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Influence of N-glycans on Expression of Cell Wall Remodeling Related Genes in Paracoccidioides brasiliensis Yeast Cells.

Current genomics

Almeida F, Antoniêto AC, Pessoni AM, Monteiro VN, Alegre-Maller AC, Pigosso LL, Pereira M, Soares CM, Roque-Barreira MC.
PMID: 27226767
Curr Genomics. 2016 Apr;17(2):112-8. doi: 10.2174/1389202917666151116212705.

Paracoccidioidomycosis is the most prevalent systemic mycosis in Latin America. It is caused by the temperature-dependent dimorphic fungus Paracoccidioides brasiliensis. The P. brasiliensis cell wall is a dynamic outer structure, composed of a network of glycoproteins and polysaccharides, such...

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Almeida F, Antoniêto AC, Pessoni AM, et al. Influence of N-glycans on Expression of Cell Wall Remodeling Related Genes in Paracoccidioides brasiliensis Yeast Cells. Curr Genomics. 2016;17(2):112-8doi: 10.2174/1389202917666151116212705.
Almeida, F., Antoniêto, A. C., Pessoni, A. M., Monteiro, V. N., Alegre-Maller, A. C., Pigosso, L. L., Pereira, M., Soares, C. M., & Roque-Barreira, M. C. (2016). Influence of N-glycans on Expression of Cell Wall Remodeling Related Genes in Paracoccidioides brasiliensis Yeast Cells. Current genomics, 17(2), 112-8. https://doi.org/10.2174/1389202917666151116212705
Almeida, Fausto, et al. "Influence of N-glycans on Expression of Cell Wall Remodeling Related Genes in Paracoccidioides brasiliensis Yeast Cells." Current genomics vol. 17,2 (2016): 112-8. doi: https://doi.org/10.2174/1389202917666151116212705
Almeida F, Antoniêto AC, Pessoni AM, Monteiro VN, Alegre-Maller AC, Pigosso LL, Pereira M, Soares CM, Roque-Barreira MC. Influence of N-glycans on Expression of Cell Wall Remodeling Related Genes in Paracoccidioides brasiliensis Yeast Cells. Curr Genomics. 2016 Apr;17(2):112-8. doi: 10.2174/1389202917666151116212705. PMID: 27226767; PMCID: PMC4864839.
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Light dependence of sexual agglutinability in Chlamydomonas eugametos.

Planta

Kooijman R, Elzenga TJ, de Wildt P, Musgrave A, Schuring F, van den Ende H.
PMID: 24232649
Planta. 1986 Nov;169(3):370-8. doi: 10.1007/BF00392133.

The mating activity of mating-type plus gametes of Chlamydomonas eugametos depends on light. Cells lost their ability to agglutinate with mating-type minus gametes after a dark period of 30 min. They regained their agglutinability after 10 min exposure to...

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Kooijman R, Elzenga TJ, de Wildt P, et al. Light dependence of sexual agglutinability in Chlamydomonas eugametos. Planta. 1986;169(3):370-8doi: 10.1007/BF00392133.
Kooijman, R., Elzenga, T. J., de Wildt, P., Musgrave, A., Schuring, F., & van den Ende, H. (1986). Light dependence of sexual agglutinability in Chlamydomonas eugametos. Planta, 169(3), 370-8. https://doi.org/10.1007/BF00392133
Kooijman, R, et al. "Light dependence of sexual agglutinability in Chlamydomonas eugametos." Planta vol. 169,3 (1986): 370-8. doi: https://doi.org/10.1007/BF00392133
Kooijman R, Elzenga TJ, de Wildt P, Musgrave A, Schuring F, van den Ende H. Light dependence of sexual agglutinability in Chlamydomonas eugametos. Planta. 1986 Nov;169(3):370-8. doi: 10.1007/BF00392133. PMID: 24232649.
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Expression, glycosylation and secretion of phaseolin in a baculovirus system.

Plant molecular biology

Bustos MM, Luckow VA, Griffing LR, Summers MD, Hall TC.
PMID: 24277620
Plant Mol Biol. 1988 Nov;10(6):475-88. doi: 10.1007/BF00033603.

In this report, we describe the efficient expression and glycosylation, in insect cells, of β-phaseolin polypeptides (M r 45 and 48 kDa) from Phaseolus vulgaris, by means of a baculovirus expression vector. N-terminal sequence analysis demonstrated that the signal...

