Academic literature on the topic 'Serum Proteomics'

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Journal articles on the topic "Serum Proteomics"

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Avram, Oren, Aya Kigel, Anna Vaisman-Mentesh, Sharon Kligsberg, Shai Rosenstein, Yael Dror, Tal Pupko, and Yariv Wine. "PASA: Proteomic analysis of serum antibodies web server." PLOS Computational Biology 17, no. 1 (January 25, 2021): e1008607. http://dx.doi.org/10.1371/journal.pcbi.1008607.

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Motivation A comprehensive characterization of the humoral response towards a specific antigen requires quantification of the B-cell receptor repertoire by next-generation sequencing (BCR-Seq), as well as the analysis of serum antibodies against this antigen, using proteomics. The proteomic analysis is challenging since it necessitates the mapping of antigen-specific peptides to individual B-cell clones. Results The PASA web server provides a robust computational platform for the analysis and integration of data obtained from proteomics of serum antibodies. PASA maps peptides derived from antibodies raised against a specific antigen to corresponding antibody sequences. It then analyzes and integrates proteomics and BCR-Seq data, thus providing a comprehensive characterization of the humoral response. The PASA web server is freely available at https://pasa.tau.ac.il and open to all users without a login requirement.
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Bhawal, Ruchika, Ann L. Oberg, Sheng Zhang, and Manish Kohli. "Challenges and Opportunities in Clinical Applications of Blood-Based Proteomics in Cancer." Cancers 12, no. 9 (August 27, 2020): 2428. http://dx.doi.org/10.3390/cancers12092428.

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Blood is a readily accessible biofluid containing a plethora of important proteins, nucleic acids, and metabolites that can be used as clinical diagnostic tools in diseases, including cancer. Like the on-going efforts for cancer biomarker discovery using the liquid biopsy detection of circulating cell-free and cell-based tumor nucleic acids, the circulatory proteome has been underexplored for clinical cancer biomarker applications. A comprehensive proteome analysis of human serum/plasma with high-quality data and compelling interpretation can potentially provide opportunities for understanding disease mechanisms, although several challenges will have to be met. Serum/plasma proteome biomarkers are present in very low abundance, and there is high complexity involved due to the heterogeneity of cancers, for which there is a compelling need to develop sensitive and specific proteomic technologies and analytical platforms. To date, liquid chromatography mass spectrometry (LC-MS)-based quantitative proteomics has been a dominant analytical workflow to discover new potential cancer biomarkers in serum/plasma. This review will summarize the opportunities of serum proteomics for clinical applications; the challenges in the discovery of novel biomarkers in serum/plasma; and current proteomic strategies in cancer research for the application of serum/plasma proteomics for clinical prognostic, predictive, and diagnostic applications, as well as for monitoring minimal residual disease after treatments. We will highlight some of the recent advances in MS-based proteomics technologies with appropriate sample collection, processing uniformity, study design, and data analysis, focusing on how these integrated workflows can identify novel potential cancer biomarkers for clinical applications.
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Arderiu, Gemma, Guiomar Mendieta, Alex Gallinat, Carmen Lambert, Alberto Díez-Caballero, Carlos Ballesta, and Lina Badimon. "Type 2 Diabetes in Obesity: A Systems Biology Study on Serum and Adipose Tissue Proteomic Profiles." International Journal of Molecular Sciences 24, no. 1 (January 3, 2023): 827. http://dx.doi.org/10.3390/ijms24010827.

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Obesity is associated with metabolic disorders such as insulin resistance and type 2 diabetes mellitus (T2DM), further increasing an already heightened cardiovascular risk. Here, amongst obese class III bariatric surgery patients, we have investigated the effect of T2DM in serum and in two, same patient, adipose tissue (AT) depots through proteomic profile expression analyses. Serum and AT samples from subcutaneous (SAT) and visceral (VAT) fat were collected during bariatric surgery. Bead-based targeted multiplex assay systems were used to simultaneously detect and quantify multiple targets in serum samples (targeted proteomics) and analyze changes in adipokine serum composition. AT samples were assessed through an untargeted proteomics approach. Through a systems biology analysis of the proteomic data, information on the affected biological pathways was acquired. In obese class III individuals, the presence of T2DM induced a significantly higher systemic release of ghrelin, GLP-1, glucagon, MMP3, BAFF, chitinase 3-like 1, TNF-R1 and TNF-R2, and a lower systemic release of IL-8. SAT and VAT proteomes belonging to the same patient showed significant differences in local protein content. While the proteins upregulated in VAT were indicative of metabolic dysregulation, SAT protein upregulation suggested adequate endocrine regulation. The presence of T2DM significantly affected VAT protein composition through the upregulation of dysregulating metabolic pathways, but SAT protein composition was not significantly modified. Our results show that T2DM induces metabolic dysregulation in obese individuals with changes in systemic marker levels and impairment of proteostasis in VAT but not in SAT.
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Issaq, Haleem J., Zhen Xiao, and Timothy D. Veenstra. "Serum and Plasma Proteomics." Chemical Reviews 107, no. 8 (August 2007): 3601–20. http://dx.doi.org/10.1021/cr068287r.

