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Quality of histone modification antibodies undermines chromatin biology research.

F1000Research

Kungulovski G, Jeltsch A.
PMID: 26834995
F1000Res. 2015 Oct 28;4:1160. doi: 10.12688/f1000research.7265.1. eCollection 2015.

Histone post-translational modification (PTM) antibodies are essential research reagents in chromatin biology. However, they suffer from variable properties and insufficient documentation of quality. Antibody manufacturers and vendors should provide detailed lot-specific documentation of quality, rendering further quality checks by...

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Kungulovski G, Jeltsch A. Quality of histone modification antibodies undermines chromatin biology research. F1000Res. 2015;4:1160doi: 10.12688/f1000research.7265.1.
Kungulovski, G., & Jeltsch, A. (2015). Quality of histone modification antibodies undermines chromatin biology research. F1000Research, 41160. https://doi.org/10.12688/f1000research.7265.1
Kungulovski, Goran, and Jeltsch, Albert. "Quality of histone modification antibodies undermines chromatin biology research." F1000Research vol. 4 (2015): 1160. doi: https://doi.org/10.12688/f1000research.7265.1
Kungulovski G, Jeltsch A. Quality of histone modification antibodies undermines chromatin biology research. F1000Res. 2015 Oct 28;4:1160. doi: 10.12688/f1000research.7265.1. eCollection 2015. PMID: 26834995.
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Expression, Purification, and Functional Characterization of Atypical Xenocin, Its Immunity Protein, and Their Domains from Xenorhabdus nematophila.

International journal of bacteriology

Rathore JS.
PMID: 26904727
Int J Bacteriol. 2013;2013:746862. doi: 10.1155/2013/746862. Epub 2013 Dec 18.

Xenorhabdus nematophila, a gram-negative bacterium belonging to the family Enterobacteriaceae is a natural symbiont of a soil nematode from the family Steinernematidae. In this study cloning, expression, and purification of broad range iron regulated multidomain bacteriocin called xenocin from...

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Rathore JS. Expression, Purification, and Functional Characterization of Atypical Xenocin, Its Immunity Protein, and Their Domains from Xenorhabdus nematophila. Int J Bacteriol. 2013;2013:746862doi: 10.1155/2013/746862.
Rathore, J. S. (2013). Expression, Purification, and Functional Characterization of Atypical Xenocin, Its Immunity Protein, and Their Domains from Xenorhabdus nematophila. International journal of bacteriology, 2013746862. https://doi.org/10.1155/2013/746862
Rathore, Jitendra Singh. "Expression, Purification, and Functional Characterization of Atypical Xenocin, Its Immunity Protein, and Their Domains from Xenorhabdus nematophila." International journal of bacteriology vol. 2013 (2013): 746862. doi: https://doi.org/10.1155/2013/746862
Rathore JS. Expression, Purification, and Functional Characterization of Atypical Xenocin, Its Immunity Protein, and Their Domains from Xenorhabdus nematophila. Int J Bacteriol. 2013;2013:746862. doi: 10.1155/2013/746862. Epub 2013 Dec 18. PMID: 26904727; PMCID: PMC4745447.
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Giardia fatty acyl-CoA synthetases as potential drug targets.

Frontiers in microbiology

Guo F, Ortega-Pierres G, Argüello-García R, Zhang H, Zhu G.
PMID: 26257723
Front Microbiol. 2015 Jul 22;6:753. doi: 10.3389/fmicb.2015.00753. eCollection 2015.

Giardiasis caused by Giardia intestinalis (syn. G. lamblia, G. duodenalis) is one of the leading causes of diarrheal parasitic diseases worldwide. Although limited drugs to treat giardiasis are available, there are concerns regarding toxicity in some patients and the...

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Guo F, Ortega-Pierres G, Argüello-García R, et al. Giardia fatty acyl-CoA synthetases as potential drug targets. Front Microbiol. 2015;6:753doi: 10.3389/fmicb.2015.00753.
Guo, F., Ortega-Pierres, G., Argüello-García, R., Zhang, H., & Zhu, G. (2015). Giardia fatty acyl-CoA synthetases as potential drug targets. Frontiers in microbiology, 6753. https://doi.org/10.3389/fmicb.2015.00753
Guo, Fengguang, et al. "Giardia fatty acyl-CoA synthetases as potential drug targets." Frontiers in microbiology vol. 6 (2015): 753. doi: https://doi.org/10.3389/fmicb.2015.00753
Guo F, Ortega-Pierres G, Argüello-García R, Zhang H, Zhu G. Giardia fatty acyl-CoA synthetases as potential drug targets. Front Microbiol. 2015 Jul 22;6:753. doi: 10.3389/fmicb.2015.00753. eCollection 2015. PMID: 26257723; PMCID: PMC4510421.
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Cloning and Stable Expression of cDNA Coding For Platelet Endothelial Cell Adhesion Molecule -1 (PECAM-1, CD31) in NIH-3T3 Cell Line.

