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N-acetylcysteine and the human serum components that inhibit bacterial invasion of gingival epithelial cells prevent experimental periodontitis in mice.

Journal of periodontal & implant science

Alam J, Baek KJ, Choi YS, Kim YC, Choi Y.
PMID: 25568806
J Periodontal Implant Sci. 2014 Dec;44(6):266-73. doi: 10.5051/jpis.2014.44.6.266. Epub 2014 Dec 31.

PURPOSE: We previously reported that human serum significantly reduces the invasion of various oral bacterial species into gingival epithelial cells in vitro. The aims of the present study were to characterize the serum component(s) responsible for the inhibition of...

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Alam J, Baek KJ, Choi YS, et al. N-acetylcysteine and the human serum components that inhibit bacterial invasion of gingival epithelial cells prevent experimental periodontitis in mice. J Periodontal Implant Sci. 2014;44(6):266-73doi: 10.5051/jpis.2014.44.6.266.
Alam, J., Baek, K. J., Choi, Y. S., Kim, Y. C., & Choi, Y. (2014). N-acetylcysteine and the human serum components that inhibit bacterial invasion of gingival epithelial cells prevent experimental periodontitis in mice. Journal of periodontal & implant science, 44(6), 266-73. https://doi.org/10.5051/jpis.2014.44.6.266
Alam, Jehan, et al. "N-acetylcysteine and the human serum components that inhibit bacterial invasion of gingival epithelial cells prevent experimental periodontitis in mice." Journal of periodontal & implant science vol. 44,6 (2014): 266-73. doi: https://doi.org/10.5051/jpis.2014.44.6.266
Alam J, Baek KJ, Choi YS, Kim YC, Choi Y. N-acetylcysteine and the human serum components that inhibit bacterial invasion of gingival epithelial cells prevent experimental periodontitis in mice. J Periodontal Implant Sci. 2014 Dec;44(6):266-73. doi: 10.5051/jpis.2014.44.6.266. Epub 2014 Dec 31. PMID: 25568806; PMCID: PMC4284374.
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Comparative binding affinities of flavonoid phytochemicals with bovine serum albumin.

Iranian journal of pharmaceutical research : IJPR

Liu S, Guo C, Guo Y, Yu H, Greenaway F, Sun MZ.
PMID: 25276204
Iran J Pharm Res. 2014;13(3):1019-28.

Dietary flavonoids show beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is poor, probably due to their interaction with serum albumins. In the current work, the binding interactions of eight related flavonoids, sharing a similar core...

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Liu S, Guo C, Guo Y, et al. Comparative binding affinities of flavonoid phytochemicals with bovine serum albumin. Iran J Pharm Res. 2014;13(3):1019-28
Liu, S., Guo, C., Guo, Y., Yu, H., Greenaway, F., & Sun, M. Z. (2014). Comparative binding affinities of flavonoid phytochemicals with bovine serum albumin. Iranian journal of pharmaceutical research : IJPR, 13(3), 1019-28.
Liu, Shuqing, et al. "Comparative binding affinities of flavonoid phytochemicals with bovine serum albumin." Iranian journal of pharmaceutical research : IJPR vol. 13,3 (2014): 1019-28.
Liu S, Guo C, Guo Y, Yu H, Greenaway F, Sun MZ. Comparative binding affinities of flavonoid phytochemicals with bovine serum albumin. Iran J Pharm Res. 2014;13(3):1019-28. PMID: 25276204; PMCID: PMC4177624.
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Clinical and laboratory determinants of low serum level of 25-hydroxyvitamin D during escalation of pharmacotherapy in heart failure patients.

Kardiochirurgia i torakochirurgia polska = Polish journal of cardio-thoracic surgery

Myrda K, Rozentryt P, Niedziela JT, Ociessa A, Kasperova M, Hudzik B, Nowak JU, Gąsior M.
PMID: 26702277
Kardiochir Torakochirurgia Pol. 2015 Sep;12(3):216-27. doi: 10.5114/kitp.2015.54457. Epub 2015 Sep 28.

INTRODUCTION: The activation of the renin-angiotensin-aldosterone (RAA) system is a main element of the pathophysiology of chronic heart failure (CHF), determining its symptoms and prognosis. Vitamin D is an RAA inhibitor, and its deficiency frequently accompanies CHF. The factors...

