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Showing 1 to 12 of 17 entries
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Development of new capillary electrophoresis-based techniques for protein analysis.

Se pu = Chinese journal of chromatography

Liu H, Yang C, Liang Z, Zhang L, Zhang Y.
PMID: 15709414
Se Pu. 2004 Jul;22(4):377-81.

No abstract available.

Cite
Liu H, Yang C, Liang Z, et al. Development of new capillary electrophoresis-based techniques for protein analysis. Se Pu. 2004;22(4):377-81
Liu, H., Yang, C., Liang, Z., Zhang, L., & Zhang, Y. (2004). Development of new capillary electrophoresis-based techniques for protein analysis. Se pu = Chinese journal of chromatography, 22(4), 377-81.
Liu, Hechun, et al. "Development of new capillary electrophoresis-based techniques for protein analysis." Se pu = Chinese journal of chromatography vol. 22,4 (2004): 377-81.
Liu H, Yang C, Liang Z, Zhang L, Zhang Y. Development of new capillary electrophoresis-based techniques for protein analysis. Se Pu. 2004 Jul;22(4):377-81. PMID: 15709414.
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A storable encapsulated bilayer chip containing a single protein nanopore.

Journal of the American Chemical Society

Kang XF, Cheley S, Rice-Ficht AC, Bayley H.
PMID: 17375923
J Am Chem Soc. 2007 Apr 18;129(15):4701-5. doi: 10.1021/ja068654g. Epub 2007 Mar 22.

A robust, portable chip containing a single protein nanopore would be a significant development in the practical application of stochastic sensing technology. Here, we describe a chip in which a single alpha-hemolysin (alphaHL) pore in a planar phospholipid bilayer...

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Kang XF, Cheley S, Rice-Ficht AC, et al. A storable encapsulated bilayer chip containing a single protein nanopore. J Am Chem Soc. 2007;129(15):4701-5doi: 10.1021/ja068654g.
Kang, X. F., Cheley, S., Rice-Ficht, A. C., & Bayley, H. (2007). A storable encapsulated bilayer chip containing a single protein nanopore. Journal of the American Chemical Society, 129(15), 4701-5. https://doi.org/10.1021/ja068654g
Kang, Xiao-feng, et al. "A storable encapsulated bilayer chip containing a single protein nanopore." Journal of the American Chemical Society vol. 129,15 (2007): 4701-5. doi: https://doi.org/10.1021/ja068654g
Kang XF, Cheley S, Rice-Ficht AC, Bayley H. A storable encapsulated bilayer chip containing a single protein nanopore. J Am Chem Soc. 2007 Apr 18;129(15):4701-5. doi: 10.1021/ja068654g. Epub 2007 Mar 22. PMID: 17375923.
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Pimp my spec!.

BioTechniques

Perkel JM.
PMID: 23227984
Biotechniques. 2012 Dec;53(6):339-43. doi: 10.2144/000113960.

No abstract available.

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Perkel JM. Pimp my spec!. Biotechniques. 2012;53(6):339-43doi: 10.2144/000113960.
Perkel, J. M. (2012). Pimp my spec!. BioTechniques, 53(6), 339-43. https://doi.org/10.2144/000113960
Perkel, Jeffrey M. "Pimp my spec!." BioTechniques vol. 53,6 (2012): 339-43. doi: https://doi.org/10.2144/000113960
Perkel JM. Pimp my spec!. Biotechniques. 2012 Dec;53(6):339-43. doi: 10.2144/000113960. PMID: 23227984.
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Bioinformatics and data mining in proteomics.

Expert review of proteomics

Haoudi A, Bensmail H.
PMID: 16771705
Expert Rev Proteomics. 2006 Jun;3(3):333-43. doi: 10.1586/14789450.3.3.333.

Proteomic studies involve the identification as well as qualitative and quantitative comparison of proteins expressed under different conditions, and elucidation of their properties and functions, usually in a large-scale, high-throughput format. The high dimensionality of data generated from these...

