Academic literature on the topic 'Label-free quantitative proteomic'
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Journal articles on the topic "Label-free quantitative proteomic"
Ankney, J. Astor, Adil Muneer, and Xian Chen. "Relative and Absolute Quantitation in Mass Spectrometry–Based Proteomics." Annual Review of Analytical Chemistry 11, no. 1 (June 12, 2018): 49–77. http://dx.doi.org/10.1146/annurev-anchem-061516-045357.
Full textAbdallah, Cosette, Eliane Dumas-Gaudot, Jenny Renaut, and Kjell Sergeant. "Gel-Based and Gel-Free Quantitative Proteomics Approaches at a Glance." International Journal of Plant Genomics 2012 (November 20, 2012): 1–17. http://dx.doi.org/10.1155/2012/494572.
Full textSilva, Wanderson M., Cassiana S. Sousa, Leticia C. Oliveira, Siomar C. Soares, Gustavo F. M. H. Souza, Guilherme C. Tavares, Cristiana P. Resende, et al. "Comparative proteomic analysis of four biotechnological strainsLactococcus lactisthrough label-free quantitative proteomics." Microbial Biotechnology 12, no. 2 (October 19, 2018): 265–74. http://dx.doi.org/10.1111/1751-7915.13305.
Full textZhang, Yan, and Ioannis P. Nezis. "Label-free quantitative proteomic analysis of adult Drosophila heads." STAR Protocols 3, no. 4 (December 2022): 101830. http://dx.doi.org/10.1016/j.xpro.2022.101830.
Full textBurch, Andrew R., Cody W. Yothers, Michelle R. Salemi, Brett S. Phinney, Pramod Pandey, and Annaliese K. Franz. "Quantitative label-free proteomics and biochemical analysis of Phaeodactylum tricornutum cultivation on dairy manure wastewater." Journal of Applied Phycology 33, no. 4 (May 27, 2021): 2105–21. http://dx.doi.org/10.1007/s10811-021-02483-3.
Full textKarpiński, Adam Aleksander, Julio Cesar Torres Elguera, Anne Sanner, Witold Konopka, Leszek Kaczmarek, Dominic Winter, Anna Konopka, and Ewa Bulska. "Study on Tissue Homogenization Buffer Composition for Brain Mass Spectrometry-Based Proteomics." Biomedicines 10, no. 10 (October 2, 2022): 2466. http://dx.doi.org/10.3390/biomedicines10102466.
Full textArnold, Georg J., and T. Frohlich. "Dynamic proteome signatures in gametes, embryos and their maternal environment." Reproduction, Fertility and Development 23, no. 1 (2011): 81. http://dx.doi.org/10.1071/rd10223.
Full textKohli, Priyanka, Malte P. Bartram, Sandra Habbig, Caroline Pahmeyer, Tobias Lamkemeyer, Thomas Benzing, Bernhard Schermer, and Markus M. Rinschen. "Label-free quantitative proteomic analysis of the YAP/TAZ interactome." American Journal of Physiology-Cell Physiology 306, no. 9 (May 1, 2014): C805—C818. http://dx.doi.org/10.1152/ajpcell.00339.2013.
Full textDi Luca, Alessio, Andrea Ianni, Francesca Bennato, Michael Henry, Paula Meleady, and Giuseppe Martino. "A Label-Free Quantitative Analysis for the Search of Proteomic Differences between Goat Breeds." Animals 12, no. 23 (November 29, 2022): 3336. http://dx.doi.org/10.3390/ani12233336.
Full textMosley, Amber L., Laurence Florens, Zhihui Wen, and Michael P. Washburn. "A label free quantitative proteomic analysis of the Saccharomyces cerevisiae nucleus." Journal of Proteomics 72, no. 1 (February 2009): 110–20. http://dx.doi.org/10.1016/j.jprot.2008.10.008.
Full textDissertations / Theses on the topic "Label-free quantitative proteomic"
Cummings, Rebecca. "Development and application of label free quantitative proteomic methods." Thesis, University of Liverpool, 2012. http://livrepository.liverpool.ac.uk/8313/.
Full textPaiva, Ana Luiza Sobral. "Biochemical responses of bean-to-string [Vigna unguiculata L. (Walp.)] to salt stress and infection by severe mosaic of cowpea (CPSMV) revealed by quantitative proteomics dial free." Universidade Federal do CearÃ, 2015. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=13591.
