Relevant bibliographies by topics / Post translational modification (PTM)

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Post translational modification (PTM)'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "Post translational modification (PTM)"

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Kim, Doo Nam, Tianzhixi Yin, Tong Zhang, et al. "Artificial Intelligence Transforming Post-Translational Modification Research." Bioengineering 12, no. 1 (2024): 26. https://doi.org/10.3390/bioengineering12010026.

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Post-Translational Modifications (PTMs) are covalent changes to amino acids that occur after protein synthesis, including covalent modifications on side chains and peptide backbones. Many PTMs profoundly impact cellular and molecular functions and structures, and their significance extends to evolutionary studies as well. In light of these implications, we have explored how artificial intelligence (AI) can be utilized in researching PTMs. Initially, rationales for adopting AI and its advantages in understanding the functions of PTMs are discussed. Then, various deep learning architectures and
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Park, Mi Kyung, Ho Lee, and Chang Hoon Lee. "Post-Translational Modification of ZEB Family Members in Cancer Progression." International Journal of Molecular Sciences 23, no. 23 (2022): 15127. http://dx.doi.org/10.3390/ijms232315127.

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Post-translational modification (PTM), the essential regulatory mechanisms of proteins, play essential roles in physiological and pathological processes. In addition, PTM functions in tumour development and progression. Zinc finger E-box binding homeobox (ZEB) family homeodomain transcription factors, such as ZEB1 and ZEB2, play a pivotal role in tumour progression and metastasis by induction epithelial-mesenchymal transition (EMT), with activation of stem cell traits, immune evasion and epigenetic reprogramming. However, the relationship between ZEB family members’ post-translational modifica
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Urasaki, Yasuyo, and Thuc T. Le. "Differentiation of Essential Oils Using Nanofluidic Protein Post-Translational Modification Profiling." Molecules 24, no. 13 (2019): 2383. http://dx.doi.org/10.3390/molecules24132383.

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Current methods for the authentication of essential oils focus on analyzing their chemical composition. This study describes the use of nanofluidic protein post-translational modification (PTM) profiling to differentiate essential oils by analyzing their biochemical effects. Protein PTM profiling was used to measure the effects of four essential oils, copaiba, mandarin, Melissa, and turmeric, on the phosphorylation of MEK1, MEK2, and ERK1/2 in the MAPK signaling pathway; Akt and 4EBP1 in the pI3K/Akt/mTOR signaling pathway; and STAT3 in the JAK/STAT signaling pathway in cultured HepG2 cells. T
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Xi, Xiaoming, and Wuli Zhao. "Anti-Tumor Potential of Post-Translational Modifications of PD-1." Current Issues in Molecular Biology 46, no. 3 (2024): 2119–32. http://dx.doi.org/10.3390/cimb46030136.

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Programmed cell death protein-1 (PD-1) is a vital immune checkpoint molecule. The location, stability, and protein–protein interaction of PD-1 are significantly influenced by post-translational modification (PTM) of proteins. The biological information of PD-1, including its gene and protein structures and the PD-1/PD-L1 signaling pathway, was briefly reviewed in this review. Additionally, recent research on PD-1 post-translational modification, including the study of ubiquitination, glycosylation, phosphorylation, and palmitoylation, was summarized, and research strategies for PD-1 PTM drugs
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Wang, Duolin, Yanchun Liang, and Dong Xu. "Capsule network for protein post-translational modification site prediction." Bioinformatics 35, no. 14 (2018): 2386–94. http://dx.doi.org/10.1093/bioinformatics/bty977.

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Abstract Motivation Computational methods for protein post-translational modification (PTM) site prediction provide a useful approach for studying protein functions. The prediction accuracy of the existing methods has significant room for improvement. A recent deep-learning architecture, Capsule Network (CapsNet), which can characterize the internal hierarchical representation of input data, presents a great opportunity to solve this problem, especially using small training data. Results We proposed a CapsNet for predicting protein PTM sites, including phosphorylation, N-linked glycosylation,
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Đukić, Teodora, Katarina Smiljanić, Jelena Mihailović, et al. "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting." Foods 11, no. 24 (2022): 3993. http://dx.doi.org/10.3390/foods11243993.