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Haoudi A, Bensmail H. Bioinformatics and data mining in proteomics. Expert Rev Proteomics. 2006;3(3):333-43doi: 10.1586/14789450.3.3.333.
Haoudi, A., & Bensmail, H. (2006). Bioinformatics and data mining in proteomics. Expert review of proteomics, 3(3), 333-43. https://doi.org/10.1586/14789450.3.3.333
Haoudi, Abdelali, and Bensmail, Halima. "Bioinformatics and data mining in proteomics." Expert review of proteomics vol. 3,3 (2006): 333-43. doi: https://doi.org/10.1586/14789450.3.3.333
Haoudi A, Bensmail H. Bioinformatics and data mining in proteomics. Expert Rev Proteomics. 2006 Jun;3(3):333-43. doi: 10.1586/14789450.3.3.333. PMID: 16771705.
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Corra: Computational framework and tools for LC-MS discovery and targeted mass spectrometry-based proteomics.

BMC bioinformatics

Brusniak MY, Bodenmiller B, Campbell D, Cooke K, Eddes J, Garbutt A, Lau H, Letarte S, Mueller LN, Sharma V, Vitek O, Zhang N, Aebersold R, Watts JD.
PMID: 19087345
BMC Bioinformatics. 2008 Dec 16;9:542. doi: 10.1186/1471-2105-9-542.

BACKGROUND: Quantitative proteomics holds great promise for identifying proteins that are differentially abundant between populations representing different physiological or disease states. A range of computational tools is now available for both isotopically labeled and label-free liquid chromatography mass spectrometry...

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Brusniak MY, Bodenmiller B, Campbell D, et al. Corra: Computational framework and tools for LC-MS discovery and targeted mass spectrometry-based proteomics. BMC Bioinformatics. 2008;9:542doi: 10.1186/1471-2105-9-542.
Brusniak, M. Y., Bodenmiller, B., Campbell, D., Cooke, K., Eddes, J., Garbutt, A., Lau, H., Letarte, S., Mueller, L. N., Sharma, V., Vitek, O., Zhang, N., Aebersold, R., & Watts, J. D. (2008). Corra: Computational framework and tools for LC-MS discovery and targeted mass spectrometry-based proteomics. BMC bioinformatics, 9542. https://doi.org/10.1186/1471-2105-9-542
Brusniak, Mi-Youn, et al. "Corra: Computational framework and tools for LC-MS discovery and targeted mass spectrometry-based proteomics." BMC bioinformatics vol. 9 (2008): 542. doi: https://doi.org/10.1186/1471-2105-9-542
Brusniak MY, Bodenmiller B, Campbell D, Cooke K, Eddes J, Garbutt A, Lau H, Letarte S, Mueller LN, Sharma V, Vitek O, Zhang N, Aebersold R, Watts JD. Corra: Computational framework and tools for LC-MS discovery and targeted mass spectrometry-based proteomics. BMC Bioinformatics. 2008 Dec 16;9:542. doi: 10.1186/1471-2105-9-542. PMID: 19087345; PMCID: PMC2651178.
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Proteomics and human embryonic stem cells.

Stem cell research

Van Hoof D, Heck AJ, Krijgsveld J, Mummery CL.
PMID: 19383398
Stem Cell Res. 2008 Sep;1(3):169-82. doi: 10.1016/j.scr.2008.05.003. Epub 2008 May 29.

The derivation of human embryonic stem cells (hESCs) brought cell therapy-based regenerative medicine significantly closer to clinical application. However, expansion of undifferentiated cells and their directed differentiation in vitro have proven difficult to control. This is mainly because of...

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Van Hoof D, Heck AJ, Krijgsveld J, et al. Proteomics and human embryonic stem cells. Stem Cell Res. 2008;1(3):169-82doi: 10.1016/j.scr.2008.05.003.
Van Hoof, D., Heck, A. J., Krijgsveld, J., & Mummery, C. L. (2008). Proteomics and human embryonic stem cells. Stem cell research, 1(3), 169-82. https://doi.org/10.1016/j.scr.2008.05.003
Van Hoof, Dennis, et al. "Proteomics and human embryonic stem cells." Stem cell research vol. 1,3 (2008): 169-82. doi: https://doi.org/10.1016/j.scr.2008.05.003
Van Hoof D, Heck AJ, Krijgsveld J, Mummery CL. Proteomics and human embryonic stem cells. Stem Cell Res. 2008 Sep;1(3):169-82. doi: 10.1016/j.scr.2008.05.003. Epub 2008 May 29. PMID: 19383398.
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Using the PRIDE proteomics identifications database for knowledge discovery and data analysis.

Methods in molecular biology (Clifton, N.J.)

Jones P, Martens L.
PMID: 20013379
Methods Mol Biol. 2010;604:297-307. doi: 10.1007/978-1-60761-444-9_20.