Advanced pharmaceutical bulletin

Salehi-Lalemarzi H, Shanehbandi D, Shafaghat F, Abbasi-Kenarsari H, Baradaran B, Movassaghpour AA, Kazemi T.
PMID: 26236664
Adv Pharm Bull. 2015 Jun;5(2):247-53. doi: 10.15171/apb.2015.034. Epub 2015 Jun 01.

PURPOSE: PECAM-1 (CD31) is a glycoprotein expressed on endothelial and bone marrow precursor cells. It plays important roles in angiogenesis, maintenance and integration of the cytoskeleton and direction of leukocytes to the site of inflammation. We aimed to clone...

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Salehi-Lalemarzi H, Shanehbandi D, Shafaghat F, et al. Cloning and Stable Expression of cDNA Coding For Platelet Endothelial Cell Adhesion Molecule -1 (PECAM-1, CD31) in NIH-3T3 Cell Line. Adv Pharm Bull. 2015;5(2):247-53doi: 10.15171/apb.2015.034.
Salehi-Lalemarzi, H., Shanehbandi, D., Shafaghat, F., Abbasi-Kenarsari, H., Baradaran, B., Movassaghpour, A. A., & Kazemi, T. (2015). Cloning and Stable Expression of cDNA Coding For Platelet Endothelial Cell Adhesion Molecule -1 (PECAM-1, CD31) in NIH-3T3 Cell Line. Advanced pharmaceutical bulletin, 5(2), 247-53. https://doi.org/10.15171/apb.2015.034
Salehi-Lalemarzi, Hamed, et al. "Cloning and Stable Expression of cDNA Coding For Platelet Endothelial Cell Adhesion Molecule -1 (PECAM-1, CD31) in NIH-3T3 Cell Line." Advanced pharmaceutical bulletin vol. 5,2 (2015): 247-53. doi: https://doi.org/10.15171/apb.2015.034
Salehi-Lalemarzi H, Shanehbandi D, Shafaghat F, Abbasi-Kenarsari H, Baradaran B, Movassaghpour AA, Kazemi T. Cloning and Stable Expression of cDNA Coding For Platelet Endothelial Cell Adhesion Molecule -1 (PECAM-1, CD31) in NIH-3T3 Cell Line. Adv Pharm Bull. 2015 Jun;5(2):247-53. doi: 10.15171/apb.2015.034. Epub 2015 Jun 01. PMID: 26236664; PMCID: PMC4517076.
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Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients.

Scientia pharmaceutica

Mueller M, Loh MQ, Gagnon P.
PMID: 26839826
Sci Pharm. 2015 Mar 04;83(2):401-10. doi: 10.3797/scipharm.1501-12. Print 2015.

Protease activity from host cell lines may cause product loss or affect the quality of recombinant proteins. In this study, we showed that excipients like glycine and sorbitol reduce the proteolysis of an immunoglobulin M (IgM) in the presence...

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Mueller M, Loh MQ, Gagnon P. Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients. Sci Pharm. 2015;83(2):401-10doi: 10.3797/scipharm.1501-12.
Mueller, M., Loh, M. Q., & Gagnon, P. (2015). Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients. Scientia pharmaceutica, 83(2), 401-10. https://doi.org/10.3797/scipharm.1501-12
Mueller, Monika, et al. "Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients." Scientia pharmaceutica vol. 83,2 (2015): 401-10. doi: https://doi.org/10.3797/scipharm.1501-12
Mueller M, Loh MQ, Gagnon P. Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients. Sci Pharm. 2015 Mar 04;83(2):401-10. doi: 10.3797/scipharm.1501-12. Print 2015. PMID: 26839826; PMCID: PMC4727821.
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Accuracy of molecular diagnostics in pemphigus and bullous pemphigoid: comparison of commercial and modified mosaic indirect immunofluorescence tests as well as enzyme-linked immunosorbent assays.

Postepy dermatologii i alergologii

Gornowicz-Porowska J, Seraszek-Jaros A, Bowszyc-Dmochowska M, Kaczmarek E, Pietkiewicz P, Bartkiewicz P, Dmochowski M.
PMID: 28261028
Postepy Dermatol Alergol. 2017 Feb;34(1):21-27. doi: 10.5114/ada.2017.65617. Epub 2017 Feb 07.