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Hohn, Andreas, Ivan Iovino, Fabrizio Cirillo, Hendrik Drinhaus, Kathrin Kleinbrahm, Lennert Boehm, Edoardo De Robertis, and Jochen Hinkelbein. "Bioinformatical Analysis of Organ-Related (Heart, Brain, Liver, and Kidney) and Serum Proteomic Data to Identify Protein Regulation Patterns and Potential Sepsis Biomarkers." BioMed Research International 2018 (March 21, 2018): 1–11. http://dx.doi.org/10.1155/2018/3576157.

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During the last years, proteomic studies have revealed several interesting findings in experimental sepsis models and septic patients. However, most studies investigated protein alterations only in single organs or in whole blood. To identify possible sepsis biomarkers and to evaluate the relationship between protein alteration in sepsis affected organs and blood, proteomics data from the heart, brain, liver, kidney, and serum were analysed. Using functional network analyses in combination with hierarchical cluster analysis, we found that protein regulation patterns in organ tissues as well as in serum are highly dynamic. In the tissue proteome, the main functions and pathways affected were the oxidoreductive activity, cell energy generation, or metabolism, whereas in the serum proteome, functions were associated with lipoproteins metabolism and, to a minor extent, with coagulation, inflammatory response, and organ regeneration. Proteins from network analyses of organ tissue did not correlate with statistically significantly regulated serum proteins or with predicted proteins of serum functions. In this study, the combination of proteomic network analyses with cluster analyses is introduced as an approach to deal with high-throughput proteomics data to evaluate the dynamics of protein regulation during sepsis.
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Shirai, Kumiko, Hayato Hikita, Sadatsugu Sakane, Ryohei Narumi, Jun Adachi, Akira Doi, Satoshi Tanaka, et al. "Serum amyloid P component and pro-platelet basic protein in extracellular vesicles or serum are novel markers of liver fibrosis in chronic hepatitis C patients." PLOS ONE 17, no. 7 (July 7, 2022): e0271020. http://dx.doi.org/10.1371/journal.pone.0271020.

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Extracellular vesicles (EVs) contain proteins, mRNAs, and microRNAs, and their cargos have emerged as novel diagnostic markers in various diseases. We aimed to discover novel and noninvasive biomarkers of liver fibrosis by proteomic analysis using serum EVs in patients with chronic hepatitis C. We performed shotgun proteomics using serum EVs isolated from 54 patients with histologically assessed liver fibrosis. Shotgun proteomics identified a total of 974 proteins, and 445 proteins were detected in more than half of the patients. Among them, a total of 9 proteins were identified as proteins that tended to increase or decrease with liver fibrosis with a significance of p<0.005 and that were different between F1-2 patients and F3-4 patients with a significance of p<0.01. Among the 9 proteins, targeted proteomics using serum EVs isolated from the sera of another 80 patients with histologically assessed liver fibrosis verified that serum amyloid P component (SAP) and pro-platelet basic protein (PPBP) levels in EVs significantly decreased with the progression of liver fibrosis and were significantly lower in F3-4 patients than in F1-2 patients. The diagnostic accuracies of SAP and PPBP in EVs for the liver fibrosis stage were comparable to those of type IV collagen 7S, hyaluronic acid, and the fibrosis-4 index (FIB-4 index). Moreover, serum SAP and PPBP levels correlated with the levels in EVs, and the ability of serum SAP and PPBP to diagnose liver fibrosis stage was also comparable to the abilities of type IV collagen 7S, hyaluronic acid, and the FIB-4 index. In conclusion, proteomic analysis of serum EVs identified SAP and PPBP as candidate biomarkers for predicting liver fibrosis in patients with chronic hepatitis C. In addition, SAP and PPBP levels in serum are strongly correlated with those in EVs and could represent markers of liver fibrosis.
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Lee, Pey Yee, Junaida Osman, Teck Yew Low, and Rahman Jamal. "Plasma/serum proteomics: depletion strategies for reducing high-abundance proteins for biomarker discovery." Bioanalysis 11, no. 19 (October 2019): 1799–812. http://dx.doi.org/10.4155/bio-2019-0145.