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Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggr
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Kitamura, Naoya, and James J. Galligan. "A global view of the human post-translational modification landscape." Biochemical Journal 480, no. 16 (2023): 1241–65. http://dx.doi.org/10.1042/bcj20220251.

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Post-translational modifications (PTMs) provide a rapid response to stimuli, finely tuning metabolism and gene expression and maintain homeostasis. Advances in mass spectrometry over the past two decades have significantly expanded the list of known PTMs in biology and as instrumentation continues to improve, this list will surely grow. While many PTMs have been studied in detail (e.g. phosphorylation, acetylation), the vast majority lack defined mechanisms for their regulation and impact on cell fate. In this review, we will highlight the field of PTM research as it currently stands, discussi
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Hernandez-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 (2019): 5317–37. http://dx.doi.org/10.2174/0929867326666190503164004.

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Background: Post-translational modification (PTM) crosstalk is a young research field. However, there is now evidence of the extraordinary characterization of the different proteoforms and their interactions in a biological environment that PTM crosstalk studies can describe. Besides gene expression and phosphorylation profiling of acute myeloid leukemia (AML) samples, the functional combination of several PTMs that might contribute to a better understanding of the complexity of the AML proteome remains to be discovered. Objective: By reviewing current workflows for the simultaneous enrichment
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Dunphy, 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 (2021): 1930. http://dx.doi.org/10.3390/cancers13081930.

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Post-translational modifications (PTMs) add a layer of complexity to the proteome through the addition of biochemical moieties to specific residues of proteins, altering their structure, function and/or localization. Mass spectrometry (MS)-based techniques are at the forefront of PTM analysis due to their ability to detect large numbers of modified proteins with a high level of sensitivity and specificity. The low stoichiometry of modified peptides means fractionation and enrichment techniques are often performed prior to MS to improve detection yields. Immuno-based techniques remain popular,
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Wang, 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.

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Protein post-translational modification (PTM) is an important mechanism that is involved in the regulation of protein function. Considering the high-cost and labor-intensive of experimental identification, many computational prediction methods are currently available for the prediction of PTM sites by using protein local sequence information in the context of conserved motif. Here we proposed a novel computational method by using the combination of multiple kernel support vector machines (SVM) for predicting PTM sites including phosphorylation, O-linked glycosylation, acetylation, sulfation an
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Dissertations / Theses on the topic "Post translational modification (PTM)"

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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.

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Matsumiya, Nozomi. "Optimization of disulfide mapping using mass spectrometry." Thesis, Kansas State University, 2009. http://hdl.handle.net/2097/1358.

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Master of Science<br>Biochemistry<br>John Tomich<br>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 s
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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.

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L'acétylation des protéines constitue l’une des plus importantes modifications post-traductionnelles (PTMs). Elle intervient dans de multiples processus bologiques et physiopathologiques tels que, l’activité transcriptionnelle, l'apoptose, la régulation des voies métaboliques, les cancers, les maladies inflammatoires et cardiovasculaires. Face à l’importance de l’acétylation des protéines, il apparaît donc indispensable de bien comprendre les mécanismes qui y sont associés, et donc, de pouvoir identifier et quantifier les protéines acétylées à partir du protéome complet d’échantillons complexe
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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.

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Epigenetic control of gene expression by histone post-translational modifications (PTMs) is a complex process regulated by proteins that can 'read', 'write' or 'erase' these PTMs. The histone lysine demethylase (KDM) family of epigenetic enzymes remove methyl modifications from lysines on histone tails. The Jumonji C domain (JmjC) family is the largest family of KDMs. Investigating the scope and mechanisms of the JmjC KDMs is of interest for understanding the diverse functions of the JmjC KDMs in vivo, as well as for the application of the basic science to medicinal chemistry design. The work
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Gopalswamy, 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.