INTRODUCTION: Pemphigus and bullous pemphigoid (BP) are identified by autoantibodies (abs) against desmoglein 1, 3 (DSG1/3) and BP180/BP230, respectively. A novel mosaic to indirect immunofluorescence (IIF) using purified BP180 recombinant proteins spotted on slide and transfected cells expressing BP230,...

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Gornowicz-Porowska J, Seraszek-Jaros A, Bowszyc-Dmochowska M, et al. Accuracy of molecular diagnostics in pemphigus and bullous pemphigoid: comparison of commercial and modified mosaic indirect immunofluorescence tests as well as enzyme-linked immunosorbent assays. Postepy Dermatol Alergol. 2017;34(1):21-27doi: 10.5114/ada.2017.65617.
Gornowicz-Porowska, J., Seraszek-Jaros, A., Bowszyc-Dmochowska, M., Kaczmarek, E., Pietkiewicz, P., Bartkiewicz, P., & Dmochowski, M. (2017). Accuracy of molecular diagnostics in pemphigus and bullous pemphigoid: comparison of commercial and modified mosaic indirect immunofluorescence tests as well as enzyme-linked immunosorbent assays. Postepy dermatologii i alergologii, 34(1), 21-27. https://doi.org/10.5114/ada.2017.65617
Gornowicz-Porowska, Justyna, et al. "Accuracy of molecular diagnostics in pemphigus and bullous pemphigoid: comparison of commercial and modified mosaic indirect immunofluorescence tests as well as enzyme-linked immunosorbent assays." Postepy dermatologii i alergologii vol. 34,1 (2017): 21-27. doi: https://doi.org/10.5114/ada.2017.65617
Gornowicz-Porowska J, Seraszek-Jaros A, Bowszyc-Dmochowska M, Kaczmarek E, Pietkiewicz P, Bartkiewicz P, Dmochowski M. Accuracy of molecular diagnostics in pemphigus and bullous pemphigoid: comparison of commercial and modified mosaic indirect immunofluorescence tests as well as enzyme-linked immunosorbent assays. Postepy Dermatol Alergol. 2017 Feb;34(1):21-27. doi: 10.5114/ada.2017.65617. Epub 2017 Feb 07. PMID: 28261028; PMCID: PMC5329104.
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Production and characterization of neurosecretory protein GM using Escherichia coli and Chinese Hamster Ovary cells.

FEBS open bio

Masuda K, Furumitsu M, Taniuchi S, Iwakoshi-Ukena E, Ukena K.
PMID: 26587371
FEBS Open Bio. 2015 Oct 22;5:844-51. doi: 10.1016/j.fob.2015.10.002. eCollection 2015.

Neurosecretory protein GL (NPGL) and neurosecretory protein GM (NPGM) are paralogs recently discovered in birds and in mammals. The post-translational products of NPGL and of NPGM genes include a signal peptide sequence, a glycine amidation signal, and a dibasic...

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Masuda K, Furumitsu M, Taniuchi S, et al. Production and characterization of neurosecretory protein GM using Escherichia coli and Chinese Hamster Ovary cells. FEBS Open Bio. 2015;5:844-51doi: 10.1016/j.fob.2015.10.002.
Masuda, K., Furumitsu, M., Taniuchi, S., Iwakoshi-Ukena, E., & Ukena, K. (2015). Production and characterization of neurosecretory protein GM using Escherichia coli and Chinese Hamster Ovary cells. FEBS open bio, 5844-51. https://doi.org/10.1016/j.fob.2015.10.002
Masuda, Keiko, et al. "Production and characterization of neurosecretory protein GM using Escherichia coli and Chinese Hamster Ovary cells." FEBS open bio vol. 5 (2015): 844-51. doi: https://doi.org/10.1016/j.fob.2015.10.002
Masuda K, Furumitsu M, Taniuchi S, Iwakoshi-Ukena E, Ukena K. Production and characterization of neurosecretory protein GM using Escherichia coli and Chinese Hamster Ovary cells. FEBS Open Bio. 2015 Oct 22;5:844-51. doi: 10.1016/j.fob.2015.10.002. eCollection 2015. PMID: 26587371; PMCID: PMC4625114.
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Gene expression in Mammalian cells and its applications.

Advanced pharmaceutical bulletin

Khan KH.
PMID: 24312845
Adv Pharm Bull. 2013;3(2):257-63. doi: 10.5681/apb.2013.042. Epub 2013 Aug 20.

The production of proteins in appropriate quantity and quality is an essential requirement of the present time. There appears to be a progressive increase in the application of mammalian cells for proteins production. Expression systems utilizing mammalian cells for...