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Plasma and serum are widely used for proteomics-based biomarker discovery. However, analysis of these biofluids is highly challenging due to the complexity and wide dynamic range of their proteomes. Notably, highly abundant proteins tend to obscure the detection of potential biomarkers that are usually of lower concentrations. Among the strategies to resolve this problem are: depletion of high-abundance proteins, enrichment of low abundant proteins of interest and prefractionation. In this review, we focus on current and emerging depletion techniques used to enhance the detection and identification of the less abundant proteins in plasma and serum. We discuss the applications and contributions of these methods to proteomics analysis of plasma and serum alongside their limitations and future perspectives.
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Cottingham, Katie. "Research Profile: Mouse serum proteomics." Journal of Proteome Research 4, no. 5 (October 2005): 1481. http://dx.doi.org/10.1021/pr050525w.

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Kawada, Norifumi. "Cancer Serum Proteomics in Gastroenterology." Gastroenterology 130, no. 6 (May 2006): 1917–19. http://dx.doi.org/10.1053/j.gastro.2006.03.029.

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ANGI, M., BE DAMATO, and SE COUPLAND. "Serum proteomics in uveal melanoma." Acta Ophthalmologica 88 (September 2010): 0. http://dx.doi.org/10.1111/j.1755-3768.2010.3263.x.

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Dissertations / Theses on the topic "Serum Proteomics"

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Kabir, M. "Ovarian cancer serum biomarker discovery using proteomics." Thesis, University College London (University of London), 2008. http://discovery.ucl.ac.uk/1444306/.

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Ovarian cancer is a lethal gynaecological malignancy which is known as the silent killer. It has a poor prognosis due to the lack of major symptoms in early stage disease and hence its late detection. Cancer antigen-125, the most widely used biomarker for ovarian cancer detection, lacks appropriate sensitivity and specificity. Thus, early biomarkers of the disease are urgently required. Proteomic analysis of human serum promises to be a valuable approach for the discovery of putative biomarkers for human malignancies like ovarian cancer, which could be developed into non-invasive blood tests. In this study, serum samples from a pilot study for ovarian cancer screening which were collected prior to diagnosis were processed at Memorial Sloan Kettering Cancer Research Centre, in collaboration with Prof. Tempst's group, who had developed a novel mass spectrometry (MS)-based technology platform for the high-throughput extraction and measurement of serum peptides. Several marker peaks were identified, which when used in combination with the ovarian cancer biomarker CA-125, assisted in the discrimination of case versus healthy samples at an earlier point prior to diagnosis. Work then involved the establishment and optimisation of a similar serum profiling platform at UCL. This involved the optimisation of a liquid-handling robot to provide semi-automated high-throughput sample purification and spotting, and optimisation of spectral acquisition and processing. The reproducibility of the platform was tested and the effects of different sample handling conditions on peptide profiles examined. The method was then used to search for putative markers of ovarian cancer, using identically processed samples from women diagnosed with malignant or benign ovarian cancer and healthy controls. Finally, as a complementary approach to discover protein biomarkers, the same samples were profiled using 2D Difference Gel Electrophoresis, employing different fractionation strategies to overcome the very large dynamic range of protein expression in serum. Mass spectrometry was used to identify several previously reported and some novel putative biomarkers of ovarian cancer, which warrant further validation.
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Brandtzaeg, Ole Kristian, Elin Johnsen, Hanne Roberg-Larsen, Knut Fredrik Seip, Evan L. MacLean, Laurence R. Gesquiere, Siri Leknes, Elsa Lundanes, and Steven Ray Wilson. "Proteomics tools reveal startlingly high amounts of oxytocin in plasma and serum." NATURE PUBLISHING GROUP, 2016. http://hdl.handle.net/10150/622705.