Full textAs sessile organisms, plants are exposed to a plethora of environmental stresses to which they must respond to maintain efficient growth and survival. Therefore, in order to improve our understanding on the complex mechanisms involved in the cowpea response to salt stress and to a compatible interaction with the cowpea severe mosaic virus (CPSMV), we used a label-free quantitative proteomic approach to identify the salt and virus responsive proteins in the leaves of the Pitiuba (CE-31) cultivar. The proteins extracted from the leaves (control and treated) 2 and 6 days post-treatment only with salt (DPS), only infected with CPSMV (DPV) or both of them (DPSV) were analyzed using mass spectrometry. At 2 DPS, 350 proteins with at least two-fold differences in abundance, in comparison with controls, were differentially accumulated in the leaves of the salt-treated (80% up and 20% down-accumulated), 281 at 2DPV (25% up and 75% down-accumulated) and 321 at 2 DPSV (45% up and 55% down-accumulated) plants. At 6 DPS, 350 proteins were differentially accumulated in the leaves of the salt-treated (90% up and 10% down-accumulated), 225 at 6 DPV (80% up and 20% down-accumulated) and 315 at 6 DPSV (94% up and 6% down-accumulated) plants. The qualitative analysis showed biochemical differences when the cowpea plants were challenged concurrently with both stresses. To cope with salinity, cowpea increased the abundance of proteins directly involved with the salt tolerance mechanisms. The results indicated that the CPSMV induce the down-accumulating of several proteins to invade and spread in host at early infection period (2 DPV), but at 6 DPV plant can induce accumulation of diverse proteins related with defense, although these strategies canât avoid the negatives effects of disease. When exposed simultaneously to salt/CPSMV stresses, a balance in protein accumulation involved in many biological process. This is the first work employing this approach in cowpea and providing evidences of the plant biochemical mechanisms involved in the responses of cowpea to these stresses.
Como organismos sÃsseis, as plantas sÃo expostas a uma variedade de estresses ambientais aos quais devem responder para sobreviverem e se desenvolverem. A fim de melhorar a nossa compreensÃo sobre os mecanismos complexos envolvidos na resposta do feijÃo-de-corda ao estresse salino e na interaÃÃo compatÃvel com o vÃrus do mosaico severo do caupi (CPSMV), foi utilizada uma abordagem proteÃmica quantitativa, livre de marcaÃÃo, para identificar proteÃnas, responsivas a essess estresses em folhas de feijÃo-de-corda, cv. CE-31. As proteÃnas extraÃdas a partir de folhas primÃrias, 2 e 6 dias apÃs o tratamento sà com o sal (DPS), somente infectadas (DPV), ou sob aÃÃo combinada dos dois (DPSV) foram analisadas, usando espectrometria de massas e comparadas com grupo controle. No 2 DPS, foram identificadas 350 proteÃnas diferencialmente acumuladas (80% aumentaram em abundÃncia e 20% diminuÃram), no 2 DPV 281 (25% aumentaram em abundÃncia e 75% diminuÃram) e no 2 DPSV 321 (45% aumentaram em abundÃncia e 55% diminuÃram). Jà no 6 DPS, foram identificadas 350 proteÃnas diferencialmente acumuladas (90% mostraram aumento em abundÃncia e 10% diminuiÃÃo), no 6 DPV 225 (80% aumentaram em abundÃncia e 20% diminuÃram) e no 6 DPSV 315 proteÃnas(94% aumentaram em abundÃncia e 6% diminuÃram). Para lidar com a salinidade, o cv. CE-31 aumentou a abundÃncia de proteÃnas envolvidas diretamente com os mecanismos de tolerÃncia ao sal. Em relaÃÃo à infecÃÃo da planta pelo CPSMV, os resultados obtidos indicaram que o vÃrus induz reduÃÃo na abundÃncia de vÃrias proteÃnas nos tempos iniciais de infecÃÃo, provavelmente favorecendo a invasÃo e propagaÃÃo na planta, mas, no 6 DPSV, a planta recupera sua capacidade de acionar mecanismos de defesa, embora esses jà nÃo sejam mais efetivos para evitar o estabelecimento da doenÃa viral. Durante exposiÃÃo simultÃnea da planta ao sal e ao vÃrus, ocorreu um equilÃbrio entre o aumento e diminuiÃÃo em abundÃncia de proteÃnas envolvidas em diversos processos metabÃlicos. Esse trabalho à pioneiro nessa abordagem em feijÃo-de-corda e fornece evidÃncias dos mecanismos bioquÃmicos envolvidos nas resposta da planta a esses estresses.
