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Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines.

Cancer cell international

Przybylo M, Hoja-Lukowicz D, Litynska A, Laidler P.
PMID: 12234377
Cancer Cell Int. 2002 Jun 18;2:6. doi: 10.1186/1475-2867-2-6.

BACKGROUND: The aim of the present study was to determine whether stage of invasiveness of bladder cancer cell lines contributes to alterations in glycan pattern of their cadherins.RESULTS: Human non-malignant epithelial cell of ureter HCV29, v-raf transfected HCV29 line...

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Przybylo M, Hoja-Lukowicz D, Litynska A, et al. Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines. Cancer Cell Int. 2002;2:6doi: 10.1186/1475-2867-2-6.
Przybylo, M., Hoja-Lukowicz, D., Litynska, A., & Laidler, P. (2002). Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines. Cancer cell international, 26. https://doi.org/10.1186/1475-2867-2-6
Przybylo, Malgorzata, et al. "Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines." Cancer cell international vol. 2 (2002): 6. doi: https://doi.org/10.1186/1475-2867-2-6
Przybylo M, Hoja-Lukowicz D, Litynska A, Laidler P. Different glycosylation of cadherins from human bladder non-malignant and cancer cell lines. Cancer Cell Int. 2002 Jun 18;2:6. doi: 10.1186/1475-2867-2-6. PMID: 12234377; PMCID: PMC140134.
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Cerebral Glycoprotein Synthesis and Long-term Memory Formation in the Chick (Gallus domesticus) Following Passive Avoidance Training Depends on the Nature of the Aversive Stimulus.

The European journal of neuroscience

Bourne RC, Davies DC, Stewart MG, Csillag A, Cooper M.
PMID: 12106202
Eur J Neurosci. 1991;3(3):243-248. doi: 10.1111/j.1460-9568.1991.tb00086.x.

Chicks that peck a small bright bead coated in a distateful substance can learn in a single trial to subsequently avoid a similar bead. The taste aversant commonly used is methyl anthranilate, which also has a strong pervasive odour....

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Bourne RC, Davies DC, Stewart MG, et al. Cerebral Glycoprotein Synthesis and Long-term Memory Formation in the Chick (Gallus domesticus) Following Passive Avoidance Training Depends on the Nature of the Aversive Stimulus. Eur J Neurosci. 1991;3(3):243-248doi: 10.1111/j.1460-9568.1991.tb00086.x.
Bourne, R. C., Davies, D. C., Stewart, M. G., Csillag, A., & Cooper, M. (1991). Cerebral Glycoprotein Synthesis and Long-term Memory Formation in the Chick (Gallus domesticus) Following Passive Avoidance Training Depends on the Nature of the Aversive Stimulus. The European journal of neuroscience, 3(3), 243-248. https://doi.org/10.1111/j.1460-9568.1991.tb00086.x
Bourne, R. C., et al. "Cerebral Glycoprotein Synthesis and Long-term Memory Formation in the Chick (Gallus domesticus) Following Passive Avoidance Training Depends on the Nature of the Aversive Stimulus." The European journal of neuroscience vol. 3,3 (1991): 243-248. doi: https://doi.org/10.1111/j.1460-9568.1991.tb00086.x
Bourne RC, Davies DC, Stewart MG, Csillag A, Cooper M. Cerebral Glycoprotein Synthesis and Long-term Memory Formation in the Chick (Gallus domesticus) Following Passive Avoidance Training Depends on the Nature of the Aversive Stimulus. Eur J Neurosci. 1991;3(3):243-248. doi: 10.1111/j.1460-9568.1991.tb00086.x. PMID: 12106202.
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Direct quantitative analysis of peptides using matrix assisted laser desorption ionization.

Analytical and bioanalytical chemistry

Gusev AI, Wilkinson WR, Proctor A, Hercules DM.
PMID: 15048433
Anal Bioanal Chem. 1996 Feb;354(4):455-63. doi: 10.1007/s0021663540455.

The protocol and various matrices were examined for quantification of biomolecules in both the low ca. 1200 amu and mid mass 6000-12000 amu ranges using an internal standard. Comparative studies of different matrices of MALDI quantitative analysis showed that...

