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Showing 1 to 12 of 13 entries
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Dissecting virus-plant interactions through proteomics approaches.

Current proteomics

Xu K, Nagy PD.
PMID: 24039615
Curr Proteomics. 2010 Dec 01;7(4):316-327. doi: 10.2174/157016410793611792.

Plant viruses exploit cellular factors, including host proteins, membranes and metabolites, for their replication in infected cells and to establish systemic infections. Besides traditional genetic, molecular, cellular and biochemical methods studying plant-virus interactions, both global and specialized proteomics methods...

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Xu K, Nagy PD. Dissecting virus-plant interactions through proteomics approaches. Curr Proteomics. 2010;7(4):316-327doi: 10.2174/157016410793611792.
Xu, K., & Nagy, P. D. (2010). Dissecting virus-plant interactions through proteomics approaches. Current proteomics, 7(4), 316-327. https://doi.org/10.2174/157016410793611792
Xu, Kai, and Nagy, Peter D. "Dissecting virus-plant interactions through proteomics approaches." Current proteomics vol. 7,4 (2010): 316-327. doi: https://doi.org/10.2174/157016410793611792
Xu K, Nagy PD. Dissecting virus-plant interactions through proteomics approaches. Curr Proteomics. 2010 Dec 01;7(4):316-327. doi: 10.2174/157016410793611792. PMID: 24039615; PMCID: PMC3769790.
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Proteomics on Fixed Tissue Specimens - A Review.

Current proteomics

Reimel BA, Pan S, May DH, Shaffer SA, Goodlett DR, McIntosh MW, Yerian LM, Bronner MP, Chen R, Brentnall TA.
PMID: 19829741
Curr Proteomics. 2009 Apr 01;6(1):63-69. doi: 10.2174/157016409787847420.

The vast majority of clinical tissue samples are formalin-fixed and paraffin-preserved. This type of preservation has been considered an obstacle to protein extraction from these tissues. However, these are the very tissue samples that have associated patient histories, diagnoses...

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Reimel BA, Pan S, May DH, et al. Proteomics on Fixed Tissue Specimens - A Review. Curr Proteomics. 2009;6(1):63-69doi: 10.2174/157016409787847420.
Reimel, B. A., Pan, S., May, D. H., Shaffer, S. A., Goodlett, D. R., McIntosh, M. W., Yerian, L. M., Bronner, M. P., Chen, R., & Brentnall, T. A. (2009). Proteomics on Fixed Tissue Specimens - A Review. Current proteomics, 6(1), 63-69. https://doi.org/10.2174/157016409787847420
Reimel, Beth Ann, et al. "Proteomics on Fixed Tissue Specimens - A Review." Current proteomics vol. 6,1 (2009): 63-69. doi: https://doi.org/10.2174/157016409787847420
Reimel BA, Pan S, May DH, Shaffer SA, Goodlett DR, McIntosh MW, Yerian LM, Bronner MP, Chen R, Brentnall TA. Proteomics on Fixed Tissue Specimens - A Review. Curr Proteomics. 2009 Apr 01;6(1):63-69. doi: 10.2174/157016409787847420. PMID: 19829741; PMCID: PMC2760948.
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Abundance- and Activity-Based Proteomics in Platelet Biology.

Current proteomics

Holly SP, Chen X, Parise LV.
PMID: 22308104
Curr Proteomics. 2011 Oct;8(3):216-228. doi: 10.2174/157016411797247512.

Human platelets are thought to express approximately 2000-3000 proteins, but post-translational modifications, alternatively spliced variants and a rich diversity of vertebrate domain architectures likely make this a conservative estimate. Even though rapidly advancing proteomic techniques have facilitated the identification...

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Holly SP, Chen X, Parise LV. Abundance- and Activity-Based Proteomics in Platelet Biology. Curr Proteomics. 2011;8(3):216-228doi: 10.2174/157016411797247512.
Holly, S. P., Chen, X., & Parise, L. V. (2011). Abundance- and Activity-Based Proteomics in Platelet Biology. Current proteomics, 8(3), 216-228. https://doi.org/10.2174/157016411797247512
Holly, Stephen P, et al. "Abundance- and Activity-Based Proteomics in Platelet Biology." Current proteomics vol. 8,3 (2011): 216-228. doi: https://doi.org/10.2174/157016411797247512
Holly SP, Chen X, Parise LV. Abundance- and Activity-Based Proteomics in Platelet Biology. Curr Proteomics. 2011 Oct;8(3):216-228. doi: 10.2174/157016411797247512. PMID: 22308104; PMCID: PMC3270490.
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Identification of Osteoporosis-Associated Protein Biomarkers from Ovariectomized Rat Urine.