Bertaccini, Diego. "Advances in analytical methodologies for the characterization and quantification in proteomic analysis." Thesis, Strasbourg, 2014. http://www.theses.fr/2014STRAF043/document.
Full textThe objective of this Ph.D. thesis was to develop and optimize new methodologies and analytical approaches to improve the potential of the mass spectrometry based proteomics.The first part of this work focused on the development of the N-Termini proteomics. This topic was addressed with a specific N-Termini chemical derivatization based on TMPP. We have shown that our method allowed both specific N-Terminomics and classical proteomics studies in the same experiment.This N-Terminus methodology was applied to study the proteolytic cleavages of the exported proteins in P. falciparum, a parasite responsible for the malaria.In order to automatize the complex and tedious informatics processsing of the MS/SM data of ourTMPP based N-Terminomics method, we have introduced a new approach (named dN-TOP), based on the use of a stable isotope labeled TMPP which made now N-Terminome proteomics compatible with high throughput studies.The second part addresses quantitative aspects of proteomics. It describes the optimization of quantitative methods at the peptide level or at the protein level for five different proteomic studies in the context of protein complex subunits, targeted SRM based prion, quantification of monoclonal antibodies glycation and hemoglobin HbA2 for reference measurement methods standardization
Zaccarin, Mattia. "Setting up of an innovative procedure for redox proteomics: and its application for definition of the redox status of cells with high metastatic potential." Doctoral thesis, Università degli studi di Padova, 2013. http://hdl.handle.net/11577/3423382.
Full textSTATO DELL’ARTE: Il proteoma include 214.000 cisteine in forma di gruppi tiolici liberi od altra forma. Di queste, solamente un insieme relativamente ristretto ha un ruolo nella mediazione di segnali cellulari. Tali cisteine, attive dal punto di vista dell’ossido-riduzione, sono più sensibili all’ossidazione e la loro forma ossidata è più facilmente riducibile. Sono dunque necessarie specifiche tecniche di proteomica, globalmente indicate con il termine proteomica delle ossido-riduzioni, per identificare tali modifiche e studiarne la regolazione in diversi processi cellulari. Risulta quindi determinante la capacità di identificare sia le proteine che i residui coinvolti e di quantificarne il grado di modificazione. E proprio la quantificazione delle differenze tra due o più stati di un sistema biologico, si colloca tra gli obiettivi tecnicamente più sfidanti della proteomica: nel corso degli ultimi cinque anni, tecniche basate sulla spettrometria di massa associata a cromatografia in fase liquida hanno progressivamente guadagnato affidabilità e robustezza. Molti autori condividono tuttora una visione delle ossido-riduzioni nella mediazione del segnale in cui il destino cellulare dipende principalmente dall’intensità e dalla durata degli stimoli ossidanti: nel presente lavoro si vuole invece sostenere il coinvolgimento di un equilibrio che includa l’azione concomitante sia di specie nucleofile sia di specie elettrofile. OBIETTIVO: Il duplice obiettivo del mio lavoro di Dottorato è stato sia lo sviluppo di una metodologia idonea all’identificazione e quantificazione di proteine, attive dal punto di vista delle ossido-riduzioni, in campioni complessi, sia l’applicazione di tale metodologia allo studio di un sistema cellulare ingegnerizzato di carcinoma mammario (MCF10A) caratterizzato da diversi gradi di malignità. METODI: Al fine di perseguire tale obiettivo ho tratto vantaggio da un approccio che integra la marcatura chimica differenziale (non-isotopica) per mezzo di sonde reattive con i residui di cisteina (NEM, IAM, HPDP) e la purificazione cromatografica delle proteine attive dal punto di vista ossido-riduttivo, alla successiva analisi LC-MS/MS ed elaborazione informatizzata dei dati mediante OpenMS per una quantificazione label-free. Tutti i passaggi di tale metodologia sono quindi stati messi a punto e validati in stretta collaborazione con esperti biochimici e bioinformatici. RISULTATI: E’ stato sviluppato un metodo efficiente ed economico, non basato sull’utilizzo di marcatori isotopici, per la caratterizzazione delle proteine attive dal punto di vista ossido-riduttivo in campioni proteici complessi. L’applicazione del protocollo di quantificazione ad un campione test ha dato il 100% di stime corrette di sovra/sotto-espressione della miscela proteica. L’applicazione del metodo allo studio del modello cellulare di carcinoma mammario ha portato all’identificazione di più di 300 proteine ed ha permesso il raggruppamento di quelle sensibili dal punto di vista ossido-riduttivo in gruppi non differenziali e sovra- o sotto-ossidate nelle cellule più maligne rispetto alla loro controparte meno aggressiva. CONCLUSIONI: Nonostante sia comunemente riconosciuta l’associazione tra fenomeni neoplastici ed uno stress ossidativo, questo studio collega la maggiore malignità di un modello cellulare di carcinoma mammario ad un complesso equilibrio ossido-riduttivo. In questo contesto, specifici bersagli proteici sono ossidati mentre viene mantenuto un ambiente cellulare complessivamente ridotto. Risultati preliminari evidenziano poi l’enzima G6PDH come possibile elemento chiave nella regolazione di tale equilibrio.