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Gusev AI, Wilkinson WR, Proctor A, et al. Direct quantitative analysis of peptides using matrix assisted laser desorption ionization. Anal Bioanal Chem. 1996;354(4):455-63doi: 10.1007/s0021663540455.
Gusev, A. I., Wilkinson, W. R., Proctor, A., & Hercules, D. M. (1996). Direct quantitative analysis of peptides using matrix assisted laser desorption ionization. Analytical and bioanalytical chemistry, 354(4), 455-63. https://doi.org/10.1007/s0021663540455
Gusev, A I, et al. "Direct quantitative analysis of peptides using matrix assisted laser desorption ionization." Analytical and bioanalytical chemistry vol. 354,4 (1996): 455-63. doi: https://doi.org/10.1007/s0021663540455
Gusev AI, Wilkinson WR, Proctor A, Hercules DM. Direct quantitative analysis of peptides using matrix assisted laser desorption ionization. Anal Bioanal Chem. 1996 Feb;354(4):455-63. doi: 10.1007/s0021663540455. PMID: 15048433.
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Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures.

Plant biotechnology journal

Bardor M, Loutelier-Bourhis C, Paccalet T, Cosette P, Fitchette AC, Vézina LP, Trépanier S, Dargis M, Lemieux R, Lange C, Faye L, Lerouge P.
PMID: 17134403
Plant Biotechnol J. 2003 Nov;1(6):451-62. doi: 10.1046/j.1467-7652.2003.00041.x.

Structural analysis of the N-glycosylation of alfalfa proteins was investigated in order to evaluate the capacity of this plant to perform this biologically important post-translational modification. We show that, in alfalfa, N-linked glycans are processed into a large variety...

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Bardor M, Loutelier-Bourhis C, Paccalet T, et al. Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures. Plant Biotechnol J. 2003;1(6):451-62doi: 10.1046/j.1467-7652.2003.00041.x.
Bardor, M., Loutelier-Bourhis, C., Paccalet, T., Cosette, P., Fitchette, A. C., Vézina, L. P., Trépanier, S., Dargis, M., Lemieux, R., Lange, C., Faye, L., & Lerouge, P. (2003). Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures. Plant biotechnology journal, 1(6), 451-62. https://doi.org/10.1046/j.1467-7652.2003.00041.x
Bardor, Muriel, et al. "Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures." Plant biotechnology journal vol. 1,6 (2003): 451-62. doi: https://doi.org/10.1046/j.1467-7652.2003.00041.x
Bardor M, Loutelier-Bourhis C, Paccalet T, Cosette P, Fitchette AC, Vézina LP, Trépanier S, Dargis M, Lemieux R, Lange C, Faye L, Lerouge P. Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures. Plant Biotechnol J. 2003 Nov;1(6):451-62. doi: 10.1046/j.1467-7652.2003.00041.x. PMID: 17134403.
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Cell walls of pseudomonas species sensitive to ethylenediaminetetraacetic Acid.

Journal of bacteriology

Wilkinson SG.
PMID: 16559075
J Bacteriol. 1970 Dec;104(3):1035-44. doi: 10.1128/jb.104.3.1035-1044.1970.

Cell walls of 12 pseudomonads considered to be sensitive to ethylenediaminetetraacetic acid (EDTA) were prepared and analyzed. The wall of each species contained protein, peptidoglycan, loosely bound lipid, and lipopolysaccharide. The walls of Pseudomonas stutzeri and P. syncyanea were...

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Wilkinson SG. Cell walls of pseudomonas species sensitive to ethylenediaminetetraacetic Acid. J Bacteriol. 1970;104(3):1035-44doi: 10.1128/jb.104.3.1035-1044.1970.
Wilkinson, S. G. (1970). Cell walls of pseudomonas species sensitive to ethylenediaminetetraacetic Acid. Journal of bacteriology, 104(3), 1035-44. https://doi.org/10.1128/jb.104.3.1035-1044.1970
Wilkinson, S G. "Cell walls of pseudomonas species sensitive to ethylenediaminetetraacetic Acid." Journal of bacteriology vol. 104,3 (1970): 1035-44. doi: https://doi.org/10.1128/jb.104.3.1035-1044.1970
Wilkinson SG. Cell walls of pseudomonas species sensitive to ethylenediaminetetraacetic Acid. J Bacteriol. 1970 Dec;104(3):1035-44. doi: 10.1128/jb.104.3.1035-1044.1970. PMID: 16559075; PMCID: PMC248259.
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A New Lectin from Meadow Saffron (Colchicum automnale).

Plant physiology

Peumans WJ, Allen AK, Cammue BP.
PMID: 16665131
Plant Physiol. 1986 Dec;82(4):1036-9. doi: 10.1104/pp.82.4.1036.