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Myrda K, Rozentryt P, Niedziela JT, et al. Clinical and laboratory determinants of low serum level of 25-hydroxyvitamin D during escalation of pharmacotherapy in heart failure patients. Kardiochir Torakochirurgia Pol. 2015;12(3):216-27doi: 10.5114/kitp.2015.54457.
Myrda, K., Rozentryt, P., Niedziela, J. T., Ociessa, A., Kasperova, M., Hudzik, B., Nowak, J. U., & Gąsior, M. (2015). Clinical and laboratory determinants of low serum level of 25-hydroxyvitamin D during escalation of pharmacotherapy in heart failure patients. Kardiochirurgia i torakochirurgia polska = Polish journal of cardio-thoracic surgery, 12(3), 216-27. https://doi.org/10.5114/kitp.2015.54457
Myrda, Krzysztof, et al. "Clinical and laboratory determinants of low serum level of 25-hydroxyvitamin D during escalation of pharmacotherapy in heart failure patients." Kardiochirurgia i torakochirurgia polska = Polish journal of cardio-thoracic surgery vol. 12,3 (2015): 216-27. doi: https://doi.org/10.5114/kitp.2015.54457
Myrda K, Rozentryt P, Niedziela JT, Ociessa A, Kasperova M, Hudzik B, Nowak JU, Gąsior M. Clinical and laboratory determinants of low serum level of 25-hydroxyvitamin D during escalation of pharmacotherapy in heart failure patients. Kardiochir Torakochirurgia Pol. 2015 Sep;12(3):216-27. doi: 10.5114/kitp.2015.54457. Epub 2015 Sep 28. PMID: 26702277; PMCID: PMC4631913.
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Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures.

Frontiers in chemistry

Miranda ÉG, Tofanello A, Brito AM, Lopes DM, Albuquerque LJ, de Castro CE, Costa FN, Giacomelli FC, Ferreira FF, Araújo-Chaves JC, Nantes IL.
PMID: 27066476
Front Chem. 2016 Mar 31;4:13. doi: 10.3389/fchem.2016.00013. eCollection 2016.

The present study aimed to investigate the influence of albumin structure and gold speciation on the synthesis of gold nanoparticles (GNPs). The strategy of synthesis was the addition of HAuCl4 solutions at different pH values (3-12) to solutions of...

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Miranda ÉG, Tofanello A, Brito AM, et al. Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures. Front Chem. 2016;4:13doi: 10.3389/fchem.2016.00013.
Miranda, �. �. G., Tofanello, A., Brito, A. M., Lopes, D. M., Albuquerque, L. J., de Castro, C. E., Costa, F. N., Giacomelli, F. C., Ferreira, F. F., Araújo-Chaves, J. C., & Nantes, I. L. (2016). Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures. Frontiers in chemistry, 413. https://doi.org/10.3389/fchem.2016.00013
Miranda, Érica G A, et al. "Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures." Frontiers in chemistry vol. 4 (2016): 13. doi: https://doi.org/10.3389/fchem.2016.00013
Miranda ÉG, Tofanello A, Brito AM, Lopes DM, Albuquerque LJ, de Castro CE, Costa FN, Giacomelli FC, Ferreira FF, Araújo-Chaves JC, Nantes IL. Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures. Front Chem. 2016 Mar 31;4:13. doi: 10.3389/fchem.2016.00013. eCollection 2016. PMID: 27066476; PMCID: PMC4814711.
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A MOLECULAR PHYLOGENY OF THE FELIDAE: IMMUNOLOGICAL DISTANCE.

Evolution; international journal of organic evolution

Collier GE, O'Brien SJ.
PMID: 28561961
Evolution. 1985 May;39(3):473-487. doi: 10.1111/j.1558-5646.1985.tb00389.x.

The phylogenetic distances between 34 of the 37 extant species of Felidae were estimated using albumin immunological distances (AID). Albumins from ten cat species were used to prepare antisera in rabbits. A consensus phylogeny was constructed from a matrix...