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Khan KH. Gene expression in Mammalian cells and its applications. Adv Pharm Bull. 2013;3(2):257-63doi: 10.5681/apb.2013.042.
Khan, K. H. (2013). Gene expression in Mammalian cells and its applications. Advanced pharmaceutical bulletin, 3(2), 257-63. https://doi.org/10.5681/apb.2013.042
Khan, Kishwar Hayat. "Gene expression in Mammalian cells and its applications." Advanced pharmaceutical bulletin vol. 3,2 (2013): 257-63. doi: https://doi.org/10.5681/apb.2013.042
Khan KH. Gene expression in Mammalian cells and its applications. Adv Pharm Bull. 2013;3(2):257-63. doi: 10.5681/apb.2013.042. Epub 2013 Aug 20. PMID: 24312845; PMCID: PMC3848218.
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Isolation and Characterization of Two Persimmon Xyloglucan Endotransglycosylase/Hydrolase (XTH) Genes That Have Divergent Functions in Cell Wall Modification and Fruit Postharvest Softening.

Frontiers in plant science

Han Y, Ban Q, Hou Y, Meng K, Suo J, Rao J.
PMID: 27242828
Front Plant Sci. 2016 May 11;7:624. doi: 10.3389/fpls.2016.00624. eCollection 2016.

Fruit cell wall modification is the primary factor affecting fruit softening. Xyloglucan endotransglycosylase/hydrolase (XTH), a cell wall-modifying enzyme, is involved in fruit softening. In this study, two novel XTH genes (DkXTH6 and DkXTH7) were identified from persimmon fruit. Transcriptional...

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Han Y, Ban Q, Hou Y, et al. Isolation and Characterization of Two Persimmon Xyloglucan Endotransglycosylase/Hydrolase (XTH) Genes That Have Divergent Functions in Cell Wall Modification and Fruit Postharvest Softening. Front Plant Sci. 2016;7:624doi: 10.3389/fpls.2016.00624.
Han, Y., Ban, Q., Hou, Y., Meng, K., Suo, J., & Rao, J. (2016). Isolation and Characterization of Two Persimmon Xyloglucan Endotransglycosylase/Hydrolase (XTH) Genes That Have Divergent Functions in Cell Wall Modification and Fruit Postharvest Softening. Frontiers in plant science, 7624. https://doi.org/10.3389/fpls.2016.00624
Han, Ye, et al. "Isolation and Characterization of Two Persimmon Xyloglucan Endotransglycosylase/Hydrolase (XTH) Genes That Have Divergent Functions in Cell Wall Modification and Fruit Postharvest Softening." Frontiers in plant science vol. 7 (2016): 624. doi: https://doi.org/10.3389/fpls.2016.00624
Han Y, Ban Q, Hou Y, Meng K, Suo J, Rao J. Isolation and Characterization of Two Persimmon Xyloglucan Endotransglycosylase/Hydrolase (XTH) Genes That Have Divergent Functions in Cell Wall Modification and Fruit Postharvest Softening. Front Plant Sci. 2016 May 11;7:624. doi: 10.3389/fpls.2016.00624. eCollection 2016. PMID: 27242828; PMCID: PMC4863071.
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Identification and Characterization of a Cleavage Site in the Proteolysis of Orf Virus 086 Protein.

Frontiers in microbiology

Wang X, Xiao B, Zhang J, Chen D, Li W, Li M, Hao W, Luo S.
PMID: 27148226
Front Microbiol. 2016 Apr 20;7:538. doi: 10.3389/fmicb.2016.00538. eCollection 2016.

The orf virus (ORFV) is among the parapoxvirus genus of the poxviridae family, but little is known about the proteolytic pathways of ORFV encoding proteins. By contrast, the proteolysis mechanism of the vaccinia virus (VV) has been extensively explored....

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Wang X, Xiao B, Zhang J, et al. Identification and Characterization of a Cleavage Site in the Proteolysis of Orf Virus 086 Protein. Front Microbiol. 2016;7:538doi: 10.3389/fmicb.2016.00538.
Wang, X., Xiao, B., Zhang, J., Chen, D., Li, W., Li, M., Hao, W., & Luo, S. (2016). Identification and Characterization of a Cleavage Site in the Proteolysis of Orf Virus 086 Protein. Frontiers in microbiology, 7538. https://doi.org/10.3389/fmicb.2016.00538
Wang, Xiaoping, et al. "Identification and Characterization of a Cleavage Site in the Proteolysis of Orf Virus 086 Protein." Frontiers in microbiology vol. 7 (2016): 538. doi: https://doi.org/10.3389/fmicb.2016.00538
Wang X, Xiao B, Zhang J, Chen D, Li W, Li M, Hao W, Luo S. Identification and Characterization of a Cleavage Site in the Proteolysis of Orf Virus 086 Protein. Front Microbiol. 2016 Apr 20;7:538. doi: 10.3389/fmicb.2016.00538. eCollection 2016. PMID: 27148226; PMCID: PMC4837287.
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Preparation of Proper Immunogen by Cloning and Stable Expression of cDNA coding for Human Hematopoietic Stem Cell Marker CD34 in NIH-3T3 Mouse Fibroblast Cell Line.