A lectin has been isolated from tubers of the meadow saffron (Colchicum autumnale). It is an octameric protein (M(r) 100,000) composed of 4A- and 4B-subunits of M(r) 15,000 and 10,000, respectively. It is a glycoprotein with 4.4% carbohydrate, the...

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Peumans WJ, Allen AK, Cammue BP. A New Lectin from Meadow Saffron (Colchicum automnale). Plant Physiol. 1986;82(4):1036-9doi: 10.1104/pp.82.4.1036.
Peumans, W. J., Allen, A. K., & Cammue, B. P. (1986). A New Lectin from Meadow Saffron (Colchicum automnale). Plant physiology, 82(4), 1036-9. https://doi.org/10.1104/pp.82.4.1036
Peumans, W J, et al. "A New Lectin from Meadow Saffron (Colchicum automnale)." Plant physiology vol. 82,4 (1986): 1036-9. doi: https://doi.org/10.1104/pp.82.4.1036
Peumans WJ, Allen AK, Cammue BP. A New Lectin from Meadow Saffron (Colchicum automnale). Plant Physiol. 1986 Dec;82(4):1036-9. doi: 10.1104/pp.82.4.1036. PMID: 16665131; PMCID: PMC1056254.
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Changes in biochemical composition of the cell wall of the cotton fiber during development.

Plant physiology

Meinert MC, Delmer DP.
PMID: 16660000
Plant Physiol. 1977 Jun;59(6):1088-97. doi: 10.1104/pp.59.6.1088.

The composition of the cell wall of the cotton fiber (Gossypium hirsutum L. Acala SJ-1) has been studied from the early stages of elongation (5 days postanthesis) through the period of secondary wall formation, using cell walls derived both...

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Meinert MC, Delmer DP. Changes in biochemical composition of the cell wall of the cotton fiber during development. Plant Physiol. 1977;59(6):1088-97doi: 10.1104/pp.59.6.1088.
Meinert, M. C., & Delmer, D. P. (1977). Changes in biochemical composition of the cell wall of the cotton fiber during development. Plant physiology, 59(6), 1088-97. https://doi.org/10.1104/pp.59.6.1088
Meinert, M C, and Delmer, D P. "Changes in biochemical composition of the cell wall of the cotton fiber during development." Plant physiology vol. 59,6 (1977): 1088-97. doi: https://doi.org/10.1104/pp.59.6.1088
Meinert MC, Delmer DP. Changes in biochemical composition of the cell wall of the cotton fiber during development. Plant Physiol. 1977 Jun;59(6):1088-97. doi: 10.1104/pp.59.6.1088. PMID: 16660000; PMCID: PMC542513.
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Tunicamycin inhibits protein glycosylation in suspension cultured soybean cells.

Plant physiology

Hori H, Elbein AD.
PMID: 16661786
Plant Physiol. 1981 May;67(5):882-6. doi: 10.1104/pp.67.5.882.

Soybean cells in suspension culture incorporate [(3)H]mannose into dolichyl-phosphoryl-mannose and into lipid-linked oligosaccharides as well as into extracellular and cell wall macromolecules. Tunicamycin completely inhibited the formation of lipid-linked oligosaccharides at a concentration of 5 to 10 micrograms per...

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Hori H, Elbein AD. Tunicamycin inhibits protein glycosylation in suspension cultured soybean cells. Plant Physiol. 1981;67(5):882-6doi: 10.1104/pp.67.5.882.
Hori, H., & Elbein, A. D. (1981). Tunicamycin inhibits protein glycosylation in suspension cultured soybean cells. Plant physiology, 67(5), 882-6. https://doi.org/10.1104/pp.67.5.882
Hori, H, and Elbein, A D. "Tunicamycin inhibits protein glycosylation in suspension cultured soybean cells." Plant physiology vol. 67,5 (1981): 882-6. doi: https://doi.org/10.1104/pp.67.5.882
Hori H, Elbein AD. Tunicamycin inhibits protein glycosylation in suspension cultured soybean cells. Plant Physiol. 1981 May;67(5):882-6. doi: 10.1104/pp.67.5.882. PMID: 16661786; PMCID: PMC425794.
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Properties of Lectins in the Root and Seed of Lotononis bainesii.

Plant physiology

Law IJ, Strijdom BW.
PMID: 16663508
Plant Physiol. 1984 Apr;74(4):773-8. doi: 10.1104/pp.74.4.773.

A lectin was purified from the root of Lotononis bainesii Baker by affinity chromatography on Sepharose-blood group substance A + H. The molecular weight of the lectin was estimated by gel filtration to be 118,000. Sodium dodecyl sulfate-polyacrylamide gel...