The PRIDE Proteomics Identifications Database provides users with the ability to explore and compare mass spectrometry-based proteomics experiments that reveal details of the protein expression found in a broad range of taxonomic groups, tissues and disease states. A PRIDE...

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Jones P, Martens L. Using the PRIDE proteomics identifications database for knowledge discovery and data analysis. Methods Mol Biol. 2010;604:297-307doi: 10.1007/978-1-60761-444-9_20.
Jones, P., & Martens, L. (2010). Using the PRIDE proteomics identifications database for knowledge discovery and data analysis. Methods in molecular biology (Clifton, N.J.), 604297-307. https://doi.org/10.1007/978-1-60761-444-9_20
Jones, Philip, and Martens, Lennart. "Using the PRIDE proteomics identifications database for knowledge discovery and data analysis." Methods in molecular biology (Clifton, N.J.) vol. 604 (2010): 297-307. doi: https://doi.org/10.1007/978-1-60761-444-9_20
Jones P, Martens L. Using the PRIDE proteomics identifications database for knowledge discovery and data analysis. Methods Mol Biol. 2010;604:297-307. doi: 10.1007/978-1-60761-444-9_20. PMID: 20013379.
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Comparative evaluation of label-free SINQ normalized spectral index quantitation in the central proteomics facilities pipeline.

Proteomics

Trudgian DC, Ridlova G, Fischer R, Mackeen MM, Ternette N, Acuto O, Kessler BM, Thomas B.
PMID: 21656681
Proteomics. 2011 Jul;11(14):2790-7. doi: 10.1002/pmic.201000800. Epub 2011 Jun 08.

Normalized spectral index quantification was recently presented as an accurate method of label-free quantitation, which improved spectral counting by incorporating the intensities of peptide MS/MS fragment ions into the calculation of protein abundance. We present SINQ, a tool implementing...

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Trudgian DC, Ridlova G, Fischer R, et al. Comparative evaluation of label-free SINQ normalized spectral index quantitation in the central proteomics facilities pipeline. Proteomics. 2011;11(14):2790-7doi: 10.1002/pmic.201000800.
Trudgian, D. C., Ridlova, G., Fischer, R., Mackeen, M. M., Ternette, N., Acuto, O., Kessler, B. M., & Thomas, B. (2011). Comparative evaluation of label-free SINQ normalized spectral index quantitation in the central proteomics facilities pipeline. Proteomics, 11(14), 2790-7. https://doi.org/10.1002/pmic.201000800
Trudgian, David C, et al. "Comparative evaluation of label-free SINQ normalized spectral index quantitation in the central proteomics facilities pipeline." Proteomics vol. 11,14 (2011): 2790-7. doi: https://doi.org/10.1002/pmic.201000800
Trudgian DC, Ridlova G, Fischer R, Mackeen MM, Ternette N, Acuto O, Kessler BM, Thomas B. Comparative evaluation of label-free SINQ normalized spectral index quantitation in the central proteomics facilities pipeline. Proteomics. 2011 Jul;11(14):2790-7. doi: 10.1002/pmic.201000800. Epub 2011 Jun 08. PMID: 21656681.
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Flow field-flow fractionation: recent trends in protein analysis.

Analytical and bioanalytical chemistry

Rambaldi DC, Reschiglian P, Zattoni A.
PMID: 21046085
Anal Bioanal Chem. 2011 Feb;399(4):1439-47. doi: 10.1007/s00216-010-4312-5. Epub 2010 Oct 28.

Flow field-flow fractionation (F4) is the gentlest flow-assisted separation technique for analysis of macromolecules. The use of an empty channel as separation device and of a second mobile phase flow as perpendicular field enable F4 to separate analytes under...

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Rambaldi DC, Reschiglian P, Zattoni A. Flow field-flow fractionation: recent trends in protein analysis. Anal Bioanal Chem. 2010;399(4):1439-47doi: 10.1007/s00216-010-4312-5.
Rambaldi, D. C., Reschiglian, P., & Zattoni, A. (2011). Flow field-flow fractionation: recent trends in protein analysis. Analytical and bioanalytical chemistry, 399(4), 1439-47. https://doi.org/10.1007/s00216-010-4312-5
Rambaldi, Diana Cristina, et al. "Flow field-flow fractionation: recent trends in protein analysis." Analytical and bioanalytical chemistry vol. 399,4 (2011): 1439-47. doi: https://doi.org/10.1007/s00216-010-4312-5
Rambaldi DC, Reschiglian P, Zattoni A. Flow field-flow fractionation: recent trends in protein analysis. Anal Bioanal Chem. 2011 Feb;399(4):1439-47. doi: 10.1007/s00216-010-4312-5. Epub 2010 Oct 28. PMID: 21046085.
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Analysis of mass spectrometry data in proteomics.