Current proteomics

Lim J, Hwang S.
PMID: 28579927
Curr Proteomics. 2017 Jun;14(2):130-137. doi: 10.2174/1570164614666161228124801.

OBJECTIVE: Osteoporotic fracture is one of the most common health risks and aggravates the quality of life among postmenopausal women worldwide. In this study, osteoporosis-associated protein biomarkers were identified from urine of osteoporotic female Sprague-Dawley rats developed by ovariectomy.METHOD:...

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Lim J, Hwang S. Identification of Osteoporosis-Associated Protein Biomarkers from Ovariectomized Rat Urine. Curr Proteomics. 2017;14(2):130-137doi: 10.2174/1570164614666161228124801.
Lim, J., & Hwang, S. (2017). Identification of Osteoporosis-Associated Protein Biomarkers from Ovariectomized Rat Urine. Current proteomics, 14(2), 130-137. https://doi.org/10.2174/1570164614666161228124801
Lim, Jinkyu, and Hwang, Sunil. "Identification of Osteoporosis-Associated Protein Biomarkers from Ovariectomized Rat Urine." Current proteomics vol. 14,2 (2017): 130-137. doi: https://doi.org/10.2174/1570164614666161228124801
Lim J, Hwang S. Identification of Osteoporosis-Associated Protein Biomarkers from Ovariectomized Rat Urine. Curr Proteomics. 2017 Jun;14(2):130-137. doi: 10.2174/1570164614666161228124801. PMID: 28579927; PMCID: PMC5427775.
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Anti-cancer Therapies in High Grade Gliomas.

Current proteomics

Tanase CP, Enciu AM, Mihai S, Neagu AI, Calenic B, Cruceru ML.
PMID: 24228024
Curr Proteomics. 2013 Sep;10(3):246-260. doi: 10.2174/1570164611310030007.

High grade gliomas represent one of the most aggressive and treatment-resistant types of human cancer, with only 1-2 years median survival rate for patients with grade IV glioma. The treatment of glioblastoma is a considerable therapeutic challenge; combination therapy...

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Tanase CP, Enciu AM, Mihai S, et al. Anti-cancer Therapies in High Grade Gliomas. Curr Proteomics. 2013;10(3):246-260doi: 10.2174/1570164611310030007.
Tanase, C. P., Enciu, A. M., Mihai, S., Neagu, A. I., Calenic, B., & Cruceru, M. L. (2013). Anti-cancer Therapies in High Grade Gliomas. Current proteomics, 10(3), 246-260. https://doi.org/10.2174/1570164611310030007
Tanase, Cristiana Pistol, et al. "Anti-cancer Therapies in High Grade Gliomas." Current proteomics vol. 10,3 (2013): 246-260. doi: https://doi.org/10.2174/1570164611310030007
Tanase CP, Enciu AM, Mihai S, Neagu AI, Calenic B, Cruceru ML. Anti-cancer Therapies in High Grade Gliomas. Curr Proteomics. 2013 Sep;10(3):246-260. doi: 10.2174/1570164611310030007. PMID: 24228024; PMCID: PMC3821381.
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Analysis of Glycosaminoglycans Using Mass Spectrometry.

Current proteomics

Staples GO, Zaia J.
PMID: 25705143
Curr Proteomics. 2011;8(4):325-336. doi: 10.2174/157016411798220871.

The glycosaminoglycans (GAGs) are linear polysaccharides expressed on animal cell surfaces and in extracellular matrices. Their biosynthesis is under complex control and confers a domain structure that is essential to their ability to bind to protein partners. Key to...

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Staples GO, Zaia J. Analysis of Glycosaminoglycans Using Mass Spectrometry. Curr Proteomics. 2011;8(4):325-336doi: 10.2174/157016411798220871.
Staples, G. O., & Zaia, J. (2011). Analysis of Glycosaminoglycans Using Mass Spectrometry. Current proteomics, 8(4), 325-336. https://doi.org/10.2174/157016411798220871
Staples, Gregory O, and Zaia, Joseph. "Analysis of Glycosaminoglycans Using Mass Spectrometry." Current proteomics vol. 8,4 (2011): 325-336. doi: https://doi.org/10.2174/157016411798220871
Staples GO, Zaia J. Analysis of Glycosaminoglycans Using Mass Spectrometry. Curr Proteomics. 2011;8(4):325-336. doi: 10.2174/157016411798220871. PMID: 25705143; PMCID: PMC4334465.
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B-factor Analysis and Conformational Rearrangement of Aldose Reductase.

Current proteomics

Balendiran GK, Pandian JR, Drake E, Vinayak A, Verma M, Cascio D.
PMID: 25364319
Curr Proteomics. 2014;11(3):151-160. doi: 10.2174/157016461103140922163444.

