Academic literature on the topic 'Post translational modification (PTM)'
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Journal articles on the topic "Post translational modification (PTM)"
Urasaki, Yasuyo, and Thuc T. Le. "Differentiation of Essential Oils Using Nanofluidic Protein Post-Translational Modification Profiling." Molecules 24, no. 13 (June 27, 2019): 2383. http://dx.doi.org/10.3390/molecules24132383.
Full textWang, Duolin, Yanchun Liang, and Dong Xu. "Capsule network for protein post-translational modification site prediction." Bioinformatics 35, no. 14 (December 6, 2018): 2386–94. http://dx.doi.org/10.1093/bioinformatics/bty977.
Full textHernandez-Valladares, Maria, Rebecca Wangen, Frode S. Berven, and Astrid Guldbrandsen. "Protein Post-Translational Modification Crosstalk in Acute Myeloid Leukemia Calls for Action." Current Medicinal Chemistry 26, no. 28 (October 25, 2019): 5317–37. http://dx.doi.org/10.2174/0929867326666190503164004.
Full textPascovici, Dana, Jemma X. Wu, Matthew J. McKay, Chitra Joseph, Zainab Noor, Karthik Kamath, Yunqi Wu, Shoba Ranganathan, Vivek Gupta, and Mehdi Mirzaei. "Clinically Relevant Post-Translational Modification Analyses—Maturing Workflows and Bioinformatics Tools." International Journal of Molecular Sciences 20, no. 1 (December 20, 2018): 16. http://dx.doi.org/10.3390/ijms20010016.
Full textDunphy, Katie, Paul Dowling, Despina Bazou, and Peter O’Gorman. "Current Methods of Post-Translational Modification Analysis and Their Applications in Blood Cancers." Cancers 13, no. 8 (April 16, 2021): 1930. http://dx.doi.org/10.3390/cancers13081930.
Full textWang, BingHua, Minghui Wang, and Ao Li. "Prediction of post-translational modification sites using multiple kernel support vector machine." PeerJ 5 (April 27, 2017): e3261. http://dx.doi.org/10.7717/peerj.3261.
Full textChen, Zhen, Xuhan Liu, Fuyi Li, Chen Li, Tatiana Marquez-Lago, André Leier, Tatsuya Akutsu, et al. "Large-scale comparative assessment of computational predictors for lysine post-translational modification sites." Briefings in Bioinformatics 20, no. 6 (October 4, 2018): 2267–90. http://dx.doi.org/10.1093/bib/bby089.
Full textYang, Tangpo, Zheng Liu, and Xiang David Li. "Developing diazirine-based chemical probes to identify histone modification ‘readers’ and ‘erasers’." Chemical Science 6, no. 2 (2015): 1011–17. http://dx.doi.org/10.1039/c4sc02328e.
Full textMalik, Arshi, Sarah Afaq, Afaf S. Alwabli, and Khalid Al-ghmady. "Networking of predicted post-translational modification (PTM) sites in human EGFR." Bioinformation 15, no. 7 (July 31, 2019): 448–54. http://dx.doi.org/10.6026/97320630015448.
Full textArntzen, Magnus Ø., Christoffer Leif Osland, Christopher Rasch-Olsen Raa, Reidun Kopperud, Stein-Ove Døskeland, Aurélia E. Lewis, and Clive S. D'Santos. "POSTMan (POST-translational modification analysis), a software application for PTM discovery." PROTEOMICS 9, no. 5 (March 2009): 1400–1406. http://dx.doi.org/10.1002/pmic.200800500.
Full textDissertations / Theses on the topic "Post translational modification (PTM)"
Dumont, Quentin. "Applications of Ion Mobility Mass Spectrometry - Screening for SUMOylation and Other Post-Translational Modifications." University of Toledo / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1345130293.
Full textMatsumiya, Nozomi. "Optimization of disulfide mapping using mass spectrometry." Thesis, Kansas State University, 2009. http://hdl.handle.net/2097/1358.
Full textBiochemistry
John Tomich
One of the important keys to characterize the biological function of a protein is the study of post-translational modification (PTM). Formation of disulfide bond linkages between cysteine residues within a protein is a common PTM which not only contributes to folding and stabilizing the protein structure, but also to accomplishing its native function. Therefore, the study and discovery of structural-functional relationships of expressed proteins using an isolated proteomics approach has been one of the biggest advances within the field of structural biology in recent years. In this study, rapid disulfide bond mapping of freshly obtained equine serum albumin (ESA) was performed using matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS). Highly sensitive MALDI-TOF MS is commonly used for the investigation of disulfide bond linkages in the proteomics field. However, it has also been known that the presence of disulfide bond linkages absorbs the energy which is created by the cysteine-cysteine kinetic vibration, resulting in a decrease of the instrumental sensitivity. To overcome this problem, the disulfide bond mapping method was optimized by applying a combination of chemical labeling, proteolytic enzymes, and matrices. With the optimized method, we were also able to achieve high protein sequence coverage. Obtaining higher sequence coverage of a protein provides more information about a protein which helps to identify the protein by peptide mass fingerprint (PMF) technique. These analyses eventually contribute to the estimation of the possible PTM sites.
