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Relevant bibliographies by topics / Histones Liquid chromatography

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Academic literature on the topic 'Histones Liquid chromatography'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Histones Liquid chromatography"

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Su, Xiaodan, Naduparambil K. Jacob, Ravindra Amunugama, David M. Lucas, Amy R. Knapp, Chen Ren, Melanie E. Davis, et al. "Liquid chromatography mass spectrometry profiling of histones." Journal of Chromatography B 850, no. 1-2 (May 2007): 440–54. http://dx.doi.org/10.1016/j.jchromb.2006.12.037.

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Lindner, Herbert, Bettina Sarg, Christoph Meraner, and Wilfried Helliger. "Separation of acetylated core histones by hydrophilic-interaction liquid chromatography." Journal of Chromatography A 743, no. 1 (August 1996): 137–44. http://dx.doi.org/10.1016/0021-9673(96)00131-8.

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Rezinciuc, Svetlana, Zhixin Tian, Si Wu, Shawna Hengel, Ljiljana Pasa-Tolic, and Heather S. Smallwood. "Mapping Influenza-Induced Posttranslational Modifications on Histones from CD8+ T Cells." Viruses 12, no. 12 (December 8, 2020): 1409. http://dx.doi.org/10.3390/v12121409.

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T cell function is determined by transcriptional networks that are regulated by epigenetic programming via posttranslational modifications (PTMs) to histone proteins and DNA. Bottom-up mass spectrometry (MS) can identify histone PTMs, whereas intact protein analysis by MS can detect species missed by bottom-up approaches. We used a novel approach of online two-dimensional liquid chromatography-tandem MS with high-resolution reversed-phase liquid chromatography (RPLC), alternating electron transfer dissociation (ETD) and collision-induced dissociation (CID) on precursor ions to maximize fragmentation of uniquely modified species. The first online RPLC separation sorted histone families, then RPLC or weak cation exchange hydrophilic interaction liquid chromatography (WCX-HILIC) separated species heavily clad in PTMs. Tentative identifications were assigned by matching proteoform masses to predicted theoretical masses that were verified with tandem MS. We used this innovative approach for histone-intact protein PTM mapping (HiPTMap) to identify and quantify proteoforms purified from CD8 T cells after in vivo influenza infection. Activation significantly altered PTMs following influenza infection, histone maps changed as T cells migrated to the site of infection, and T cells responding to secondary infections had significantly more transcription enhancing modifications. Thus, HiPTMap identified and quantified proteoforms and determined changes in CD8 T cell histone PTMs over the course of infection.

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Ausió, Juan, and Susan C. Moore. "Reconstitution of Chromatin Complexes from High-Performance Liquid Chromatography-Purified Histones." Methods 15, no. 4 (August 1998): 333–42. http://dx.doi.org/10.1006/meth.1998.0637.

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Zhang, Kangling, and Hui Tang. "Analysis of core histones by liquid chromatography–mass spectrometry and peptide mapping." Journal of Chromatography B 783, no. 1 (January 2003): 173–79. http://dx.doi.org/10.1016/s1570-0232(02)00631-1.

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Lindner, H., W. Helliger, S. Hauptlorenz, and B. Puschendorf. "Separation and isolation of chicken erythrocyte histones by high-performance liquid chromatography." Fresenius' Zeitschrift für analytische Chemie 327, no. 1 (January 1987): 36. http://dx.doi.org/10.1007/bf00474548.

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Kurokawa, Masahiko, and Michael C. MacLeod. "Separation of histones by reverse-phase high-performance liquid chromatography: Analysis of the binding of carcinogens to histones." Analytical Biochemistry 144, no. 1 (January 1985): 47–54. http://dx.doi.org/10.1016/0003-2697(85)90082-x.

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Abrams, Simon Timothy, Dunhao Su, Yasmina Sahraoui, Yasir Alhamdi, Guozheng Wang, and Cheng Hock Toh. "Histones Bind Prothrombin to Generate Alternative Prothrombinase Complexes That Can Disseminate Intravascular Coagulation." Blood 132, Supplement 1 (November 29, 2018): 218. http://dx.doi.org/10.1182/blood-2018-99-116117.