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Collier GE, O'Brien SJ. A MOLECULAR PHYLOGENY OF THE FELIDAE: IMMUNOLOGICAL DISTANCE. Evolution. 1985;39(3):473-487doi: 10.1111/j.1558-5646.1985.tb00389.x.
Collier, G. E., & O'Brien, S. J. (1985). A MOLECULAR PHYLOGENY OF THE FELIDAE: IMMUNOLOGICAL DISTANCE. Evolution; international journal of organic evolution, 39(3), 473-487. https://doi.org/10.1111/j.1558-5646.1985.tb00389.x
Collier, Glen E, and O'Brien, Stephen J. "A MOLECULAR PHYLOGENY OF THE FELIDAE: IMMUNOLOGICAL DISTANCE." Evolution; international journal of organic evolution vol. 39,3 (1985): 473-487. doi: https://doi.org/10.1111/j.1558-5646.1985.tb00389.x
Collier GE, O'Brien SJ. A MOLECULAR PHYLOGENY OF THE FELIDAE: IMMUNOLOGICAL DISTANCE. Evolution. 1985 May;39(3):473-487. doi: 10.1111/j.1558-5646.1985.tb00389.x. PMID: 28561961.
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Sensitization to secretoglobin and lipocalins in a group of young children with risk of developing respiratory allergy.

Clinical and molecular allergy : CMA

Nagao M, Borres MP, Sugimoto M, Petersson CJ, Nakayama S, Kuwabara Y, Masuda S, Dykiel P, Fujisawa T.
PMID: 28270741
Clin Mol Allergy. 2017 Mar 03;15:4. doi: 10.1186/s12948-017-0061-8. eCollection 2017.

BACKGROUND: Multiple sensitizations in early age have been reported to be a risk for development of asthma. This study evaluates the emergence and evolution of IgE to aeroallergens among a cohort of children with physician-diagnosed atopic dermatitis and/or showing...

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Nagao M, Borres MP, Sugimoto M, et al. Sensitization to secretoglobin and lipocalins in a group of young children with risk of developing respiratory allergy. Clin Mol Allergy. 2017;15:4doi: 10.1186/s12948-017-0061-8.
Nagao, M., Borres, M. P., Sugimoto, M., Petersson, C. J., Nakayama, S., Kuwabara, Y., Masuda, S., Dykiel, P., & Fujisawa, T. (2017). Sensitization to secretoglobin and lipocalins in a group of young children with risk of developing respiratory allergy. Clinical and molecular allergy : CMA, 154. https://doi.org/10.1186/s12948-017-0061-8
Nagao, Mizuho, et al. "Sensitization to secretoglobin and lipocalins in a group of young children with risk of developing respiratory allergy." Clinical and molecular allergy : CMA vol. 15 (2017): 4. doi: https://doi.org/10.1186/s12948-017-0061-8
Nagao M, Borres MP, Sugimoto M, Petersson CJ, Nakayama S, Kuwabara Y, Masuda S, Dykiel P, Fujisawa T. Sensitization to secretoglobin and lipocalins in a group of young children with risk of developing respiratory allergy. Clin Mol Allergy. 2017 Mar 03;15:4. doi: 10.1186/s12948-017-0061-8. eCollection 2017. PMID: 28270741; PMCID: PMC5335719.
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Heat stress during seed filling interferes with sulfur restriction on grain composition and seed germination in oilseed rape (Brassica napus L.).

Frontiers in plant science

Brunel-Muguet S, D'Hooghe P, Bataillé MP, Larré C, Kim TH, Trouverie J, Avice JC, Etienne P, Dürr C.
PMID: 25914702
Front Plant Sci. 2015 Apr 10;6:213. doi: 10.3389/fpls.2015.00213. eCollection 2015.

In coming decades, increasing temperatures are expected to impact crop yield and seed quality. To develop low input systems, the effects of temperature and sulfur (S) nutrition in oilseed rape, a high S demanding crop, need to be jointly...

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Brunel-Muguet S, D'Hooghe P, Bataillé MP, et al. Heat stress during seed filling interferes with sulfur restriction on grain composition and seed germination in oilseed rape (Brassica napus L.). Front Plant Sci. 2015;6:213doi: 10.3389/fpls.2015.00213.
Brunel-Muguet, S., D'Hooghe, P., Bataillé, M. P., Larré, C., Kim, T. H., Trouverie, J., Avice, J. C., Etienne, P., & Dürr, C. (2015). Heat stress during seed filling interferes with sulfur restriction on grain composition and seed germination in oilseed rape (Brassica napus L.). Frontiers in plant science, 6213. https://doi.org/10.3389/fpls.2015.00213
Brunel-Muguet, Sophie, et al. "Heat stress during seed filling interferes with sulfur restriction on grain composition and seed germination in oilseed rape (Brassica napus L.)." Frontiers in plant science vol. 6 (2015): 213. doi: https://doi.org/10.3389/fpls.2015.00213
Brunel-Muguet S, D'Hooghe P, Bataillé MP, Larré C, Kim TH, Trouverie J, Avice JC, Etienne P, Dürr C. Heat stress during seed filling interferes with sulfur restriction on grain composition and seed germination in oilseed rape (Brassica napus L.). Front Plant Sci. 2015 Apr 10;6:213. doi: 10.3389/fpls.2015.00213. eCollection 2015. PMID: 25914702; PMCID: PMC4392296.
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[First Results in the prevaluation of the human whole blood assay for pyrogens in biological pharmaceuticals].