Advanced pharmaceutical bulletin

Shafaghat F, Abbasi-Kenarsari H, Majidi J, Movassaghpour AA, Shanehbandi D, Kazemi T.
PMID: 25789221
Adv Pharm Bull. 2015 Mar;5(1):69-75. doi: 10.5681/apb.2015.009. Epub 2015 Mar 05.

PURPOSE: Transmembrane CD34 glycoprotein is the most important marker for identification, isolation and enumeration of hematopoietic stem cells (HSCs). We aimed in this study to clone the cDNA coding for human CD34 from KG1a cell line and stably express...

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Shafaghat F, Abbasi-Kenarsari H, Majidi J, et al. Preparation of Proper Immunogen by Cloning and Stable Expression of cDNA coding for Human Hematopoietic Stem Cell Marker CD34 in NIH-3T3 Mouse Fibroblast Cell Line. Adv Pharm Bull. 2015;5(1):69-75doi: 10.5681/apb.2015.009.
Shafaghat, F., Abbasi-Kenarsari, H., Majidi, J., Movassaghpour, A. A., Shanehbandi, D., & Kazemi, T. (2015). Preparation of Proper Immunogen by Cloning and Stable Expression of cDNA coding for Human Hematopoietic Stem Cell Marker CD34 in NIH-3T3 Mouse Fibroblast Cell Line. Advanced pharmaceutical bulletin, 5(1), 69-75. https://doi.org/10.5681/apb.2015.009
Shafaghat, Farzaneh, et al. "Preparation of Proper Immunogen by Cloning and Stable Expression of cDNA coding for Human Hematopoietic Stem Cell Marker CD34 in NIH-3T3 Mouse Fibroblast Cell Line." Advanced pharmaceutical bulletin vol. 5,1 (2015): 69-75. doi: https://doi.org/10.5681/apb.2015.009
Shafaghat F, Abbasi-Kenarsari H, Majidi J, Movassaghpour AA, Shanehbandi D, Kazemi T. Preparation of Proper Immunogen by Cloning and Stable Expression of cDNA coding for Human Hematopoietic Stem Cell Marker CD34 in NIH-3T3 Mouse Fibroblast Cell Line. Adv Pharm Bull. 2015 Mar;5(1):69-75. doi: 10.5681/apb.2015.009. Epub 2015 Mar 05. PMID: 25789221; PMCID: PMC4352225.
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Comparison of Expression Vectors for Transient Expression of Recombinant Proteins in Plants.

Plant molecular biology reporter

Shah KH, Almaghrabi B, Bohlmann H.
PMID: 24415845
Plant Mol Biol Report. 2013;31:1529-1538. doi: 10.1007/s11105-013-0614-z.

Production of recombinant proteins in plants is of increasing importance for practical applications. However, the production of stable transformed transgenic plants is a lengthy procedure. Transient expression, on the other hand, can deliver recombinant proteins within a week, and...

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Shah KH, Almaghrabi B, Bohlmann H. Comparison of Expression Vectors for Transient Expression of Recombinant Proteins in Plants. Plant Mol Biol Report. 2013;31:1529-1538doi: 10.1007/s11105-013-0614-z.
Shah, K. H., Almaghrabi, B., & Bohlmann, H. (2013). Comparison of Expression Vectors for Transient Expression of Recombinant Proteins in Plants. Plant molecular biology reporter, 311529-1538. https://doi.org/10.1007/s11105-013-0614-z
Shah, Kausar Hussain, et al. "Comparison of Expression Vectors for Transient Expression of Recombinant Proteins in Plants." Plant molecular biology reporter vol. 31 (2013): 1529-1538. doi: https://doi.org/10.1007/s11105-013-0614-z
Shah KH, Almaghrabi B, Bohlmann H. Comparison of Expression Vectors for Transient Expression of Recombinant Proteins in Plants. Plant Mol Biol Report. 2013;31:1529-1538. doi: 10.1007/s11105-013-0614-z. PMID: 24415845; PMCID: PMC3881577.
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Showing 25 to 36 of 1326 entries