Search

Your search keyword '"Schachter H"' showing total 437 results
Start Over Author "Schachter H"
437 results on '"Schachter H"'

11. Carbohydrate-deficient glycoprotein syndromes become congenital disorders of glycosylation: An updated nomenclature for CDG

Author

Aebi, M., Helenius, A., Schenk, B., Barone, R., Fiumara, A., Berger, E.G., Hennet, T., Imbach, T., Stutz, A., Bjursell, C., Uller, A., Wahlström, J.G., Briones, P., Cardo, E., Clayton, P., Winchester, B., Cormier-Dalre, V., de Lonlay, P., Cuer, M., Dupré, T., Seta, N., de Koning, T., Dorland, L., de Loos, F., Kupers, L., Fabritz, L., Hasilik, M., Marquardt, T., Niehues, R., Freeze, H., Grünewald, S., Heykants, L., Jaeken, J., Matthijs, G., Schollen, E., xKeir, G. Keir, Kjaergaard, S., Schwartz, M., Skovby, F., Klein, A., Roussel, P., Körner, C., Lübke, T., Thiel, C., von Figura, K., Koscielak, J., Krasnewich, D., Lehle, L., Peters, V., Raab, M., Saether, O., Schachter, H., Van Schaftingen, E., Verbert, A., Vilaseca, A., Wevers, R., and Yamashita, K.

Published
1999
Full Text
View/download PDF

12. Preface

Author

Montreuil, J., primary, Vliegenthart, J.F.G., additional, and Schachter, H., additional

Published
1997
Full Text
View/download PDF

13. Preface

Author

Montreuil, J., primary, Vliegenthart, J.F.G., additional, and Schachter, H., additional

Published
1996
Full Text
View/download PDF

22. Regulation of expression of the human beta-1,2-N-acetylglucosaminyltransferase II gene (MGAT2) by Ets transcription factors

Author

Zhang, W, Revers, L, Pierce, M, and Schachter, H

Subjects
Chloramphenicol O-Acetyltransferase, Transcriptional Activation, Binding Sites, Proto-Oncogene Proteins c-ets, Transcription, Genetic, DNA, N-Acetylglucosaminyltransferases, Response Elements, Transfection, Gene Expression Regulation, Enzymologic, Proto-Oncogene Protein c-ets-1, Genes, src, Genes, Reporter, Proto-Oncogene Proteins, COS Cells, Tumor Cells, Cultured, Animals, Humans, RNA, Messenger, Promoter Regions, Genetic, Research Article, Sequence Deletion, Transcription Factors
Abstract

Oncogenic transformation of fibroblasts by the src oncogene has long been known to cause an increase in the size of cell-surface protein-bound oligosaccharides, owing primarily to increased N-glycan branching mediated by increased beta-1,6-N-acetylglucosaminyltransferase V (GnT V) activity. The src-responsive element of the GnT V promoter was localized to Ets-binding sites and the promoter was transcriptionally stimulated by both ets-1 and ets-2 expression [Buckhaults, Chen, Fregien and Pierce (1997) J. Biol. Chem. 272, 19575-19581; Kang, Saito, Ihara, Miyoshi, Koyama, Sheng and Taniguchi (1996) J. Biol. Chem. 271, 26706-26712]. Because GnT V action requires the prior action of beta-1,2-N-acetylglucosaminyltransferase II (GnT II) and the human GnT II promoter contains four putative Ets-binding sites [Chen, Zhou, Tan and Schachter (1998) Glycoconj. J. 15, 301-308], GnT II might also be under oncogenic control via Ets transcription factors. We now report that co-transfection into HepG2 or COS-1 cells of either ets-1 or ets-2 expression plasmids together with chimaeric GnT II promoter-chloramphenicol acetyltransferase plasmids results in a 2-4-fold stimulation of promoter activity. Mobility-shift assays and South-Western blots localized the functional Ets-binding site to one of the four putative sites on the GnT II promoter. The GnT II promoter, unlike the GnT V promoter, is not activated by either src or neu. Therefore although both promoters are stimulated by a member of the Ets family of transcription factors, the functional role of this Ets transcriptional control seems to be different for the two genes.