ALTEX

Fischer M, Hartzsch K, Hartung T, Montag-Lessing T.
PMID: 11178527
ALTEX. 1998;15(5):10-13.

When establishing the whole blood assay for pyrogens in our laboratory we did several investigations on the standard pyrogen to be used. Because of the hydrophobicity of the lipopolysaccharid (LPS) it is difficult to get a homogeneous solution. Therefore...

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Fischer M, Hartzsch K, Hartung T, et al. Erste Erfahrungen bei der Prävalidierung des Vollblutpyrogentests für biologische Arzneimittel. [First Results in the prevaluation of the human whole blood assay for pyrogens in biological pharmaceuticals]. ALTEX. 1998;15(5):10-13
Fischer, M., Hartzsch, K., Hartung, T., & Montag-Lessing, T. (1998). Erste Erfahrungen bei der Prävalidierung des Vollblutpyrogentests für biologische Arzneimittel. [First Results in the prevaluation of the human whole blood assay for pyrogens in biological pharmaceuticals]. ALTEX, 15(5), 10-13.
Fischer, Matthias, et al. "Erste Erfahrungen bei der Prävalidierung des Vollblutpyrogentests für biologische Arzneimittel." [First Results in the prevaluation of the human whole blood assay for pyrogens in biological pharmaceuticals]. ALTEX vol. 15,5 (1998): 10-13.
Fischer M, Hartzsch K, Hartung T, Montag-Lessing T. Erste Erfahrungen bei der Prävalidierung des Vollblutpyrogentests für biologische Arzneimittel. [First Results in the prevaluation of the human whole blood assay for pyrogens in biological pharmaceuticals]. ALTEX. 1998;15(5):10-13. PMID: 11178527.
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Protein Synthesis in Cotyledons of Pisum sativum L: I. Changes in Cell-Free Amino Acid Incorporation Capacity during Seed Development and Maturation.

Plant physiology

Beevers L, Poulson R.
PMID: 16657987
Plant Physiol. 1972 Apr;49(4):476-81. doi: 10.1104/pp.49.4.476.

The changes in protein content of pea cotyledons have been followed during the period from 9 to 33 days after flowering. Initially protein content increased gradually with a rapid period of deposition occurring between days 21 and 27 after...

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Beevers L, Poulson R. Protein Synthesis in Cotyledons of Pisum sativum L: I. Changes in Cell-Free Amino Acid Incorporation Capacity during Seed Development and Maturation. Plant Physiol. 1972;49(4):476-81doi: 10.1104/pp.49.4.476.
Beevers, L., & Poulson, R. (1972). Protein Synthesis in Cotyledons of Pisum sativum L: I. Changes in Cell-Free Amino Acid Incorporation Capacity during Seed Development and Maturation. Plant physiology, 49(4), 476-81. https://doi.org/10.1104/pp.49.4.476
Beevers, L, and Poulson, R. "Protein Synthesis in Cotyledons of Pisum sativum L: I. Changes in Cell-Free Amino Acid Incorporation Capacity during Seed Development and Maturation." Plant physiology vol. 49,4 (1972): 476-81. doi: https://doi.org/10.1104/pp.49.4.476
Beevers L, Poulson R. Protein Synthesis in Cotyledons of Pisum sativum L: I. Changes in Cell-Free Amino Acid Incorporation Capacity during Seed Development and Maturation. Plant Physiol. 1972 Apr;49(4):476-81. doi: 10.1104/pp.49.4.476. PMID: 16657987; PMCID: PMC365991.
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Albumin storage proteins in the protein bodies of castor bean.

Plant physiology

Youle RJ, Huang AH.
PMID: 16660226
Plant Physiol. 1978 Jan;61(1):13-6. doi: 10.1104/pp.61.1.13.