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The neuropeptide oxytocin (OT) is associated with a plethora of social behaviors, and is a key topic at the intersection of psychology and biology. However, tools for measuring OT are still not fully developed. We describe a robust nano liquid chromatography-mass spectrometry (nanoLC-MS) platform for measuring the total amount of OT in human plasma/serum. OT binds strongly to plasma proteins, but a reduction/alkylation (R/A) procedure breaks this bond, enabling ample detection of total OT. The method (R/A + robust nanoLC-MS) was used to determine total OT plasma/serum levels to startlingly high concentrations (high pg/mL-ng/mL). Similar results were obtained when combining R/A and ELISA. Compared to measuring free OT, measuring total OT can have advantages in e.g. biomarker studies.
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Grassl, Julia. "Breast cancer serum proteomics : sample processing and protein profiling by mass spectrometry." Thesis, Swansea University, 2007. https://cronfa.swan.ac.uk/Record/cronfa42525.

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The aim of this project was to develop a method for discovery of biomarkers or a protein pattern, as a signature of breast cancer. Early detection of breast cancer is crucial to increase the survival rates of patients. Little was published about biomarker discovery from serum using mass spectrometry, so over the course of the project each factor of the methodology was analysed and optimized. It was shown that standardisation of sample preparation and handling is critical for any quantitative study. The presence of albumin and other highly abundant proteins in serum interferes with proteomic analysis and so depletion techniques were investigated. Centrifugal ultrafiltration was optimised and an extensive study showed it to be a robust and efficient method to enrich the LMW proteome for subsequent biomarker discovery in serum. SELDI-ToF and MALDI-ToF MS were compared for intact protein profiling for breast cancer. In contrast to SELDI-ToF, MALDI-ToF MS had been little tested for this purpose and therefore new software was developed for peak alignment enabling comparison of multiple spectra. LMW serum samples from 8 breast cancer and 8 control individuals were analysed in each experiment. Here we detected seven potential markers in total and gained initial peptide identifications for three markers. This study also tested the use of label-free quantitation using LC-MS on serum samples from breast cancer patients; one differentially-expressed peptide was discovered. The lack of a software tool for comparison of the resulting spectra limited the detection of further markers. The profiling results showed that the use of replicates all the way from starting with the initial serum sample through to data retrieval is crucial due to variation between the biological replicates, and also to reduce any variation occurring from sample preparation.
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Koutroukides, Theodoros Alexis. "Serum proteome profiling using amine-reactive isobaric tagging mass spectrometry in schizophrenia." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.607699.

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Ward, Nicholas. "Serum protein profiling using a proteomics approach in the diagnosis of colorectal cancer." Thesis, University of Essex, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.510507.

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Sabounchi, Schütt Fariba. "Bronchoalveolar lavage and serum protein patterns in healthy individuals and sarcoidosis patients : a proteomics approach /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-790-8/.

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Cai, Guimei. "Evaluating the effective peak capacity of a saw-tooth gradient for reverse-phase high performance liquid chromatography separation of proteins and peptides." Morgantown, W. Va. : [West Virginia University Libraries], 2007. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5326.

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Thesis (M.S.)--West Virginia University, 2007.
Title from document title page. Document formatted into pages; contains viii, 59 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 54-56).
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Mlynarek, Marcin Aleksander. "Proteomics and the identification of serum biomarkers in a mouse model of oral squamous cell carcinoma." Thesis, McGill University, 2006. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=101731.

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Objective. To establish a clinically relevant model for the identification of protein serum biomarkers for oral squamous cell carcinoma, and to identify specific candidate proteins.
Methods. Samples of oral cancer and adjacent normal tissue were obtained and were transplanted orthotopically into tongues of immunocompromised mice. When the mice lost 20% of their weight, they were sacrificed by exsanguinations. The serum was analyzed by two separate protocols: DIGE/MALDI and MudPIT/LC/ESI. Preliminary validation was conducted on an established cancer marker.
Results. We identified over one hundred proteins as being differentially expressed between control and cancer-bearing mice (p<0.05); including EGFR, cytokeratin 10, gelsolin, titin, vitronectin, retinoblastoma protein family, bullous pemphigoid antigen, and clusterin.
Conclusion. We report a proteomic approach for the identification of serum biomarkers of oral cancer using an orthotopic mouse model. We identified several proteins that can be exploited as potential markers for diagnosis of oral squamous cell carcinoma.
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Zaman, Khadiza. "Revisiting the Neuroprotective Role of 17 Beta Estradiol: A Multi-Omics Based Analysis of the Rat Brain and Serum." Thesis, University of North Texas, 2008. https://digital.library.unt.edu/ark:/67531/metadc1248456/.