Methods in molecular biology (Clifton, N.J.)

Matthiesen R, Jensen ON.
PMID: 18712299
Methods Mol Biol. 2008;453:105-22. doi: 10.1007/978-1-60327-429-6_4.

The systematic study of proteins and protein networks, that is, proteomics, calls for qualitative and quantitative analysis of proteins and peptides. Mass spectrometry (MS) is a key analytical technology in current proteomics and modern mass spectrometers generate large amounts...

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Matthiesen R, Jensen ON. Analysis of mass spectrometry data in proteomics. Methods Mol Biol. 2008;453:105-22doi: 10.1007/978-1-60327-429-6_4.
Matthiesen, R., & Jensen, O. N. (2008). Analysis of mass spectrometry data in proteomics. Methods in molecular biology (Clifton, N.J.), 453105-22. https://doi.org/10.1007/978-1-60327-429-6_4
Matthiesen, Rune, and Jensen, Ole N. "Analysis of mass spectrometry data in proteomics." Methods in molecular biology (Clifton, N.J.) vol. 453 (2008): 105-22. doi: https://doi.org/10.1007/978-1-60327-429-6_4
Matthiesen R, Jensen ON. Analysis of mass spectrometry data in proteomics. Methods Mol Biol. 2008;453:105-22. doi: 10.1007/978-1-60327-429-6_4. PMID: 18712299.
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Separation methodology to improve proteome coverage depth.

Expert review of proteomics

Lenz C, Urlaub H.
PMID: 24834482
Expert Rev Proteomics. 2014 Aug;11(4):409-14. doi: 10.1586/14789450.2014.919862. Epub 2014 May 16.

So-called 'in-depth proteomics' and its applied separation methodology to improve the proteome coverage depth has become an important issue in mass spectrometric-based proteomics and system-wide cell biology studies. Employing a bottom-up approach and a variety of separation techniques, it...

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Lenz C, Urlaub H. Separation methodology to improve proteome coverage depth. Expert Rev Proteomics. 2014;11(4):409-14doi: 10.1586/14789450.2014.919862.
Lenz, C., & Urlaub, H. (2014). Separation methodology to improve proteome coverage depth. Expert review of proteomics, 11(4), 409-14. https://doi.org/10.1586/14789450.2014.919862
Lenz, Christof, and Urlaub, Henning. "Separation methodology to improve proteome coverage depth." Expert review of proteomics vol. 11,4 (2014): 409-14. doi: https://doi.org/10.1586/14789450.2014.919862
Lenz C, Urlaub H. Separation methodology to improve proteome coverage depth. Expert Rev Proteomics. 2014 Aug;11(4):409-14. doi: 10.1586/14789450.2014.919862. Epub 2014 May 16. PMID: 24834482.
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The Rise of Mass Spectrometry and the Fall of Edman Degradation.

Clinical chemistry

Mann M.
PMID: 26430071
Clin Chem. 2016 Jan;62(1):293-4. doi: 10.1373/clinchem.2014.237271. Epub 2015 Oct 01.

No abstract available.

Cite
Mann M. The Rise of Mass Spectrometry and the Fall of Edman Degradation. Clin Chem. 2015;62(1):293-4doi: 10.1373/clinchem.2014.237271.
Mann, M. (2016). The Rise of Mass Spectrometry and the Fall of Edman Degradation. Clinical chemistry, 62(1), 293-4. https://doi.org/10.1373/clinchem.2014.237271
Mann, Matthias. "The Rise of Mass Spectrometry and the Fall of Edman Degradation." Clinical chemistry vol. 62,1 (2016): 293-4. doi: https://doi.org/10.1373/clinchem.2014.237271
Mann M. The Rise of Mass Spectrometry and the Fall of Edman Degradation. Clin Chem. 2016 Jan;62(1):293-4. doi: 10.1373/clinchem.2014.237271. Epub 2015 Oct 01. PMID: 26430071.
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Showing 1 to 12 of 17 entries