The NADPH-dependent reduction of glucose reaction that is catalyzed by Aldose Reductase (AR) follows a sequential ordered kinetic mechanism in which the co-factor NADPH binds to the enzyme prior to the aldehyde substrate. The kinetic/structural experiments have found a...

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Balendiran GK, Pandian JR, Drake E, et al. B-factor Analysis and Conformational Rearrangement of Aldose Reductase. Curr Proteomics. 2014;11(3):151-160doi: 10.2174/157016461103140922163444.
Balendiran, G. K., Pandian, J. R., Drake, E., Vinayak, A., Verma, M., & Cascio, D. (2014). B-factor Analysis and Conformational Rearrangement of Aldose Reductase. Current proteomics, 11(3), 151-160. https://doi.org/10.2174/157016461103140922163444
Balendiran, Ganesaratnam K, et al. "B-factor Analysis and Conformational Rearrangement of Aldose Reductase." Current proteomics vol. 11,3 (2014): 151-160. doi: https://doi.org/10.2174/157016461103140922163444
Balendiran GK, Pandian JR, Drake E, Vinayak A, Verma M, Cascio D. B-factor Analysis and Conformational Rearrangement of Aldose Reductase. Curr Proteomics. 2014;11(3):151-160. doi: 10.2174/157016461103140922163444. PMID: 25364319; PMCID: PMC4212266.
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DIFFERENTIAL SERUM LEVEL OF SPECIFIC HAPTOGLOBIN ISOFORMS IN SMALL CELL LUNG CANCER.

Current proteomics

Shah A, Singh H, Sachdev V, Lee J, Yotsukura S, Salgia R, Bharti A.
PMID: 20526421
Curr Proteomics. 2010 Apr 01;7(1):49-65. doi: 10.2174/157016410790979635.

Lung cancer is the leading cause of cancer death for both men and women in the United States, and similar trends are seen world wide. The lack of early diagnosis is one of the primary reasons for the high...

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Shah A, Singh H, Sachdev V, et al. DIFFERENTIAL SERUM LEVEL OF SPECIFIC HAPTOGLOBIN ISOFORMS IN SMALL CELL LUNG CANCER. Curr Proteomics. 2010;7(1):49-65doi: 10.2174/157016410790979635.
Shah, A., Singh, H., Sachdev, V., Lee, J., Yotsukura, S., Salgia, R., & Bharti, A. (2010). DIFFERENTIAL SERUM LEVEL OF SPECIFIC HAPTOGLOBIN ISOFORMS IN SMALL CELL LUNG CANCER. Current proteomics, 7(1), 49-65. https://doi.org/10.2174/157016410790979635
Shah, Ankur, et al. "DIFFERENTIAL SERUM LEVEL OF SPECIFIC HAPTOGLOBIN ISOFORMS IN SMALL CELL LUNG CANCER." Current proteomics vol. 7,1 (2010): 49-65. doi: https://doi.org/10.2174/157016410790979635
Shah A, Singh H, Sachdev V, Lee J, Yotsukura S, Salgia R, Bharti A. DIFFERENTIAL SERUM LEVEL OF SPECIFIC HAPTOGLOBIN ISOFORMS IN SMALL CELL LUNG CANCER. Curr Proteomics. 2010 Apr 01;7(1):49-65. doi: 10.2174/157016410790979635. PMID: 20526421; PMCID: PMC2880513.
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Bioinformatics Tools for Mass Spectrometry-Based High-Throughput Quantitative Proteomics Platforms.

Current proteomics

Nefedov AV, Gilski MJ, Sadygov RG.
PMID: 23002391
Curr Proteomics. 2011 Jul;8(2):125-137. doi: 10.2174/157016411795678020.

Determining global proteome changes is important for advancing a systems biology view of cellular processes and for discovering biomarkers. Liquid chromatography, coupled to mass spectrometry, has been widely used as a proteomics technique for discovering differentially expressed proteins in...

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Nefedov AV, Gilski MJ, Sadygov RG. Bioinformatics Tools for Mass Spectrometry-Based High-Throughput Quantitative Proteomics Platforms. Curr Proteomics. 2011;8(2):125-137doi: 10.2174/157016411795678020.
Nefedov, A. V., Gilski, M. J., & Sadygov, R. G. (2011). Bioinformatics Tools for Mass Spectrometry-Based High-Throughput Quantitative Proteomics Platforms. Current proteomics, 8(2), 125-137. https://doi.org/10.2174/157016411795678020
Nefedov, Alexey V, et al. "Bioinformatics Tools for Mass Spectrometry-Based High-Throughput Quantitative Proteomics Platforms." Current proteomics vol. 8,2 (2011): 125-137. doi: https://doi.org/10.2174/157016411795678020
Nefedov AV, Gilski MJ, Sadygov RG. Bioinformatics Tools for Mass Spectrometry-Based High-Throughput Quantitative Proteomics Platforms. Curr Proteomics. 2011 Jul;8(2):125-137. doi: 10.2174/157016411795678020. PMID: 23002391; PMCID: PMC3448448.
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Proteomic Changes Between .