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The ovarian hormone 17β-estradiol (E2) is one of the central regulators of the female reproductive system. E2 is also a pleiotropic regulator since it can exert its non-reproductive role on other organ systems. E2 is neuroprotective, it maintains body's energy homeostasis, participates in various repair mechanism and is required for neural development. However, there is a substantial evidence suggesting that there might be a molecular reprogramming of E2's action when it is supplied exogenously after E2 deprivation. Though the length of E2 deprivation and age has been linked to this phenomenon, the molecular components and how they activate this reprogramming is still elusive. Our main goal was to perform global proteomics and metabolomics study to identify the molecular components and their interaction networks that are being altered in the brain and serum after a short-term E2 treatment following ovariectomy (OVX) in Sprague Dawley rats. One of the strength of our global study is that it gave us extensive information on the brain proteome itself by identification of a wide number of proteins in different brain sections. By analyzing the differentially expressed proteins, our proteomics study revealed 49 different networks to be altered in 7 sections of the brain. Most of the perturbed networks were involved in cell metabolism, neural development, protein synthesis, cellular trafficking and degradation, and several stress response signaling pathways. We assessed the neuroenergetic status of the brain based on E2's response to various energy generating pathways, including glycolysis, TCA cycle, and oxidative phosphorylation, and several signaling pathways. All energetics pathways were shown to be downregulated in E2 treatment, which suggests that E2 exerts its neuroprotective role by restoring energy homeostasis in OVX rat model by regulating complex signaling and metabolic networks. Our second focus was to determine the metabolite response (amino acids and lipids) after E2 treatment in the brain and serum by employing targeted metabolomics study. We have found that in rat brain cortex there was significant upregulation of a wide number of amino acids suggesting alternate route of metabolism. Another alternate explanation is that E2 replacement replenished the amino acid pool in the tissue. Pathway enrichment analysis revealed upregulation of several pathways, including amino sugar metabolism, purine metabolism, and glutathione metabolism. By combining proteomics and metabolomics in two different biological matrices we were able to gather a vast array of information on how E2 replacement after E2 deprivation can confer neuroprotection. Our findings will help to create a foundation of basic science to be used for developing potentially effective hormone therapies.
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Zaman, Khadiza. "Revisiting the Neuroprotective Role of 17B-Estradiol (E2): A Multi-Omics Based Analysis of the Rat Brain and Serum." Thesis, University of North Texas, 2018. https://digital.library.unt.edu/ark:/67531/metadc1248456/.

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The ovarian hormone 17β-estradiol (E2) is one of the central regulators of the female reproductive system. E2 is also a pleiotropic regulator since it can exert its non-reproductive role on other organ systems. E2 is neuroprotective, it maintains body's energy homeostasis, participates in various repair mechanism and is required for neural development. However, there is a substantial evidence suggesting that there might be a molecular reprogramming of E2's action when it is supplied exogenously after E2 deprivation. Though the length of E2 deprivation and age has been linked to this phenomenon, the molecular components and how they activate this reprogramming is still elusive. Our main goal was to perform global proteomics and metabolomics study to identify the molecular components and their interaction networks that are being altered in the brain and serum after a short-term E2 treatment following ovariectomy (OVX) in Sprague Dawley rats. One of the strength of our global study is that it gave us extensive information on the brain proteome itself by identification of a wide number of proteins in different brain sections. By analyzing the differentially expressed proteins, our proteomics study revealed 49 different networks to be altered in 7 sections of the brain. Most of the perturbed networks were involved in cell metabolism, neural development, protein synthesis, cellular trafficking and degradation, and several stress response signaling pathways. We assessed the neuroenergetic status of the brain based on E2's response to various energy generating pathways, including glycolysis, TCA cycle, and oxidative phosphorylation, and several signaling pathways. All energetics pathways were shown to be downregulated in E2 treatment, which suggests that E2 exerts its neuroprotective role by restoring energy homeostasis in OVX rat model by regulating complex signaling and metabolic networks. Our second focus was to determine the metabolite response (amino acids and lipids) after E2 treatment in the brain and serum by employing targeted metabolomics study. We have found that in rat brain cortex there was significant upregulation of a wide number of amino acids suggesting alternate route of metabolism. Another alternate explanation is that E2 replacement replenished the amino acid pool in the tissue. Pathway enrichment analysis revealed upregulation of several pathways, including amino sugar metabolism, purine metabolism, and glutathione metabolism. By combining proteomics and metabolomics in two different biological matrices we were able to gather a vast array of information on how E2 replacement after E2 deprivation can confer neuroprotection. Our findings will help to create a foundation of basic science to be used for developing potentially effective hormone therapies.
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Books on the topic "Serum Proteomics"