Diallo, Issa. "Nouvelle méthode en protéomique pour améliorer l'identification et la quantification des protéines acétylées." Thesis, Université Grenoble Alpes (ComUE), 2017. http://www.theses.fr/2017GREAS035.
Full textProtein acetylation is one of the most widespread post-translational modifications which is involved in many cellular physiologies and pathologies such as cancers. Regarding the important biological effect of protein acetylation and a non-negligible number of proteins bearing this PTM, several methods emerged last decade to investigate such PTM. But the detection of acetylations and their quantification are still limited and enrichment method allowing a better detection of acetylation target mostly one kind of acetylation (K-acetylation). To improve the detection of the three kind of acetylation (N-ter, K, and O-) and their quantification, we propose the RAQIAT method (Relative Absolute Quantification Isobaric Affinity Tag), based on protein digestion followed by 3 steps : i) a protection of free primary amines at N-ter, lysine (i.e. primary amine not bearing PTM) based on a reductive di-methylation strategy ii) a deacetylation of acetylated residues to obtain free primary amine corresponding to peptides previously acetylated iii) a RAQIAT labeling on the free primary amine obtained in the previous step to allow the enrichment of peptides previously acetylated and their quantifications. Herein, we present the investigation of the two first steps of RAQIAT method.In the first step, we evidenced that the reductive di-methylation strategy improved the detection of the three kind of acetylation: N-ter, K- and O- acetylations. Yeast protein samples were digested with trypsin prior di-methylation of resulting peptide mixture. Then, di-methylated peptide mixtures were fractionated by OFFGEL and reverse phase liquid chromatography followed by MALDI-TOF/TOF mass spectrometry analysis. Data analysis was performed by using Mascot as search engines.Our results showed that OFFGEL fractionation is a useful step to increase detection of acetylations. Moreover, we showed that our di-methylation treatment improved significantly detection of acetylation. Indeed, after di-methylation treatment, 385 unique acetylated sites were identified while 164 unique acetylated peptides were detected without di-methylation treatment. The improvement of acetylation detection using our di-methylation strategy is observed for each of acetylations: N-ter, K- and O-acetylations. Thus, this new proteomic method is promising to enhance N-ter, K- and O-acetylation detection.In the second step, we presented preliminary results of deacetylation by sirtuin 1 in the presence of p53 peptide (Ac-Arg-His-Lys-Lys- (Ac) –AMC. However, the low deacetylation efficiency of the p53 peptide observed, conclude that is not suitable to applicate into RAQIAT Method
Schiller, Rachel Shamo. "Investigating the inhibitor and substrate diversity of the JmjC histone demethylases." Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:1e7fd2a1-a9c3-48f7-8fa7-a041299d42f9.
Full textGopalswamy, Mohanraj [Verfasser]. "Aggregation and post-translational modification of the parathyroid hormone and its agonistic activity towards the G-protein coupled PTH receptors / Mohanraj Gopalswamy." Halle, 2017. http://d-nb.info/1141177951/34.
Full textDedieu, Alain. "Exploration des modifications post-traductionnelles des protéines : nouvelles approches et nouveaux modèles biologiques." Thesis, Montpellier 1, 2014. http://www.theses.fr/2014MON13516/document.
Full textRecently, the study of post-translational modifications has greatly evolved, mainly because of crucial progresses in mass spectrometry methodology which have allowed high-throughput, high resolution analysis. Their variety and their role in the regulation of key molecular mechanisms are increasingly documented. In this work, the different degrees of iodination of tyrosine were probed with a "shotgun" approach carried out from an entire organ, the mice thyroid. Post-translational modifications present in two radioresistant organism models, the bacterium Deinococcus deserti and the archaeon Thermococcus gammatolerans, were analyzed. The large scale exploration of N-terminal acetylation in D. deserti indicates a specific pattern of this modification on serine and threonine, as well as an atypical, high propension to acetylation with 50% of modified N-termini. In T. gammatolerans, N-terminal acetylation is rare, but the presence of acetylation on lysine side chains is significant. The presence of phosphorylation on these proteins suggests a potential "cross talk" between the acetylated lysine and phosphorylated serine or threonine residues. This work demonstrates that the complexity of the proteome in prokaryotes through post-translational modifications is higher than expected when extremophiles are scrutinized compared to classical prokaryote models. Interdependencies between post-translational modifications definitively deserve a fresher look
Gibson, Matthew D. "Reading the Epigenetic State of Chromatin Alters its Accessibility." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1480534756664384.