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Abstract Background: Increased thrombin generation in vivo is pivotal to the development of disseminated intravascular coagulation (DIC). Typically, thrombin is generated when the prothrombinase complex, composed of activated factor X (FXa), activated co-factor V (FVa) and phospholipids, cleaves prothrombin in the presence of calcium. In critical illness, extensive cell death releases histones into the circulation, which can increase thrombin generation. However, the underlying pathophysiological mechanisms remains to be fully elucidated. Methods: In vitro: Isolation of histone-binding proteins with mass spectrometry analysis. Surface plasmon resonance binding studies, prothrombin cleavage and thrombin generation assays. In vivo: histone infusion mouse models (C57BL/6 mice) with or without prothrombin fragment F1+F2 infusion. Clinical: a prospective cohort of 129 adult intensive care unit patients (ICU) with sepsis and analysed for DIC. Results: Histone-conjugated Sepharose beads were used to pull down proteins from human plasma. Histone-binding proteins were subjected to 2D gel electrophoresis and sequenced by liquid chromatography-mass spectrometry. Prothrombin was the only coagulation factor identified. Histones directly bind to prothrombin (H3 [Kd = 6.8 x 107 M] and H4 [Kd = 7.0 x 107 M]), specifically prothrombin fragments F1+F2, to facilitate FXa-induced prothrombin cleavage and thrombin generation (H4 [12.25 ± 1.25 fold] and H3 [8.82 ± 0.67 fold]). FXa levels are the limiting factor of histone-enhanced thrombin generation since this process was inhibited in FX-deficient plasma unless exogenous FXa was added. Specifically, using either heparin or anti-histone antibodies to block histones, histone-prothrombin interactions, prothrombin cleavage and subsequent thrombin generation were significantly reduced. Unlike FVa which requires a phospholipid surface to form functional prothrombinase complexes, histones can substitute for FVa in the absence of phospholipids. The addition of histones to FV-deficient plasma restored thrombin generation, suggesting that histones can bypass FVa to induce thrombin generation. In vivo, infusion of histones into mice caused significant decreases in platelet counts and fibrinogen levels with elevations in thrombin-antithrombin complexes, D-dimer and prothrombin time in a dose-dependent manner. Pathological examination indicated intravascular thrombi with various organs, particularly in within lung tissues. These histone-induced DIC changes were significantly abrogated when prothrombin fragments F1+F2 were infused prior to histones to act as a decoy for binding of histones to circulating prothrombin. Analysis of DIC scores in ICU patients (n=129) with sepsis showed circulating histone levels to strongly correlate with DIC scores (r=0.446, p<0.0001). Conclusions: Histones can replace FVa in prothrombinase and not require phospholipid surfaces. This alternative histone-assembled prothrombinase can explain how thrombin could be generated and amplified away from cell surfaces to cause systemic dissemination of its effects and potentiate DIC. This study also identifies circulating histones as a potential target for therapeutic intervention in reducing DIC development and subsequent multi-organ failure in ICU patients. Disclosures No relevant conflicts of interest to declare.

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Lindner, Herbert, Bettina Sarg, and Wilfried Helliger. "Application of hydrophilic-interaction liquid chromatography to the separation of phosphorylated H1 histones." Journal of Chromatography A 782, no. 1 (October 1997): 55–62. http://dx.doi.org/10.1016/s0021-9673(97)00468-8.

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Lindner, Herbert, Wilfried Helliger, and Bernd Puschendorf. "Rapid separation of histones by high-performance liquid chromatography on C4 reversed-phase columns." Journal of Chromatography A 357 (January 1986): 301–10. http://dx.doi.org/10.1016/s0021-9673(01)95832-7.

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Dissertations / Theses on the topic "Histones Liquid chromatography"

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Su, Xiaodan. "Characterization of histones and their post-translational modifications using reversed-phase high performance liquid chromatography and mass spectrometry." Columbus, Ohio : Ohio State University, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1155687874.

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Su, Xiaodan M. S. "Characterization of histones and their post-translational modifications using reversed-phse high performance liquid chromatography and mass spectrometry." The Ohio State University, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=osu1155687874.

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Meade, Mitchell L. "Characterization of chromatin by use of high performance liquid chromatography-tandem mass spectrometry for insights into the epigenetics of cancer." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1190132832.

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Loik, Nikita D. "Development and application of methods for qualitative and quantitative analysis of amino acid post-translational modifications using liquid chromatography coupled to mass spectrometry." Thesis, University of Oxford, 2014. http://ora.ox.ac.uk/objects/uuid:8c737f3c-b24d-437d-abac-bada61351173.