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Bustos MM, Luckow VA, Griffing LR, et al. Expression, glycosylation and secretion of phaseolin in a baculovirus system. Plant Mol Biol. 1988;10(6):475-88doi: 10.1007/BF00033603.
Bustos, M. M., Luckow, V. A., Griffing, L. R., Summers, M. D., & Hall, T. C. (1988). Expression, glycosylation and secretion of phaseolin in a baculovirus system. Plant molecular biology, 10(6), 475-88. https://doi.org/10.1007/BF00033603
Bustos, M M, et al. "Expression, glycosylation and secretion of phaseolin in a baculovirus system." Plant molecular biology vol. 10,6 (1988): 475-88. doi: https://doi.org/10.1007/BF00033603
Bustos MM, Luckow VA, Griffing LR, Summers MD, Hall TC. Expression, glycosylation and secretion of phaseolin in a baculovirus system. Plant Mol Biol. 1988 Nov;10(6):475-88. doi: 10.1007/BF00033603. PMID: 24277620.
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IRE1α knockdown rescues tunicamycin-induced developmental defects and apoptosis in Xenopus laevis.

Journal of biomedical research

Yuan L, Yu J, Li X, Feng J, Yin C, Wang X.
PMID: 25050111
J Biomed Res. 2014 Jul;28(4):275-81. doi: 10.7555/JBR.28.20120075. Epub 2014 Mar 15.

Inositol requiring enzyme-1 (IRE1) is highly conserved from yeasts to humans. Upon endoplasmic reticulum (ER) stress, IRE1 activates X-box-binding protein 1 (XBP1) by unconventional splicing of XBP1 mRNA, which activates unfolded protein response (UPR) to restore ER homeostasis. In...

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Yuan L, Yu J, Li X, et al. IRE1α knockdown rescues tunicamycin-induced developmental defects and apoptosis in Xenopus laevis. J Biomed Res. 2014;28(4):275-81doi: 10.7555/JBR.28.20120075.
Yuan, L., Yu, J., Li, X., Feng, J., Yin, C., & Wang, X. (2014). IRE1α knockdown rescues tunicamycin-induced developmental defects and apoptosis in Xenopus laevis. Journal of biomedical research, 28(4), 275-81. https://doi.org/10.7555/JBR.28.20120075
Yuan, Li, et al. "IRE1α knockdown rescues tunicamycin-induced developmental defects and apoptosis in Xenopus laevis." Journal of biomedical research vol. 28,4 (2014): 275-81. doi: https://doi.org/10.7555/JBR.28.20120075
Yuan L, Yu J, Li X, Feng J, Yin C, Wang X. IRE1α knockdown rescues tunicamycin-induced developmental defects and apoptosis in Xenopus laevis. J Biomed Res. 2014 Jul;28(4):275-81. doi: 10.7555/JBR.28.20120075. Epub 2014 Mar 15. PMID: 25050111; PMCID: PMC4102841.
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RETRACTED ARTICLE: TN-2 Ameliorates Tunicamycin-Induced Mitochondria and Endoplasmic Reticulum Stress-Associated Apoptosis in Rat Dorsal Root Ganglion Neurons.

Journal of molecular neuroscience : MN

Deng Q, Xu C, Wang R, Zheng J, Li S, Jin Q, Yang Y.
PMID: 26076740
J Mol Neurosci. 2015 Oct;57(2):314. doi: 10.1007/s12031-015-0599-1. Epub 2015 Jun 16.

No abstract available.

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Deng Q, Xu C, Wang R, et al. RETRACTED ARTICLE: TN-2 Ameliorates Tunicamycin-Induced Mitochondria and Endoplasmic Reticulum Stress-Associated Apoptosis in Rat Dorsal Root Ganglion Neurons. J Mol Neurosci. 2015;57(2):314doi: 10.1007/s12031-015-0599-1.
Deng, Q., Xu, C., Wang, R., Zheng, J., Li, S., Jin, Q., & Yang, Y. (2015). RETRACTED ARTICLE: TN-2 Ameliorates Tunicamycin-Induced Mitochondria and Endoplasmic Reticulum Stress-Associated Apoptosis in Rat Dorsal Root Ganglion Neurons. Journal of molecular neuroscience : MN, 57(2), 314. https://doi.org/10.1007/s12031-015-0599-1
Deng, Qiukui, et al. "RETRACTED ARTICLE: TN-2 Ameliorates Tunicamycin-Induced Mitochondria and Endoplasmic Reticulum Stress-Associated Apoptosis in Rat Dorsal Root Ganglion Neurons." Journal of molecular neuroscience : MN vol. 57,2 (2015): 314. doi: https://doi.org/10.1007/s12031-015-0599-1
Deng Q, Xu C, Wang R, Zheng J, Li S, Jin Q, Yang Y. RETRACTED ARTICLE: TN-2 Ameliorates Tunicamycin-Induced Mitochondria and Endoplasmic Reticulum Stress-Associated Apoptosis in Rat Dorsal Root Ganglion Neurons. J Mol Neurosci. 2015 Oct;57(2):314. doi: 10.1007/s12031-015-0599-1. Epub 2015 Jun 16. PMID: 26076740.
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Exendin-4 Inhibits the Expression of SEPP1 and Fetuin-A via Improvement of Palmitic Acid-Induced Endoplasmic Reticulum Stress by AMPK.