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Dedieu, Alain. "Exploration des modifications post-traductionnelles des protéines : nouvelles approches et nouveaux modèles biologiques." Thesis, Montpellier 1, 2014. http://www.theses.fr/2014MON13516/document.

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L'étude des modifications post-traductionnelles a connu au cours des dernières années un regain d'intérêt notable. Tout d'abord car elle s'effectue aujourd'hui au travers d'approches basées sur la spectrométrie de masse, technique qui pendant cette période a connu de profonds bouleversements, conduisant à des études plus aisées et systématiques.Mais aussi car tant par leur variété que par le rôle qu'elles jouent dans la vie et la régulation cellulaire, ces modifications ne peuvent plus être négligées. Par ailleurs au cours de ces quinze dernières années, nous avons assisté concernant les proca
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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.

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Silverman, H. S. "Post-translational modification of mucins." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365785.

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Wright, Tom. "Post-translational mutagenesis : radical methods for protein modification." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:774aa93a-489e-4051-aa01-b33781215968.

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The naturally occurring post-translational modification of proteins expands the chemical and structural diversity available for protein function. Enzymatic processes are known to modify proteins after translation, and in many cases these modifications have been demonstrated to be critical for biological function. However, the paucity of methods for introduction of site-specific modifications to proteins remains a key obstacle to their biochemical study. Access to these naturally modified proteins has long been complicated by their low abundance, difficulties in purifying homogeneous samples fr
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Inche, 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.

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The retinoblastoma protein (pRb) is a central figure in the control of not only the cell cycle, but also other cellular functions such as differentiation. The regulation of pRb function is through a variety of post translational modifications, either on pRb itself, or by the controlling influence of pRb on the post translational modification of the histone proteins. Phosphorylation of pRb is a key mechanism in the regulation of the cell cycle. pRb is also involved in the recruitment of histone methyltransferase (HMT) and acetyltransferase (HAT) to the chromatin to modify histones. Previous wor
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Books on the topic "Post translational modification (PTM)"

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Kannicht, Christoph, ed. Post-Translational Modification of Proteins. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9.

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Walsh, Gary. Post-translational modification of protein biopharmaceuticals. Wiley-VCH, 2009.

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Syozo, Tuboi, Taniguchi Naoyuki, and Katunuma Nobuhiko, eds. The post-translational modification of proteins. CRC Press, 1992.

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Brodbeck, Urs, and Clement Bordier, eds. Post-translational Modification of Proteins by Lipids. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74009-1.

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KC, Dukka B., ed. Computational Methods for Predicting Post-Translational Modification Sites. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2317-6.

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R, Lill Jennie, Sandoval Wendy N, and Pham Victoria C, eds. Protocols for the bioanalytical discovery of post translational modifications. Transworld Research Network, 2008.

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Christoph, Kannicht, ed. Post-translational modifications of proteins: Tools for functional proteomics. 2nd ed. Humana Press, 2008.

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D, Hames B., and Higgins S. J, eds. Post-translational processing: A practical approach. Oxford University Press, 1999.

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Vincenzo, Zappia, and International Symposium on Post-Translational Modifications of Proteins and Aging (1st : 1987 : Naples, Italy), eds. Advances in post-translational modifications of proteins and aging. Plenum Press, 1988.

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1938-, Brodbeck U., and Bordier Clément, eds. Post-translational modification of proteins by lipids: A laboratory manual. Springer-Verlag, 1988.

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Book chapters on the topic "Post translational modification (PTM)"

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Holtz, Anja, Nathan Basisty, and Birgit Schilling. "Quantification and Identification of Post-Translational Modifications Using Modern Proteomics." In Methods in Molecular Biology. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1024-4_16.

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AbstractPost-translational modifications (PTMs) occur dynamically, allowing cells to quickly respond to changes in the environment. Lysine residues can be targeted by several modifications including acylations (acetylation, succinylation, malonylation, glutarylation, and others), methylation, ubiquitination, and other modifications. One of the most efficient methods for the identification of post-translational modifications is utilizing immunoaffinity enrichment followed by high-resolution mass spectrometry. This workflow can be coupled with comprehensive data-independent acquisition (DIA) mas
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Li, Yuxuan, Yuanhua Huang, and Tingting Li. "PTM-X: Prediction of Post-Translational Modification Crosstalk Within and Across Proteins." In Methods in Molecular Biology. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2317-6_14.