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The 2-oxoglutarate and ferrous ion dependent oxygenases are a super family of enzymes that are involved in a wide range of biological processes regulated trough the mechanism of post-translational modification (PTM). Such biological processes include hypoxia sensing (through regulating HIF transcription), fatty acid metabolism (through carnitine production), transcriptional regulation (through demethylation of histones), and collagen structure formation (through proline and lysine hydroxylation). To understand the underlying mechanisms of such regulatory processes, and to develop clinically useful inhibitors, and thereby regulate these processes in living organisms, requires sensitive methods for monitoring enzyme activity. The use of indirect methods such as quantification of reaction products (14CO2 or succinate) can be problematic, as both products can result from competitive reactions. Alternative direct measurement of substrate modifications using mass spectrometry-based proteomics can be applied; however, (1) for this technique the limit of detection is often prohibitive, (2) the method is best suited for the confirmation of known modifications, rather than for the discovery of new modifications, and (3) sequence coverage may often be only 60%, and therefore many modifications can be missed. The aim of the research presented in this thesis was to develop amino acid analysis and to apply these methods to the identification and quantification of PTMs catalysed by 2-oxoglutarate and ferrous ion dependent oxygenases. A range of LC-MS approaches were investigated including: (1) C18 reversed phase chromatography of quinoline derivatised amino acids, (2) ion paring chromatography, and (3) mixed mode chromatography with either UV, or conventional molecular MS, or isotope ratio mass spectrometry detection. Analysis of the elution patterns for those separation techniques enabled estimation of the retention parameters of modified amino acids and the identification of the modifications, where no standards were available. The most sensitive approach developed employed mixed mode chromatography coupled to isotope ratio mass spectrometry which was optimised for the analysis of modified amino acids. This was shown to have a limit of detection two orders of magnitude lower (0.01μM) than other conventional mass spectrometry techniques. Using amino acid labelling in cell culture, a quantification protocol was developed which employed a non-labelled internal standard and selectively labelled cell culture. The method was shown to be suitable for both very accurate quantification at low concentration levels and metabolic studies, allowing us to track back the modifications to their precursors. The analytical methods developed for amino acid analysis were successfully applied to the analysis of modifications resulting from 2-oxoglutarate and Fe dependent oxygenase activity. Stereochemistry of lysyl hydroxylation in the splicing regulatory protein Luk7L2 by JmjD6 as well as of the self hydroxylation of the JmjD6 was identified. The stereochemistry was shown to be different from that of previously reported for the collagen hydroxyline, hydroxylated by the another member of this enzyme family. mbP4H enzyme was shown to catalyse prolyl hydroxylation of taODD resulting in 4R-hydroxyprolyl. Amino acid analysis was used in order to verify the mechanism of the hBBOX catalysed rearrangement of Mildronate. Using the method developed for the analysis of non-derivatised amino acids the screening of potential substrates of hBBOX enzyme was carried out and two new substrates were identified. The isotope ratio mass spectrometry protocol was applied to the study of histones from cell culture; low levels of hydroxylated and methylated amino acids were quantified. The analytical methods described were developed to complement to the well established proteomics techniques. The methods developed enable investigation into the region- and stereo- chemistry of the modified groups within the modified AA residue and has proved to be a powerful tool of exploratory PTM analysis.

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Bilgraer, Raphaël. "Déchiffrer le code histone : épigénétique et toxicologie placentaire." Thesis, Paris 5, 2014. http://www.theses.fr/2014PA05P627/document.

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En influençant le degré de compaction de la chromatine ainsi que ses interactions avec différents partenaires protéiques, les modifications post-traductionnelles des histones sont impliquées dans la régulation de l’expression des gènes. Avec les différents variants d’histones incorporés dans la chromatine, ces modifications dynamiques et sensibles à l’environnement sont constitutives du code histone. Ce travail présente une approche globale de criblage baptisée approche histonomique, visant à révéler une perturbation épigénétique à l’échelle des histones. Cette approche originale offre une comparaison rapide et fiable des abondances relatives des variants d’histones et de leurs modifications post-traductionnelles dans des cellules humaines en une seule analyse LC-MS. Comme preuve de concept, des cellules BeWo issues de choriocarcinome humain ont été exposées au butyrate de sodium, un inhibiteur non spécifique d’histones désacétylases. Les histones extraites des échantillons témoins ou traités au butyrate de sodium à 1 ou 2,5 mM ont été analysées par chromatographie liquide ultra performante couplée à un spectromètre de masse de type Q-TOF. Les analyses statistiques multivariées ont permis de discriminer les échantillons témoins des échantillons traités sur la base des différences de degrés d’acétylation observés sur plusieurs formes d’histones. La même approche a ensuite été appliquée à des cellules exposées au B[a]P à 1 μM et a révélé deux principaux marqueurs caractéristiques d’un remodelage de la chromatine induit par les effets génotoxiques duB[a]P. En résumé, cette approche histonomique globale pourrait se révéler être un outil complémentaire très utile pour explorer une potentielle perturbation du code histone lors d’exposition à des xénobiotiques environnementaux
While acting upon chromatin compaction, histone post-translational modifications (PTMs) are involved in modulating gene expression through histone–DNA affinity and protein–protein interactions. These dynamic and environment-sensitive modifications are constitutive of the histone code that reflects the transient transcriptional state of the chromatin. Here we describe a global screening approach for revealing epigenetic disruption at the histone level. This original approach enables fast and reliable relative abundance comparison of histone PTMs and variants in human cells within a single LC-MS experiment. As a proof of concept, we exposed BeWo human choriocarcinoma cells to sodium butyrate (SB), a universal histone deacetylase (HDAC) inhibitor. Histone acide xtracts equally representing 3 distinct classes, Control, 1 mM and 2.5 mM SB, we reanalyzed using ultra-performance liquid chromatography coupled with a hybrid quadrupoletime-of-flight mass spectrometer (UPLC-QTOF-MS). Multivariate statistics allowed us to discriminate control from treated samples based on differences in the acetylation level of several histone forms. We then applied the same procedure to cells treated with 1 μMB[a]P and suceeded in revealing two markers of chromatin remodeling in relation withgenotoxic properties of B[a]P. Indeed, this untargeted histonomic approach could be auseful exploratory tool in many cases of environmental xenobiotic exposure when histone code disruption is suspected