Endocrinology and metabolism (Seoul, Korea)

Lee J, Hong SW, Park SE, Rhee EJ, Park CY, Oh KW, Park SW, Lee WY.
PMID: 26194078
Endocrinol Metab (Seoul). 2015 Jun;30(2):177-84. doi: 10.3803/EnM.2015.30.2.177. Epub 2014 Jul 02.

BACKGROUND: Selenoprotein P (SEPP1) and fetuin-A, both circulating liver-derived glycoproteins, are novel biomarkers for insulin resistance and nonalcoholic fatty liver disease. However, the effect of exendin-4 (Ex-4), a glucagon-like peptide-1 receptor agonist, on the expression of hepatokines, SEPP1, and...

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Lee J, Hong SW, Park SE, et al. Exendin-4 Inhibits the Expression of SEPP1 and Fetuin-A via Improvement of Palmitic Acid-Induced Endoplasmic Reticulum Stress by AMPK. Endocrinol Metab (Seoul). 2014;30(2):177-84doi: 10.3803/EnM.2015.30.2.177.
Lee, J., Hong, S. W., Park, S. E., Rhee, E. J., Park, C. Y., Oh, K. W., Park, S. W., & Lee, W. Y. (2015). Exendin-4 Inhibits the Expression of SEPP1 and Fetuin-A via Improvement of Palmitic Acid-Induced Endoplasmic Reticulum Stress by AMPK. Endocrinology and metabolism (Seoul, Korea), 30(2), 177-84. https://doi.org/10.3803/EnM.2015.30.2.177
Lee, Jinmi, et al. "Exendin-4 Inhibits the Expression of SEPP1 and Fetuin-A via Improvement of Palmitic Acid-Induced Endoplasmic Reticulum Stress by AMPK." Endocrinology and metabolism (Seoul, Korea) vol. 30,2 (2015): 177-84. doi: https://doi.org/10.3803/EnM.2015.30.2.177
Lee J, Hong SW, Park SE, Rhee EJ, Park CY, Oh KW, Park SW, Lee WY. Exendin-4 Inhibits the Expression of SEPP1 and Fetuin-A via Improvement of Palmitic Acid-Induced Endoplasmic Reticulum Stress by AMPK. Endocrinol Metab (Seoul). 2015 Jun;30(2):177-84. doi: 10.3803/EnM.2015.30.2.177. Epub 2014 Jul 02. PMID: 26194078; PMCID: PMC4508262.
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Synthesis of an O-glycosylated cell surface protein induced in yeast by alpha factor.

Proceedings of the National Academy of Sciences of the United States of America

Orlean P, Ammer H, Watzele M, Tanner W.
PMID: 16593749
Proc Natl Acad Sci U S A. 1986 Sep;83(17):6263-6. doi: 10.1073/pnas.83.17.6263.

A number of cell surface glycoproteins can be specifically and completely released from intact cells of Saccharomyces cerevisiae with 0.5% mercaptoethanol. Among these proteins is one with a molecular mass of 22 kDa, which is synthesized only in haploid...

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Orlean P, Ammer H, Watzele M, et al. Synthesis of an O-glycosylated cell surface protein induced in yeast by alpha factor. Proc Natl Acad Sci U S A. 1986;83(17):6263-6doi: 10.1073/pnas.83.17.6263.
Orlean, P., Ammer, H., Watzele, M., & Tanner, W. (1986). Synthesis of an O-glycosylated cell surface protein induced in yeast by alpha factor. Proceedings of the National Academy of Sciences of the United States of America, 83(17), 6263-6. https://doi.org/10.1073/pnas.83.17.6263
Orlean, P, et al. "Synthesis of an O-glycosylated cell surface protein induced in yeast by alpha factor." Proceedings of the National Academy of Sciences of the United States of America vol. 83,17 (1986): 6263-6. doi: https://doi.org/10.1073/pnas.83.17.6263
Orlean P, Ammer H, Watzele M, Tanner W. Synthesis of an O-glycosylated cell surface protein induced in yeast by alpha factor. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6263-6. doi: 10.1073/pnas.83.17.6263. PMID: 16593749; PMCID: PMC386483.
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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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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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Characterization of the oligosaccharides from lipid-linked oligosaccharides of mung bean seedlings.

Plant physiology

Hori H, Elbein AD.
PMID: 16662430
Plant Physiol. 1982 Jul;70(1):12-20. doi: 10.1104/pp.70.1.12.