Full textSilverman, H. S. "Post-translational modification of mucins." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365785.
Full textInche, Adam. "The post translational modification of the retinoblastoma protein." Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491620.
Full textStrong, Emily. "Post translational modification of Exo1 in Saccharomyces cerevisiae." Thesis, University of Sheffield, 2017. http://etheses.whiterose.ac.uk/19163/.
Full textBooks on the topic "Post translational modification (PTM)"
Kannicht, Christoph, ed. Post-Translational Modification of Proteins. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9.
Full textWalsh, Gary. Post-translational modification of protein biopharmaceuticals. Weinheim: Wiley-VCH, 2009.
Find full textBrodbeck, Urs, and Clement Bordier, eds. Post-translational Modification of Proteins by Lipids. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74009-1.
Full textPosttranslational modification of proteins: Expanding nature's inventory. Englewood, Colo: Roberts and Co. Publishers, 2006.
Find full text1959-, Martin Bruce L., and Wang Jerry H, eds. Co- and post-translational modification of proteins: Chemical principles and biological effects. New York: Oxford University Press, 1994.
Find full textTroit͡skiĭ, G. V. Defektnye belki: Postsinteticheskai͡a modifikat͡sii͡a. Kiev: Nauk. dumka, 1991.
Find full textInternational, EBSA Symposium (2nd 1988 Gwatt Switzerland). Cytoskeletal and extracellular proteins: Structure, interaction, and assembly. Berlin: Springer-Verlag, 1989.
Find full textNATO Advanced Study Institute on Cellular Regulation by Protein Phosphorylation (1990 La Londe les Maures, France). Cellular regulation by protein phosphorylation. Berlin: Springer-Verlag, 1991.
Find full textBook chapters on the topic "Post translational modification (PTM)"
Holtz, Anja, Nathan Basisty, and Birgit Schilling. "Quantification and Identification of Post-Translational Modifications Using Modern Proteomics." In Methods in Molecular Biology, 225–35. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1024-4_16.
Full textNicosia, Luciano, and Tiziana Bonaldi. "Native Chromatin Proteomics (N-ChroP) to Characterize Histone Post-translational Modification (PTM) Combinatorics at Distinct Genomic Regions." In Methods in Molecular Biology, 251–74. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1597-3_14.
Full textMcAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, Raymond S. Hurst, Linda P. Spear, Tim C. Kirkham, Thomas Steckler, et al. "Post-Translational Modification." In Encyclopedia of Psychopharmacology, 1052–53. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1545.
Full textWang, Jun, and Robert J. Schwartz. "Post-translational Modification." In Congenital Heart Diseases: The Broken Heart, 173–202. Vienna: Springer Vienna, 2016. http://dx.doi.org/10.1007/978-3-7091-1883-2_14.
Full textMcAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, Raymond S. Hurst, Linda P. Spear, Tim C. Kirkham, Thomas Steckler, et al. "Post-Translational Protein Modification." In Encyclopedia of Psychopharmacology, 1053. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_4474.
Full textMcAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, Raymond S. Hurst, Linda P. Spear, Tim C. Kirkham, Thomas Steckler, et al. "Post-Translational Amino Acid Modification." In Encyclopedia of Psychopharmacology, 1052. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_4473.
Full textKrishna, Radha G., and Finn Wold. "Post-Translational Modification of Proteins." In Advances in Enzymology - and Related Areas of Molecular Biology, 265–98. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123133.ch3.
Full textIvanisenko, Vladimir A., Timofey V. Ivanisenko, Olga V. Saik, Pavel S. Demenkov, Dmitry A. Afonnikov, and Nikolay A. Kolchanov. "Web-Based Computational Tools for the Prediction and Analysis of Posttranslational Modifications of Proteins." In Post-Translational Modification of Proteins, 1–20. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9_1.
Full textAzzouz, Nahid, Peter Gerold, and Ralph T. Schwarz. "Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa." In Post-Translational Modification of Proteins, 145–62. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9_10.
Full textLenz, Christof. "Identification of Protein Phosphorylation Sites by Advanced LC-ESI-MS/MS Methods." In Post-Translational Modification of Proteins, 163–78. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9_11.