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Greening, David W., and Richard J. Simpson, eds. Serum/Plasma Proteomics. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7057-5.

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Simpson, Richard J., and David W. Greening, eds. Serum/Plasma Proteomics. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-068-3.

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Greening, David W., and Richard J. Simpson, eds. Serum/Plasma Proteomics. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2978-9.

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Serum/plasma proteomics: Methods and protocols. New York: Humana Press, 2011.

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Conrads, Thomas P. Serum Proteomics. Humana Press, 2007.

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Serum/Plasma Proteomics: Methods and Protocols. Springer, 2023.

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Simpson, Richard J., and David W. Greening. Serum/Plasma Proteomics: Methods and Protocols. Humana Press, 2016.

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Serum/Plasma Proteomics: Methods and Protocols. Humana, 2018.

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Simpson, Richard J., and David W. Greening. Serum/Plasma Proteomics: Methods and Protocols. Springer New York, 2017.

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Dave S. B. Hoon (Editor) and Bret Taback (Editor), eds. Circulating Nucleic Acids in Plasma/Serum III and Serum Proteomics (Annals of the New York Academy of Sciences). New York Academy of Sciences, 2004.

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Book chapters on the topic "Serum Proteomics"

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Govorukhina, Natalia, Peter Horvatovich, and Rainer Bischoff. "Label-Free Proteomics of Serum." In Functional Proteomics, 67–77. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-398-1_5.

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Hood, Brian L., David E. Malehorn, Thomas P. Conrads, and William L. Bigbee. "Serum Proteomics Using Mass Spectrometry." In Methods in Molecular Biology, 107–28. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-811-9_8.

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Roncada, Paola, Cristian Piras, Luigi Bonizzi, Alessio Soggiu, Michele De Canio, Romana Turk, Mislav Kovačić, Marko Samardžija, and Andrea Urbani. "Serum proteomic analysis in bovine mastitis." In Farm animal proteomics, 159–64. Wageningen: Wageningen Academic Publishers, 2012. http://dx.doi.org/10.3920/978-90-8686-751-6_38.

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Koller, Antonius, Purvi Patel, Jenny Kim Kim, and Emily I. Chen. "Proteomics Analysis of Circulating Serum Exosomes." In Methods in Molecular Biology, 213–25. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7057-5_17.

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Merrick, B. Alex. "Toxicoproteomics: Correlating Tissue and Serum Proteomics in Liver Injury." In Clinical Proteomics, 403–33. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2008. http://dx.doi.org/10.1002/9783527622153.ch24.

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Lourido, Lucía, Rocío Paz-González, Cristina Ruiz-Romero, Peter Nilsson, and Francisco J. Blanco. "Serum Proteomic Profiling in by Antibody Suspension Bead Arrays." In Shotgun Proteomics, 143–51. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1178-4_8.

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Wang, David. "Systematic Glycolytic Enzyme Activity Analysis from Human Serum with PEP Technology." In Functional Proteomics, 69–81. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8814-3_4.

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Blokland, Marco H., Klaas L. Wubs, Merel A. Nessen, Saskia S. Sterk, and Michel W. F. Nielen. "Analysis of endogenous and recombinant bovine somatotropin in serum." In Farm animal proteomics 2013, 209–12. Wageningen: Wageningen Academic Publishers, 2013. http://dx.doi.org/10.3920/978-90-8686-776-9_53.

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Soler, L., J. J. Cerón, A. Gutiérrez, C. Lecchi, A. Scarafoni, and F. Ceciliani. "Proteomic characterization of serum amyloid A protein in different porcine body fluids." In Farm animal proteomics, 106–10. Wageningen: Wageningen Academic Publishers, 2012. http://dx.doi.org/10.3920/978-90-8686-751-6_25.