Of the total protein in the protein bodies of castor bean (Ricinus communis L.), approximately 40% is represented by a group of closely related albumins localized in the matrix of the organelle. This group of albumins has a sedimentation...

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Youle RJ, Huang AH. Albumin storage proteins in the protein bodies of castor bean. Plant Physiol. 1978;61(1):13-6doi: 10.1104/pp.61.1.13.
Youle, R. J., & Huang, A. H. (1978). Albumin storage proteins in the protein bodies of castor bean. Plant physiology, 61(1), 13-6. https://doi.org/10.1104/pp.61.1.13
Youle, R J, and Huang, A H. "Albumin storage proteins in the protein bodies of castor bean." Plant physiology vol. 61,1 (1978): 13-6. doi: https://doi.org/10.1104/pp.61.1.13
Youle RJ, Huang AH. Albumin storage proteins in the protein bodies of castor bean. Plant Physiol. 1978 Jan;61(1):13-6. doi: 10.1104/pp.61.1.13. PMID: 16660226; PMCID: PMC1091786.
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Protein Bodies from the Endosperm of Castor Bean: Subfractionation, Protein Components, Lectins, and Changes during Germination.

Plant physiology

Youle RJ, Huang AH.
PMID: 16659749
Plant Physiol. 1976 Dec;58(6):703-9. doi: 10.1104/pp.58.6.703.

Protein bodies from the storage endosperm of dry castor bean (Ricinus communis L.) were isolated by successive nonaqueous linear density gradient centrifugation. The isolated protein bodies were lysed by the addition of water, and the various structural components of...

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Youle RJ, Huang AH. Protein Bodies from the Endosperm of Castor Bean: Subfractionation, Protein Components, Lectins, and Changes during Germination. Plant Physiol. 1976;58(6):703-9doi: 10.1104/pp.58.6.703.
Youle, R. J., & Huang, A. H. (1976). Protein Bodies from the Endosperm of Castor Bean: Subfractionation, Protein Components, Lectins, and Changes during Germination. Plant physiology, 58(6), 703-9. https://doi.org/10.1104/pp.58.6.703
Youle, R J, and Huang, A H. "Protein Bodies from the Endosperm of Castor Bean: Subfractionation, Protein Components, Lectins, and Changes during Germination." Plant physiology vol. 58,6 (1976): 703-9. doi: https://doi.org/10.1104/pp.58.6.703
Youle RJ, Huang AH. Protein Bodies from the Endosperm of Castor Bean: Subfractionation, Protein Components, Lectins, and Changes during Germination. Plant Physiol. 1976 Dec;58(6):703-9. doi: 10.1104/pp.58.6.703. PMID: 16659749; PMCID: PMC542291.
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Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family.

Plant physiology

Krebbers E, Herdies L, De Clercq A, Seurinck J, Leemans J, Van Damme J, Segura M, Gheysen G, Van Montagu M, Vandekerckhove J.
PMID: 16666238
Plant Physiol. 1988 Aug;87(4):859-66. doi: 10.1104/pp.87.4.859.

The most abundant isoform of the 2S albumin present in seeds of Arabidopsis thaliana has been sequenced and the corresponding gene isolated. Examination of the protein and DNA sequences allows the determination of the exact proteolytic cleavage sites during...

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Krebbers E, Herdies L, De Clercq A, et al. Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family. Plant Physiol. 1988;87(4):859-66doi: 10.1104/pp.87.4.859.
Krebbers, E., Herdies, L., De Clercq, A., Seurinck, J., Leemans, J., Van Damme, J., Segura, M., Gheysen, G., Van Montagu, M., & Vandekerckhove, J. (1988). Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family. Plant physiology, 87(4), 859-66. https://doi.org/10.1104/pp.87.4.859
Krebbers, E, et al. "Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family." Plant physiology vol. 87,4 (1988): 859-66. doi: https://doi.org/10.1104/pp.87.4.859
Krebbers E, Herdies L, De Clercq A, Seurinck J, Leemans J, Van Damme J, Segura M, Gheysen G, Van Montagu M, Vandekerckhove J. Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family. Plant Physiol. 1988 Aug;87(4):859-66. doi: 10.1104/pp.87.4.859. PMID: 16666238; PMCID: PMC1054859.
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Showing 1 to 12 of 218 entries