Academic literature on the topic 'Proteomics approaches'

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Journal articles on the topic "Proteomics approaches"

1

DePalma, Angelo. "Improving Proteomics Approaches." Genetic Engineering & Biotechnology News 33, no. 10 (2013): 24–26. http://dx.doi.org/10.1089/gen.33.10.10.

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2

Kalvodova, Lucie. "Understanding the proteomes using non-proteomics approaches: Expanding the scope of PROTEOMICS." PROTEOMICS 17, no. 1-2 (2017): 1770013. http://dx.doi.org/10.1002/pmic.201770013.

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3

Mahajan, R., and P. Gupta. "Proteomics: taking over where genomics leaves off." Czech Journal of Genetics and Plant Breeding 46, No. 2 (2010): 47–53. http://dx.doi.org/10.17221/34/2009-cjgpb.

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The proteomic studies are simultaneously developed in several directions and significantly influence our notions on the capabilities of biological sciences. The need for proteomics research is necessary as there are certain genes in a cell that encode proteins with specific functions. Using a variety of techniques, proteomics can be used to study how proteins interact within a system or how the protein expression changes in different parts of the body, in different stages of its life cycle and in different environmental conditions as every individual has one genome and many proteomes. Besides
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4

Sokolowska, Izabela, Armand G. Ngounou Wetie, Alisa G. Woods, and Costel C. Darie. "Applications of Mass Spectrometry in Proteomics." Australian Journal of Chemistry 66, no. 7 (2013): 721. http://dx.doi.org/10.1071/ch13137.

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Characterisation of proteins and whole proteomes can provide a foundation to our understanding of physiological and pathological states and biological diseases or disorders. Constant development of more reliable and accurate mass spectrometry (MS) instruments and techniques has allowed for better identification and quantification of the thousands of proteins involved in basic physiological processes. Therefore, MS-based proteomics has been widely applied to the analysis of biological samples and has greatly contributed to our understanding of protein functions, interactions, and dynamics, adva
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5

Roeraade, Johan. "Nanotechnology Approaches to Proteomics." Biochemical Society Transactions 27, no. 3 (1999): A69. http://dx.doi.org/10.1042/bst027a069a.

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6

Vahkal, Brett, Jamie Kraft, Emanuela Ferretti, Minyoung Chung, Jean-François Beaulieu, and Illimar Altosaar. "Review of Methodological Approaches to Human Milk Small Extracellular Vesicle Proteomics." Biomolecules 11, no. 6 (2021): 833. http://dx.doi.org/10.3390/biom11060833.

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Proteomics can map extracellular vesicles (EVs), including exosomes, across disease states between organisms and cell types. Due to the diverse origin and cargo of EVs, tailoring methodological and analytical techniques can support the reproducibility of results. Proteomics scans are sensitive to in-sample contaminants, which can be retained during EV isolation procedures. Contaminants can also arise from the biological origin of exosomes, such as the lipid-rich environment in human milk. Human milk (HM) EVs and exosomes are emerging as a research interest in health and disease, though the exp
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7

Oikonomou, Panos, Roberto Salatino, and Saeed Tavazoie. "In vivo mRNA display enables large-scale proteomics by next generation sequencing." Proceedings of the National Academy of Sciences 117, no. 43 (2020): 26710–18. http://dx.doi.org/10.1073/pnas.2002650117.

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Large-scale proteomic methods are essential for the functional characterization of proteins in their native cellular context. However, proteomics has lagged far behind genomic approaches in scalability, standardization, and cost. Here, we introduce in vivo mRNA display, a technology that converts a variety of proteomics applications into a DNA sequencing problem. In vivo-expressed proteins are coupled with their encoding messenger RNAs (mRNAs) via a high-affinity stem-loop RNA binding domain interaction, enabling high-throughput identification of proteins with high sensitivity and specificity
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8

FOSTER, LEONARD J. "MASS SPECTROMETRY OUTGROWS SIMPLE BIOCHEMISTRY: NEW APPROACHES TO ORGANELLE PROTEOMICS." Biophysical Reviews and Letters 01, no. 02 (2006): 209–21. http://dx.doi.org/10.1142/s1793048006000057.

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Organelles are subcellular compartments or structures that typically carry out a defined set of functions within the cell. The functions of many organelles are known or predicted, but without knowing all the components of any recognized organelle it is difficult to fully understand them. Mass spectrometry-based proteomics now allows for routine identification of several hundreds or thousands of proteins in very complex samples; for cell biologists, organelles represent perhaps the most interesting class of cellular components to apply this new technology to. However, in order to analyze the pr
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9

Pino, Lindsay K., Jacob Rose, Amy O'Broin, Samah Shah, and Birgit Schilling. "Emerging mass spectrometry-based proteomics methodologies for novel biomedical applications." Biochemical Society Transactions 48, no. 5 (2020): 1953–66. http://dx.doi.org/10.1042/bst20191091.

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Research into the basic biology of human health and disease, as well as translational human research and clinical applications, all benefit from the growing accessibility and versatility of mass spectrometry (MS)-based proteomics. Although once limited in throughput and sensitivity, proteomic studies have quickly grown in scope and scale over the last decade due to significant advances in instrumentation, computational approaches, and bio-sample preparation. Here, we review these latest developments in MS and highlight how these techniques are used to study the mechanisms, diagnosis, and treat
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10

Gnatenko, Dmitri V., Peter L. Perrotta, and Wadie F. Bahou. "Proteomic approaches to dissect platelet function: half the story." Blood 108, no. 13 (2006): 3983–91. http://dx.doi.org/10.1182/blood-2006-06-026518.

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AbstractPlatelets play critical roles in diverse hemostatic and pathologic disorders and are broadly implicated in various biological processes that include inflammation, wound healing, and thrombosis. Recent progress in high-throughput mRNA and protein profiling techniques has advanced our understanding of the biological functions of platelets. Platelet proteomics has been adopted to decode the complex processes that underlie platelet function by identifying novel platelet-expressed proteins, dissecting mechanisms of signal or metabolic pathways, and analyzing functional changes of the platel
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