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Zhang, Liwen. "Characterization of histone post-translational modification using reversed-phase high performance liquid chromatography and fourier transform ion cyclotron resonance mass spectrometry." Connect to this title online, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1054660495.

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Thesis (Ph. D.)--Ohio State University, 2003.
Title from first page of PDF file. Document formatted into pages; contains xv, 219 p.; also includes graphics (some col.) Includes bibliographical references (p. 147-173). Available online via OhioLINK's ETD Center

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Tchouatcha, Tchouassom Jeanne-Chantal. "Isolement et caractérisation de variants de l'histone H1 du foie de rat." Lyon 1, 1988. http://www.theses.fr/1988LYO10167.

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Un melange d'histone h1 extraites du foie de rat est fractionne par hplc en phase inverse. Une histone h#o et cinq sous-fractions d'histones h1-1 sont obtenues sous forme pure. La composition en acides amines est determinee; la structure est caracterisee par degradation enzymatique, renaturation in vitro, electrophorese, fluorence intrinseque

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Bin, Saeedan Abdulaziz S. A. "The role of MMP10 in non-small cell Lung cancer, and pharmacological evaluation of its potential as a target for therapeutic intervention. Investigation of the role of MMP10 in the tumour microenvironment of non-small cell lung cancer using gene, protein and mass spectrometry approaches to determine MMP10’s potential in drug development strategies." Thesis, University of Bradford, 2014. http://hdl.handle.net/10454/14070.

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Non-Small Cell Lung Cancer (NSCLC), which accounts for 80% of all lung cancer cases, is associated with resistance to chemotherapy and poor prognosis. Exploitation of NSCLC-upregulated pathways that can either be targeted by novel therapeutics or used to improve the tumour-delivery of current chemotherapeutics are required. Among the matrix metalloproteinases (MMPs) that are essential for tumour development, MMP10 is a potential candidate as a therapeutic target based on its expression and contribution to NSCLC development. This research aims to explore the expression and functions of MMP10 in the tumour microenvironment of NSCLC and evaluate the potential of MMP10 as a target for therapeutic intervention. Herein, MMP10 expression at gene and protein levels were analysed in a panel of NSCLC cell lines using RT-PCR and Western blotting analysis. To determine MMP10 functional relevance, an in vitro angiogenesis assay using cell conditioned media was carried out. To identify specific peptide sequences for the design of prodrugs rationalised to be MMP10 activated, in vitro substrate cleavage studies were performed using a mass spectrometry approach to differentiate between MMP10 and the structurally similar MMP3. This study demonstrates that MMP10 is highly expressed in NSCLC and that high levels of MMP10 are associated with induction of angiogenesis, a crucial process supporting tumour growth. In addition to the achievement of having been able to differentiate between closely similar MMP3 and MMP10 through carefully monitoring the hydrolysis rate of compound 444259 (a known MMP substrate), data generated herein provides the basis for further studies to exploit MMP10 as a prodrug-activator.
Full text was made available at the end of the embargo period, 12th Dec 2019

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Bin, Saeedan Abdulaziz Saad Abdulaziz. "The role of MMP10 in non-small cell lung cancer, and pharmacological evaluation of its potential as a target for therapeutic intervention : investigation of the role of MMP10 in the tumour microenvironment of non-small cell lung cancer using gene, protein and mass spectrometry approaches to determine MMP10's potential in drug development strategies." Thesis, University of Bradford, 2014. http://hdl.handle.net/10454/14070.

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Ghitun, Mihaela. "Module microfluidique intégrant des séparations multidimensionnelles : applications d'analyses protéomiques sur des extraits cellulaires." Thèse, 2006. http://hdl.handle.net/1866/17982.

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Book chapters on the topic "Histones Liquid chromatography"

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Cao, Xing-Jun, Barry M. Zee, and Benjamin A. Garcia. "Heavy Methyl-SILAC Labeling Coupled with Liquid Chromatography and High-Resolution Mass Spectrometry to Study the Dynamics of Site-Specific Histone Methylation." In Methods in Molecular Biology, 299–313. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-284-1_24.

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