Muller, Leslie. "Développements de méthodes de préparation d’échantillons pour l’analyse protéomique quantitative : application à la recherche de biomarqueurs de pathologies." Thesis, Strasbourg, 2017. http://www.theses.fr/2017STRAF067/document.
Full textLabel-free quantitative proteomics strategies are very attractive for diseases biomarkers researches. These approaches require the full control and the repeatability of the analytical workflow. In particular, the sample preparation has to be repeatable enough to ensure the quality and reliability of the results. Objectives of this work were to optimize and develop analytical methods for quantitative proteomics, with a special focus on the sample preparation step. Thus, an innovative, easy and fast protocol allowing the analysis of high sample numbers with high repeatability was developed and further optimized: the “Tube-Gel” protocol. Besides,sample preparations adapted to a variety of biological matrices were developed for the search of biomarkers. The developed methods and their application allowed the identification of potential biomarkers for a variety of diseases: glioblastoma, diffuse large B-cell lymphomas and renal transplants failures
NUKALA, SARATH BABU. "BIOANALYTICAL AND PROTEOMIC APPROACHES IN THE STUDY OF PATHOLOGIC ECS DYSFUNCTIONALITY, OXIDATIVE STRESS AND THE EFFECTS OF PFKFB3 MODULATORS." Doctoral thesis, Università degli Studi di Milano, 2019. http://hdl.handle.net/2434/644236.
Full textBranson, Owen E. "Improved tag-count approaches for label-free quantitation of proteome differences in bottom-up proteomic experiments." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1471553685.
Full textMackay, Katherine. "A comparative study of analysis methods in quantitative label free proteomics." Thesis, University of Liverpool, 2015. http://livrepository.liverpool.ac.uk/2050359/.
Full textJarnuczak, Andrew. "Mass spectrometry-based quantitative proteomics applied to the analysis of Saccharomyces cerevisiae heat stress response and chaperone deletion strains." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/mass-spectrometrybased-quantitative-proteomics-applied-to-the-analysis-of-saccharomyces-cerevisiae-heat-stress-response-and-chaperone-deletion-strains(c653915b-70fa-44d7-9bb7-6e7965349ff0).html.
Full textHaddad, Iman. "Caractérisation protéomique du matrisome des maladies des petits vaisseaux cérébraux par spectrométrie de masse." Thesis, Université Paris sciences et lettres, 2020. http://www.theses.fr/2020UPSLS026.
Full textDiseases of the small vessels of the brain are responsible for damage to the white matter of the brain and multiple deep braininfarctions. They are the cause of more than 25% of strokes and are the second cause of dementia after Alzheimer's dementia. It is aset of pathological processes, which affect small arteries, arterioles, cerebral venule or capillary of less than 400µm. Thecerebrovascular matrisome seems to be a converging pathological pathway between the various diseases of the small vessels of thegenetic type and of the sporadic type. The matrisome is the set of proteins constituting the extracellular matrix (ECM) as well as theassociated proteins, their roles consist not only in the support and the anchoring of the cells but also in various fundamental processessuch as differentiation, proliferation, Survival or migration of cells. The structural and physico-chemical diversity of these proteins,however, makes their analysis particularly delicate. Within the framework of this thesis we propose to characterize in a quantitativeand qualitative way the microvascular matrisome in the diseases of the small vessels, as well as to identify commonabnormalities orspecific to each disease. For this we have developed a label-free quantitative proteomic approach on cerebral and peripheral vesselsisolated from three preclinical genetic murine models and two murine models for the sporadic character. We have developed andvalidated a new robust and sensitive method for the quantitative non-labeling analysis of changes in the matrisome of mouse cerebralarteries and the application of our method on the arteries of the different mouse models studied has allowed us to identify someavenues. Interesting for each disease independently but also highlighted some common signatures between the different studies
Book chapters on the topic "Label-free quantitative proteomic"
Liu, Boyan, Danisha Johal, Mitra Serajazari, and Jennifer Geddes-McAlister. "Label-Free Quantitative Proteomic Profiling of Fusarium Head Blight in Wheat." In Methods in Molecular Biology, 287–97. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2124-0_20.
