Registro:

Referencias:

• Alfa, C., Fantes, P., Hyams, J., McLeod, M., Wabrik, E., (1993) Experiments with Fission Yeast: a Laboratory Manual, , Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
• Alonso, J.M., Santa-Cecilia, A., Calvo, P., Effect of bromoconduritol on glucosidase II from rat liver. a new kinetic model for the binding and hydrolysis of the substrate (1993) Eur. J. Biochem., 215, pp. 37-42
• D'Alessio, C., Caramelo, J.J., Parodi, A.J., Absence of nucleoside diphosphatase activities in the yeast secretory pathway does not abolish nucleotide sugar-dependent protein glycosylation (2005) J. Biol. Chem., 280, pp. 40417-40427
• D'Alessio, C., Fernández, F., Trombetta, E.S., Parodi, A.J., Genetic evidence for the heterodimeric structure of glucosidase II. the effect of disrupting the subunit-encoding genes on glycoprotein folding (1999) J. Biol. Chem., 274, pp. 25899-25905
• Davila, S., Mutations in SEC63 cause autosomal dominant polycystic liver disease (2004) Nat. Genet., 36, pp. 575-577
• 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 (2005) Mol. Cell., 19, pp. 183-195
• Drenth, J.P., Martina, J.A., Van De Kerkhof, R., Bonifacino, J.S., Jansen, J.B., Polycystic liver disease is a disorder of cotranslational protein processing (2005) Trends Mol. Med., 11, pp. 37-42
• Drenth, J.P., Morsche, R.H., Smink, R., Bonifacino, J.S., Jansen, J.B., Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease (2003) Nat. Genet., 33, pp. 345-347
• Engel, J.C., Parodi, A.J., Trypanosoma cruzi cells undergo an alteration in protein N-glycosylation upon differentiation (1985) J. Biol. Chem., 260, pp. 10105-10110
• Feng, J., Romaniouk, A.V., Samal, S.K., Vijay, I.K., Processing enzyme glucosidase II: Proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland (2004) Glycobiology, 14 (10), pp. 909-921. , DOI 10.1093/glycob/cwh110
• Fernández, F., D'Alessio, C., Fanchiotti, S., Parodi, A.J., A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase (1998) EMBO J., 17, pp. 5877-5886
• Fernandez, F.S., Trombetta, S.E., Hellman, U., Parodi, A.J., Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae (1994) Journal of Biological Chemistry, 269 (48), pp. 30701-30706
• Grinna, L.S., Robbins, P.W., Substrate specificities of rat liver microsomal glucosidases which process glycoproteins (1980) J. Biol. Chem., 255, pp. 2255-2258
• Hoffman, C.S., Winston, F., A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli (1987) Gene., 57, pp. 267-272
• Hoffrogge, R., Beyer, S., Hubner, R., Mikkat, S., Mix, E., Scharf, C., Schmitz, U., Rolfs, A., 2-DE profiling of GDNF overexpression-related proteome changes in differentiating ST14A rat progenitor cells (2007) Proteomics, 7 (1), pp. 33-46. , DOI 10.1002/pmic.200600614
• Jannatipour, M., Callejo, M., Parodi, A.J., Armstrong, J., Rokeach, L.A., Calnexin and BiP interact with acid phosphatase independently of glucose trimming and reglucosylation in Schizosaccharomyces pombe (1998) Biochemistry, 37 (49), pp. 17253-17261. , DOI 10.1021/bi981785c
• Matsuyama, A., ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe (2006) Nat. Biotechnol., 24, pp. 841-847. , correction published in Nat. Biotechnol. (2006). 24, 1033
• Moreno, S., Klar, A., Nurse, P., Molecular genetic analysis of fission yeast Schizosaccharomyces pombe (1991) Methods Enzymol, 194, pp. 795-823
• Munro, S., The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins (2001) Curr. Biol., 11, pp. 499-501
• Munro, S., Pelham, H.R., A C-terminal signal prevents secretion of luminal ER proteins (1987) Cell, 48, pp. 899-907
• Olson, L.J., Hancock, M.K., Dix, D., Kim, J.J., Dahms, N.M., Mutational analysis of the binding site residues of the bovine cation-dependent mannose 6-phosphate receptor (1999) J. Biol. Chem., 274, pp. 36905-36911
• Parodi, A.J., Protein glucosylation and its role in protein folding (2000) Annu. Rev. Biochem., 69, pp. 69-95
• Pelletier, M.F., Marcil, A., Sevigny, G., Jakob, C.A., Tessier, D.C., Chevet, E., Menard, R., Thomas, D.Y., The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo (2000) Glycobiology, 10 (8), pp. 815-827
• 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 (1997) EMBO J., 16, pp. 4302-4310
• Puccia, R., Grondin, B., Herscovics, A., Disruption of the processing alpha-mannosidase gene does not prevent outer chain synthesis in Saccharomyces cerevisiae (1993) Biochem. J., 290, pp. 21-26
• Sambrook, J., Russell, D.W., (2001) Molecular Cloning: a Laboratory Manual, , Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
• Sonnichsen, B., Fullekrug, J., Nguyen Van, P., Diekmann, W., Robinson, D.G., Mieskes, G., Retention and retrieval: Both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum (1994) Journal of Cell Science, 107 (10), pp. 2705-2717
• Soussilane, P., D'Alessio, C., Paccalet, T., Fitchette, A.C., Parodi, A.J., Williamson, R., Plasson, C., Gomord, V., N-glycan trimming by glucosidase II is essential for Arabidopsis development (2009) Glycoconj. J., 26, pp. 597-607
• Sun, G., Zhao, H., Kalyanaraman, B., Dahms, N.M., Identification of residues essential for carbohydrate recognition and cation dependence of the 46-kDa mannose 6-phosphate receptor (2005) Glycobiology, 15 (11), pp. 1136-1149. , DOI 10.1093/glycob/cwi098
• Totani, K., Ihara, Y., Matsuo, I., Ito, Y., Effects of macromolecular crowding on glycoprotein processing enzymes (2008) J. Am. Chem. Soc., 130, pp. 2101-2107
• Treml, K., Meimaroglou, D., Hentges, A., Bause, E., The α- And β-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver (2000) Glycobiology, 10 (5), pp. 493-502
• Trombetta, S.E., Bosch, M., Parodi, A.J., Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes (1989) Biochemistry, 28 (20), pp. 8108-8116
• Trombetta, E.S., Fleming, K.G., Helenius, A., Quaternary and domain structure of glycoprotein processing glucosidase II (2001) Biochemistry, 40, pp. 10717-10722
• Trombetta, E.S., Parodi, A.J., Quality control and protein folding in the secretory pathway (2003) Annu. Rev. Cell. Dev. Biol., 19, pp. 649-676
• Trombetta, E.S., Parodi, A.J., Glycoprotein reglucosylation (2005) Methods, 35, pp. 328-337
• Trombetta, E.S., Simons, J.F., Helenius, A., Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit (1996) J. Biol. Chem., 271, pp. 27509-27516
• Wilkinson, B.M., Purswani, J., Stirling, C.J., Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum (2006) J. Biol. Chem., 10, pp. 6325-6333
• Winzeler, E.A., Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis (1999) Science, 285, pp. 901-906
• Woods, R.J., Pathiaseril, A., Wormald, M.R., Edge, C.J., Dwek, R.A., The high degree of internal flexibility observed for an oligomannose oligosaccharide does not alter the overall topology of the molecule (1998) Eur. J. Biochem., 258, pp. 372-386

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------