Full textConference papers on the topic "Post translational modification (PTM)"
Cao, Zhendong, Krista A. Budinich, Hua Huang, Bin Lu, Zhen Zhang, Diqiu Ren, Yeqiao Zhou, et al. "Abstract LB205: The IRF8-MEF2D transcription factor circuit regulated by a druggable multiple post-translational modification (PTM) reader ZMYND8 in acute myeloid leukemia." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-lb205.
Full textKannan, Surya, and Serhiy Souchelnytski. "Post-Translational Modifications of Albumin in Cancer – A Rich Source for Diagnostic and Monitoring of Treatment." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0171.
Full textToes, R. "SP0155 The role of post-translational modification and autoreactivity." 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.7219.
Full textMeng, Peng, and Rita Ghosh. "Abstract 4208: Post-translational modification of E2F1 in malignant melanoma." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4208.
Full textWang, Duolin, and Dongpeng Liu. "MusiteDeep: A deep-learning framework for protein post-translational modification site prediction." In 2017 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2017. http://dx.doi.org/10.1109/bibm.2017.8218046.
Full textCleland, Timothy Paul, Elena R. Schroeter, Robert S. Feranec, and Deepak Vashishth. "PROTEIN AND POST-TRANSLATIONAL MODIFICATION PRESERVATION IN CASTOROIDES OHIOENSIS FROM NEW YORK." In GSA Annual Meeting in Denver, Colorado, USA - 2016. Geological Society of America, 2016. http://dx.doi.org/10.1130/abs/2016am-285233.
Full textBaker, Rachael, Aaron Hobbs, Minh Huynh, Atsuo Sasaki, Henrik Dohlman, and Sharon L. Campbell. "Abstract IA18: Activation of RAS by post-translational modification: Ubiquitination and thiol oxidation." In Abstracts: AACR Special Conference on RAS Oncogenes: From Biology to Therapy; February 24-27, 2014; Lake Buena Vista, FL. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1557-3125.rasonc14-ia18.
Full textIto, Tatsuo, Zhao Xinyang, Yoshiyuki Suehara, Akira Kawai, Stephen D. Nimer, and Marc Ladanyi. "Abstract LB-172: Role of post-translational modification of the RUNX2 transcription factor in osteosarcoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-lb-172.
Full textCasey, J. L., L. Gu, D. Davis, G. Q. Cai, Q. Ding, and A. B. B. Carter. "Oxidant-Mediated Transcription and Post-Translational Modification of PGC-1α Is Required for Fibrotic Repair." 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.a7874.
Full textSanthosh, K. T., Sai Prasad Pydi, Prashen Chelikani, and Shyamala Dakshinamurti. "Serine Phosphorylation: An Important Post-translational Modification For Functional Regulation Of Smooth Muscle Thromboxane Receptor." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6361.
Full textReports on the topic "Post translational modification (PTM)"
Podlevsky, Joshua. Cas9 Protein Post-translational Modifications (PTMs): A Potential Biomarker of Gene-editing. Office of Scientific and Technical Information (OSTI), October 2019. http://dx.doi.org/10.2172/1571552.
Full textDeCastro, Andrew J., Pratima Cherukuri, and James DiRenzo. Regulation of Mammary Stem Cell Quiescence via Post-Translational Modification of DeltaNp63alpha. Fort Belvoir, VA: Defense Technical Information Center, December 2012. http://dx.doi.org/10.21236/ada576304.
Full textDeCastro, Andrew J., Pratima Cherukuri, and James DiRenzo. Regulation of Mammary Stem Cell Quiescence via Post-Translational Modification of DeltaNp63alpha. Fort Belvoir, VA: Defense Technical Information Center, February 2014. http://dx.doi.org/10.21236/ada599224.
Full textEichler, Jerry. Protein Glycosylation in Archaea: A Post-Translational Modification to Enhance Extremophilic Protein Stability. Fort Belvoir, VA: Defense Technical Information Center, January 2010. http://dx.doi.org/10.21236/ada515568.
Full textChen, J. D. Obstructing Androgen Receptor Activation in Prostate Cancer Cells Through Post-translational Modification by NEDD8. Fort Belvoir, VA: Defense Technical Information Center, November 2012. http://dx.doi.org/10.21236/ada582181.
Full textChen, J. D. Obstructing Androgen Receptor Activation in Prostate Cancer Cells Through Post-translational Modification by NEDD8. Fort Belvoir, VA: Defense Technical Information Center, May 2011. http://dx.doi.org/10.21236/ada553448.
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