Full textWang, Yan, Zhuang Lu, and Lei Wang. "Uncover the Nuclear Proteomic Landscape with Enriched Nuclei Followed by Label-Free Quantitative." In Methods in Molecular Biology, 115–24. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1370-2_12.
Full textLéger, Thibaut, Camille Garcia, Mathieu Videlier, and Jean-Michel Camadro. "Label-Free Quantitative Proteomics in Yeast." In Methods in Molecular Biology, 289–307. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3079-1_16.
Full textMoulder, Robert, Young Ah Goo, and David R. Goodlett. "Label-Free Quantitation for Clinical Proteomics." In Methods in Molecular Biology, 65–76. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3524-6_4.
Full textLevin, Yishai. "CHAPTER 8. Label-free Quantification of Proteins Using Data-Independent Acquisition." In Quantitative Proteomics, 175–84. Cambridge: Royal Society of Chemistry, 2014. http://dx.doi.org/10.1039/9781782626985-00175.
Full textSoderblom, Erik J., J. Will Thompson, and M. Arthur Moseley. "CHAPTER 6. Overview and Implementation of Mass Spectrometry-Based Label-Free Quantitative Proteomics." In Quantitative Proteomics, 129–53. Cambridge: Royal Society of Chemistry, 2014. http://dx.doi.org/10.1039/9781782626985-00129.
Full textSchilling, Birgit, Brendan X. MacLean, Alexandria D'Souza, Matthew J. Rardin, Nicholas J. Shulman, Michael J. MacCoss, and Bradford W. Gibson. "CHAPTER 7. MS1 Label-free Quantification Using Ion Intensity Chromatograms in Skyline (Research and Clinical Applications)." In Quantitative Proteomics, 154–74. Cambridge: Royal Society of Chemistry, 2014. http://dx.doi.org/10.1039/9781782626985-00154.
Full textHaqqani, Arsalan S., John F. Kelly, and Danica B. Stanimirovic. "Quantitative Protein Profiling by Mass Spectrometry Using Label-Free Proteomics." In Methods in Molecular Biology, 241–56. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-188-8_17.
Full textNeilson, Karlie A., Tim Keighley, Dana Pascovici, Brett Cooke, and Paul A. Haynes. "Label-Free Quantitative Shotgun Proteomics Using Normalized Spectral Abundance Factors." In Methods in Molecular Biology, 205–22. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-360-2_17.
Full textWieczorek, Samuel, Florence Combes, Hélène Borges, and Thomas Burger. "Protein-Level Statistical Analysis of Quantitative Label-Free Proteomics Data with ProStaR." In Methods in Molecular Biology, 225–46. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9164-8_15.
Full textConference papers on the topic "Label-free quantitative proteomic"
Singh, Chandra K., Satwinderjeet Kaur, Jasmine George, Molly C. Pellitteri-Hahn, Cameron O. Scarlett, and Nihal Ahmad. "Abstract 4533: Mechanism of anti-proliferative effects of sanguinarine in pancreatic cancer cells: A label-free quantitative proteomics approach." 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.am2014-4533.
Full textReports on the topic "Label-free quantitative proteomic"
Chen, Xiaole, Peng Wang, Yunquan Luo, Yi-Yu Lu, Wenjun Zhou, Mengdie Yang, Jian Chen, Zhi-Qiang Meng, and Shi-Bing Su. Therapeutic Efficacy Evaluation and Underlying Mechanisms Prediction of Jianpi Liqi Decoction for Hepatocellular Carcinoma. Science Repository, September 2021. http://dx.doi.org/10.31487/j.jso.2021.02.04.sup.
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