Biol Chem. 271:6241-6244. (Pubitemid 26095431)
-
(1996)
Journal of Biological Chemistry
, vol.271
, Issue.11
, pp. 6241-6244
-
-
Whitley, P.1
Nilsson, I.2
Von Heijne, G.3
-
34
-
-
0032513212
-
Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
-
DOI 10.1074/jbc.273.11.6009
-
Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY. 1998. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem. 273:6009-6012. (Pubitemid 28144676)
-
(1998)
Journal of Biological Chemistry
, vol.273
, Issue.11
, pp. 6009-6012
-
-
Zapun, A.1
Darby, N.J.2
Tessier, D.C.3
Michalak, M.4
Bergeron, J.J.M.5
Thomas, D.Y.6
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