Current proteomics

Wang Y, Li Y, Suo Y, Min Y, Kang X.
PMID: 29151823
Curr Proteomics. 2017 Sep;14(3):166-174. doi: 10.2174/1570164614666170310142405.

BACKGROUND: Polyploid breeding is a powerful approach for Populus genetic improve-ment because polyploid trees have valuable characteristics, including better timber quality and a higher degree of stress resistance compared with their full-sib diploids. However, the genetic mech-anism underlying this...

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Wang Y, Li Y, Suo Y, et al. Proteomic Changes Between . Curr Proteomics. 2017;14(3):166-174doi: 10.2174/1570164614666170310142405.
Wang, Y., Li, Y., Suo, Y., Min, Y., & Kang, X. (2017). Proteomic Changes Between . Current proteomics, 14(3), 166-174. https://doi.org/10.2174/1570164614666170310142405
Wang, Yi, et al. "Proteomic Changes Between ." Current proteomics vol. 14,3 (2017): 166-174. doi: https://doi.org/10.2174/1570164614666170310142405
Wang Y, Li Y, Suo Y, Min Y, Kang X. Proteomic Changes Between . Curr Proteomics. 2017 Sep;14(3):166-174. doi: 10.2174/1570164614666170310142405. PMID: 29151823; PMCID: PMC5676023.
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Immunomics in Skin Cancer - Improvement in Diagnosis, Prognosis and Therapy Monitoring.

Current proteomics

Bulman A, Neagu M, Constantin C.
PMID: 24228023
Curr Proteomics. 2013 Sep;10(3):202-217. doi: 10.2174/1570164611310030003.

This review will focus on the elements of the skin's immune system, immune cells and/or non-immune cells that support immune mechanisms, molecules with immune origin and/or immune functions that are involved in skin carcinogenesis. All these immune elements are...

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Bulman A, Neagu M, Constantin C. Immunomics in Skin Cancer - Improvement in Diagnosis, Prognosis and Therapy Monitoring. Curr Proteomics. 2013;10(3):202-217doi: 10.2174/1570164611310030003.
Bulman, A., Neagu, M., & Constantin, C. (2013). Immunomics in Skin Cancer - Improvement in Diagnosis, Prognosis and Therapy Monitoring. Current proteomics, 10(3), 202-217. https://doi.org/10.2174/1570164611310030003
Bulman, Amanda, et al. "Immunomics in Skin Cancer - Improvement in Diagnosis, Prognosis and Therapy Monitoring." Current proteomics vol. 10,3 (2013): 202-217. doi: https://doi.org/10.2174/1570164611310030003
Bulman A, Neagu M, Constantin C. Immunomics in Skin Cancer - Improvement in Diagnosis, Prognosis and Therapy Monitoring. Curr Proteomics. 2013 Sep;10(3):202-217. doi: 10.2174/1570164611310030003. PMID: 24228023; PMCID: PMC3821382.
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Insight into the Protein Components of the Box H/ACA RNP.

Current proteomics

Karijolich J, Yu YT.
PMID: 19829749
Curr Proteomics. 2008 Jul 01;5(2):129-137. doi: 10.2174/157016408784911936.

Among eukaryotic organisms a vast majority of Box H/ACA ribonucleoproteins (RNPs) are responsible for the post-transcriptional introduction of pseudouridine (Psi) into ribosomal RNAs (rRNA) and spliceosomal small nuclear RNAs (snRNA), thus influencing protein translation and pre-mRNA splicing, respectively. Additionally,...

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Karijolich J, Yu YT. Insight into the Protein Components of the Box H/ACA RNP. Curr Proteomics. 2008;5(2):129-137doi: 10.2174/157016408784911936.
Karijolich, J., & Yu, Y. T. (2008). Insight into the Protein Components of the Box H/ACA RNP. Current proteomics, 5(2), 129-137. https://doi.org/10.2174/157016408784911936
Karijolich, John, and Yu, Yi-Tao. "Insight into the Protein Components of the Box H/ACA RNP." Current proteomics vol. 5,2 (2008): 129-137. doi: https://doi.org/10.2174/157016408784911936
Karijolich J, Yu YT. Insight into the Protein Components of the Box H/ACA RNP. Curr Proteomics. 2008 Jul 01;5(2):129-137. doi: 10.2174/157016408784911936. PMID: 19829749; PMCID: PMC2760984.
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Showing 1 to 12 of 13 entries