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Tóthová, Csilla, Oskar Nagy, Gabriel Kováč, and Veronika Nagyová. "Serum protein electrophoretic pattern in clinically healthy calves and cows." In Farm animal proteomics 2013, 249–52. Wageningen: Wageningen Academic Publishers, 2013. http://dx.doi.org/10.3920/978-90-8686-776-9_63.

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Conference papers on the topic "Serum Proteomics"

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Santis, M. De, E. Generali, A. Ceribelli, N. Isailovic, M. Caprioli, GM Guidelli, and C. Selmi. "FRI0353 Serum proteomics profile in systemic sclerosis patients." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.5693.

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Futami, Y., Y. Takeda, T. Koba, R. Edahiro, Y. Shirai, H. Hirata, I. Nagatomo, et al. "Target Proteomics Identifies Novel Biomarkers from Serum Exosomes in Sarcoidosis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a3103.

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Remih, Katharina, Franziska-Maria Hufnagel, Valerie Durkalski-Mauldin, William Martens Lee, Zemin Su, Jody Rule, Laura Krieg, et al. "Serum proteomics to characterize adult patients with Acute Liver Failure." In 39. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag, 2023. http://dx.doi.org/10.1055/s-0042-1759931.

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Wang, L., H. Zhao, and G. Yu. "Serum Proteomics Identify Potential Biomarkers in Frequent Exacerbation of COPD." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a3332.

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Beletić, Anđjelo, Josipa Kuleš, Ivana Rubić I, Filipović Milica Kovačević, and Vladimir Mrljak. "Serum, Saliva, and Liver Proteome Indices Associated with Platelet Biology during Inflammatory Conditions in Different Animal Species." In Socratic Lectures 8. University of Lubljana Press, 2023. http://dx.doi.org/10.55295/psl.2023.i1.

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Abstract:
The understanding of platelet biology stepped out of the (patho)physiology of hemostasis long ago. Currently, platelets are acknowledged as effective sentinels against pathogens and powerful regulators of inflammatory processes. While accomplishing these tasks, their structural and physiological features undergo constant changes, often associated with the proteomics indices in the tissues and biofluids. Assessing these associations in different animal species provides a substantial comparative benefit. Nevertheless, the sine qua non for the reliable interpretation of the obtained data is a comprehensive understanding of the applied analytical and bioinformatics methods. Keywords: Tissue; Body fluids; Proteomics; Platelet biology; Animals; Infections
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Koba, T., Y. Takeda, R. Narumi, Y. Nojima, Y. N. Futami, R. Edahiro, M. N. Itoh, et al. "Targeted Proteomics of Serum Extracellular Vesicles to Identify Novel Biomarkers for COPD." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a2550.

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Szacherski, P., J. F. Giovannelli, L. Gerfault, A. Giremus, and P. Grangeat. "Robust MS serum sample classification in proteomics by the use of inverse problems." In 2012 IEEE International Workshop on Genomic Signal Processing and Statistics (GENSIPS). IEEE, 2012. http://dx.doi.org/10.1109/gensips.2012.6507761.

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Meiqun, Cao, Gui Zifan, Sun Kehuan, and Wu Zhengzhi. "Application of iTRAQ quantitative proteomics in identification of serum biomarkers in breast cancer." In 2011 4th International Conference on Biomedical Engineering and Informatics. IEEE, 2011. http://dx.doi.org/10.1109/bmei.2011.6098563.

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Abe, Y., Y. Takeda, Y. Suga, H. Hirata, T. Yokoi, T. Minami, K. Kuribayashi, T. Kijima, and A. Kumanogoh. "Identification of Novel Biomarkers for Malignant Pleural Mesothelioma by Proteomics of Serum Exosomes." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a2586.

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AlZaabi, Adhari A., Marc Hansen, and Steven Graves. "Abstract 4016: Serum proteomics uncover possible biomarkers associated with progression of metastatic breast cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4016.

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Reports on the topic "Serum Proteomics"

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Steffen, Martin A., and Agnes Bergerat. Proteomics of Peripheral Leukocytes in Patients with Elevated Serum Levels of PSA. Fort Belvoir, VA: Defense Technical Information Center, September 2012. http://dx.doi.org/10.21236/ada568607.

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