Lipid-linked oligosaccharides were synthesized with the particulate enzyme preparation from mung bean (Phaseolus aureus) seedlings in the presence of GDP-[(14)C] mannose. The oligosaccharides were released from the lipids by mild acid hydrolysis and purified by several passages on Biogel...

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Hori H, Elbein AD. Characterization of the oligosaccharides from lipid-linked oligosaccharides of mung bean seedlings. Plant Physiol. 1982;70(1):12-20doi: 10.1104/pp.70.1.12.
Hori, H., & Elbein, A. D. (1982). Characterization of the oligosaccharides from lipid-linked oligosaccharides of mung bean seedlings. Plant physiology, 70(1), 12-20. https://doi.org/10.1104/pp.70.1.12
Hori, H, and Elbein, A D. "Characterization of the oligosaccharides from lipid-linked oligosaccharides of mung bean seedlings." Plant physiology vol. 70,1 (1982): 12-20. doi: https://doi.org/10.1104/pp.70.1.12
Hori H, Elbein AD. Characterization of the oligosaccharides from lipid-linked oligosaccharides of mung bean seedlings. Plant Physiol. 1982 Jul;70(1):12-20. doi: 10.1104/pp.70.1.12. PMID: 16662430; PMCID: PMC1067077.
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Glycoproteins in the matrix of glyoxysomes in endosperm of castor bean seedlings.

Plant physiology

González E.
PMID: 16664747
Plant Physiol. 1986 Apr;80(4):950-5. doi: 10.1104/pp.80.4.950.

The matrix of glyoxysomes from endosperm of castor bean (Ricinus communis cv Hale) seedlings has been analyzed for the presence of glycosylated proteins. Glyoxysome preparations were monitored for organelle homogeneity by electron microscopy and enzyme marker activities. Glyoxysomes were...

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González E. Glycoproteins in the matrix of glyoxysomes in endosperm of castor bean seedlings. Plant Physiol. 1986;80(4):950-5doi: 10.1104/pp.80.4.950.
González, E. (1986). Glycoproteins in the matrix of glyoxysomes in endosperm of castor bean seedlings. Plant physiology, 80(4), 950-5. https://doi.org/10.1104/pp.80.4.950
González, E. "Glycoproteins in the matrix of glyoxysomes in endosperm of castor bean seedlings." Plant physiology vol. 80,4 (1986): 950-5. doi: https://doi.org/10.1104/pp.80.4.950
González E. Glycoproteins in the matrix of glyoxysomes in endosperm of castor bean seedlings. Plant Physiol. 1986 Apr;80(4):950-5. doi: 10.1104/pp.80.4.950. PMID: 16664747; PMCID: PMC1075235.
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Combination of tunicamycin with anticancer drugs synergistically enhances their toxicity in multidrug-resistant human ovarian cystadenocarcinoma cells.

Cancer cell international

Hiss DC, Gabriels GA, Folb PI.
PMID: 17439664
Cancer Cell Int. 2007 Apr 18;7:5. doi: 10.1186/1475-2867-7-5.

BACKGROUND: The pharmacologic modulatory effects of the antibiotic, tunicamycin (TM), on multidrug-resistant human UWOV2 ovarian cancer cells are reported. The UWOV2 cell line was derived from a cystadenocarcinoma in a patient refractory to combination chemotherapy with actinomycin D, vincristine...

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Hiss DC, Gabriels GA, Folb PI. Combination of tunicamycin with anticancer drugs synergistically enhances their toxicity in multidrug-resistant human ovarian cystadenocarcinoma cells. Cancer Cell Int. 2007;7:5doi: 10.1186/1475-2867-7-5.
Hiss, D. C., Gabriels, G. A., & Folb, P. I. (2007). Combination of tunicamycin with anticancer drugs synergistically enhances their toxicity in multidrug-resistant human ovarian cystadenocarcinoma cells. Cancer cell international, 75. https://doi.org/10.1186/1475-2867-7-5
Hiss, Donavon C, et al. "Combination of tunicamycin with anticancer drugs synergistically enhances their toxicity in multidrug-resistant human ovarian cystadenocarcinoma cells." Cancer cell international vol. 7 (2007): 5. doi: https://doi.org/10.1186/1475-2867-7-5
Hiss DC, Gabriels GA, Folb PI. Combination of tunicamycin with anticancer drugs synergistically enhances their toxicity in multidrug-resistant human ovarian cystadenocarcinoma cells. Cancer Cell Int. 2007 Apr 18;7:5. doi: 10.1186/1475-2867-7-5. PMID: 17439664; PMCID: PMC1865531.
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Showing 1 to 12 of 348 entries