Published
2000

23. D.I.4 Patient fibroblast functional complementation studies: A valuable tool in the identification of novel Walker–Warburg syndrome disease genes

Author

Willer, T., primary, Lee, H., additional, Lommel, M., additional, Yoshida-Moriguchi, T., additional, Beltran Valero de Bernabe, D., additional, Venzke, D., additional, Cirak, S., additional, Schachter, H., additional, Vajsar, J., additional, Voit, T., additional, Muntoni, F., additional, Strahl, S., additional, Mathews, K.D., additional, Nelson, S.F., additional, Moore, S.A., additional, and Campbell, K.P., additional

Published
2012
Full Text
View/download PDF

24. O-glycosylation in plants

Author

Klis, F.M., Schachter, H., Montreuil, J., Vliegenthart, J.F.G., and SILS (FNWI)

Published
1995

33. Glycoconjugate abnormalities in patients with congenital dyserythropoietic anaemia type I, II and III.

Author

Zdebska, E, Gołaszewska, E, Fabijańska-Mitek, J, Schachter, H, Shalev, H, Tamary, H, Sandström, Herbert, Wahlin, A, Kościelak, J, Zdebska, E, Gołaszewska, E, Fabijańska-Mitek, J, Schachter, H, Shalev, H, Tamary, H, Sandström, Herbert, Wahlin, A, and Kościelak, J

Abstract

Congenital dyserythropoietic anaemia type II (CDA II) is well known for glycosylation abnormalities affecting erythrocyte membrane glycoconjugates that encompass hypoglycosylation of band 3 glycoprotein and accumulation of glycosphingolipids: lactotriaosylceramides, neolactotriaosylceramide and polyglycosylceramides. These abnormalities were not observed in erythrocytes from patients with CDA of either type I or III. Recently, however, we have described a CDA type I patient in Poland with identical, though less pronounced, glycoconjugate abnormalities to those observed in patients with CDA type II. The abnormalities included partial unglycosylation of O-linked glycosylation sites in glycophorin A. These abnormalities are now reported in three Bedouin patients from Israel with CDA type I. In addition, the erythrocyte membranes of these patients exhibited highly increased globotetraosylceramide content. Glycoconjugate abnormalities were also present in erythrocyte membranes from three patients from Northern Sweden with CDA type III but they almost exclusively affected glycosphingolipids. In erythrocytes of all patients examined including one with CDA type II, polyglycosylceramides were significantly hypoglycosylated although, on a molar basis, their contents in erythrocyte membranes were increased. Thus, glycoconjugate abnormalities of varying intensity occur in erythrocyte membranes from all patients with CDA that were investigated.

Published
2001

34. Three level delta modulation

Author

Frank, J, Schachter, H, and Schilling, D. L

Subjects
Communications And Radar
Abstract

The basic concept of three-level delta modulation (TLDM) is to quantize the error signal of a delta modulator into three levels instead of the usual two levels as in ordinary DM. A TLDM system must be able to transmit three different signals, corresponding to three possible states of the quantizer, whereas the ordinary DM system has to transmit only two signals. The problem of transmitting these signals over a noisy channel is examined, where the input signal is band-limited Gaussian noise. Two parameters that can be adjusted to optimize the performance of the system with respect to quantizing noise are considered: step size and quantizer threshold setting. The effect of additive channel noise on the performance of a TLDM system is assessed in terms of baseband transmission, probability of error, FSK and PSK transmission, transmission bandwidth, and baseband pulse transmission. It is concluded that TLDM can provide a 5 to 6 dB improvement in quantizing signal to noise ratio over ordinary DM for band-limited Gaussian signals. This improvement can be achieved without increasing the channel bandwidth and with an increase in system threshold of less than 2 dB.

Published
1975

36. C.P.3.04 Mild POMGnT1 mutations underlie a novel limb girdle muscular dystrophy variant

Author

Godfrey, C., primary, Clement, E., additional, Tan, J., additional, Brockington, M., additional, Torelli, S., additional, Feng, L., additional, Brown, S., additional, Jimenez-Mallebrera, C., additional, Sewry, C., additional, Longman, C., additional, Mein, R., additional, Abbs, S., additional, Vajsar, J., additional, Schachter, H., additional, and Muntoni, F., additional

Published
2007
Full Text
View/download PDF

41. Modeling human congenital disorder of glycosylation type IIa in the mouse: conservation of asparagine-linked glycan-dependent functions in mammalian physiology and insights into disease pathogenesis

Author

Wang, Y., primary, Tan, J., additional, Sutton-Smith, M., additional, Ditto, D., additional, Panico, M., additional, Campbell, R. M., additional, Varki, N. M., additional, Long, J. M., additional, Jaeken, J., additional, Levinson, S. R., additional, Wynshaw-Boris, A., additional, Morris, H. R., additional, Le, D., additional, Dell, A., additional, Schachter, H., additional, and Marth, J. D., additional

Published
2001
Full Text
View/download PDF

46. Editorial

Author

Schachter H and Turner Ga

Subjects
chemistry.chemical_classification, Pathology, medicine.medical_specialty, chemistry, Glycoconjugate, medicine, Cell Biology, Molecular Biology, Biochemistry, Pathological
Published
1995

Catalog

Books, media, physical & digital resources
See catalog results