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Law IJ, Strijdom BW. Properties of Lectins in the Root and Seed of Lotononis bainesii. Plant Physiol. 1984;74(4):773-8doi: 10.1104/pp.74.4.773.
Law, I. J., & Strijdom, B. W. (1984). Properties of Lectins in the Root and Seed of Lotononis bainesii. Plant physiology, 74(4), 773-8. https://doi.org/10.1104/pp.74.4.773
Law, I J, and Strijdom, B W. "Properties of Lectins in the Root and Seed of Lotononis bainesii." Plant physiology vol. 74,4 (1984): 773-8. doi: https://doi.org/10.1104/pp.74.4.773
Law IJ, Strijdom BW. Properties of Lectins in the Root and Seed of Lotononis bainesii. Plant Physiol. 1984 Apr;74(4):773-8. doi: 10.1104/pp.74.4.773. PMID: 16663508; PMCID: PMC1066766.
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Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine.

Plant physiology

Hori H, Kaushal GP, Elbein AD.
PMID: 16664119
Plant Physiol. 1985 Mar;77(3):687-94. doi: 10.1104/pp.77.3.687.

Cultures of soybean cells incorporate [5,6-(3)H]-l-fucose into various cellular components including lipids and proteins. The membrane glyco-proteins were digested with pronase to produce glycopeptides, and the glycopeptides were isolated on columns of Biogel P-4. The major fucoselabeled glycopeptide sized...

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Hori H, Kaushal GP, Elbein AD. Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant Physiol. 1985;77(3):687-94doi: 10.1104/pp.77.3.687.
Hori, H., Kaushal, G. P., & Elbein, A. D. (1985). Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant physiology, 77(3), 687-94. https://doi.org/10.1104/pp.77.3.687
Hori, H, et al. "Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine." Plant physiology vol. 77,3 (1985): 687-94. doi: https://doi.org/10.1104/pp.77.3.687
Hori H, Kaushal GP, Elbein AD. Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant Physiol. 1985 Mar;77(3):687-94. doi: 10.1104/pp.77.3.687. PMID: 16664119; PMCID: PMC1064585.
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Structural Analysis of Secreted Root Slime from Maize (Zea mays L.).

Plant physiology

Bacic A, Moody SF, Clarke AE.
PMID: 16664700
Plant Physiol. 1986 Mar;80(3):771-7. doi: 10.1104/pp.80.3.771.

Secreted slime isolated from the incubation medium of Zea mays roots maintained axenically contains fucose, arabinose, xylose, galactose, and glucose as the major monosaccharides. The slime preparation contains low levels (3% weight/weight [w/w]) of uronic acids. Methylation analysis reveals...

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Bacic A, Moody SF, Clarke AE. Structural Analysis of Secreted Root Slime from Maize (Zea mays L.). Plant Physiol. 1986;80(3):771-7doi: 10.1104/pp.80.3.771.
Bacic, A., Moody, S. F., & Clarke, A. E. (1986). Structural Analysis of Secreted Root Slime from Maize (Zea mays L.). Plant physiology, 80(3), 771-7. https://doi.org/10.1104/pp.80.3.771
Bacic, A, et al. "Structural Analysis of Secreted Root Slime from Maize (Zea mays L.)." Plant physiology vol. 80,3 (1986): 771-7. doi: https://doi.org/10.1104/pp.80.3.771
Bacic A, Moody SF, Clarke AE. Structural Analysis of Secreted Root Slime from Maize (Zea mays L.). Plant Physiol. 1986 Mar;80(3):771-7. doi: 10.1104/pp.80.3.771. PMID: 16664700; PMCID: PMC1075198.
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Smallest Sarcoma of the Choroid.

Transactions of the American Ophthalmological Society

Fuchs E.
PMID: 16692228
Trans Am Ophthalmol Soc. 1911;12:787-90.

No abstract available.

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Fuchs E. Smallest Sarcoma of the Choroid. Trans Am Ophthalmol Soc. 1911;12:787-90
Fuchs, E. (1911). Smallest Sarcoma of the Choroid. Transactions of the American Ophthalmological Society, 12787-90.
Fuchs, E. "Smallest Sarcoma of the Choroid." Transactions of the American Ophthalmological Society vol. 12 (1911): 787-90.
Fuchs E. Smallest Sarcoma of the Choroid. Trans Am Ophthalmol Soc. 1911;12:787-90. PMID: 16692228; PMCID: PMC1322783.
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Showing 25 to 36 of 1219 entries