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Nicosia, 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. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1597-3_14.

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Wang, Jun, and Robert J. Schwartz. "Post-translational Modification." In Congenital Heart Diseases: The Broken Heart. Springer Vienna, 2016. http://dx.doi.org/10.1007/978-3-7091-1883-2_14.

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McAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, et al. "Post-Translational Modification." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1545.

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McAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, et al. "Post-Translational Protein Modification." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_4474.

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McAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, et al. "Post-Translational Amino Acid Modification." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_4473.

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Krishna, Radha G., and Finn Wold. "Post-Translational Modification of Proteins." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123133.ch3.

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Ivanisenko, 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. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9_1.

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Azzouz, Nahid, Peter Gerold, and Ralph T. Schwarz. "Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa." In Post-Translational Modification of Proteins. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9055-9_10.

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Conference papers on the topic "Post translational modification (PTM)"

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Lai, Shengzhi, Peize Zhao, Ning Li, and Weichuan Yu. "A Mixed Integer Linear Program for Post-translational Modification Characterization." In 2024 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2024. https://doi.org/10.1109/bibm62325.2024.10822607.

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Cao, Zhendong, Krista A. Budinich, Hua Huang, 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.

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Toes, 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.

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Meng, 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.

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Wang, 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.

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Cleland, 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.

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Brenner, Riley, Kurtis Bertauche, Alexander Choi, and So Young Ryu. "VA-PRT: A Visualization Tool for Analyzing Post-translational Modification Retention Times." In 2021 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2021. http://dx.doi.org/10.1109/bibm52615.2021.9669150.

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Elwirehardja, Gregorius Natanael, Nicholas Dominic, and Bens Pardamean. "Web Information System Design for Fast Protein Post-Translational Modification Site Prediction." In 2022 International Conference on Information Management and Technology (ICIMTech). IEEE, 2022. http://dx.doi.org/10.1109/icimtech55957.2022.9915096.

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Baker, 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.

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Casey, J. L., L. Gu, D. Davis, G. Q. Cai, Q. Ding та A. B. B. Carter. "Oxidant-Mediated Transcription and Post-Translational Modification of PGC-1α Is Required for Fibrotic Repair". У 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.

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Reports on the topic "Post translational modification (PTM)"

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Podlevsky, Joshua. Cas9 Protein Post-translational Modifications (PTMs): A Potential Biomarker of Gene-editing. Office of Scientific and Technical Information (OSTI), 2019. http://dx.doi.org/10.2172/1571552.

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DeCastro, Andrew J., Pratima Cherukuri, and James DiRenzo. Regulation of Mammary Stem Cell Quiescence via Post-Translational Modification of DeltaNp63alpha. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada576304.

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DeCastro, Andrew J., Pratima Cherukuri, and James DiRenzo. Regulation of Mammary Stem Cell Quiescence via Post-Translational Modification of DeltaNp63alpha. Defense Technical Information Center, 2014. http://dx.doi.org/10.21236/ada599224.

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Eichler, Jerry. Protein Glycosylation in Archaea: A Post-Translational Modification to Enhance Extremophilic Protein Stability. Defense Technical Information Center, 2010. http://dx.doi.org/10.21236/ada515568.

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Chen, J. D. Obstructing Androgen Receptor Activation in Prostate Cancer Cells Through Post-translational Modification by NEDD8. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada582181.

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Chen, J. D. Obstructing Androgen Receptor Activation in Prostate Cancer Cells Through Post-translational Modification by NEDD8. Defense Technical Information Center, 2011. http://dx.doi.org/10.21236/ada553448.

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Epel, Bernard L., Roger N. Beachy, A. Katz, et al. Isolation and Characterization of Plasmodesmata Components by Association with Tobacco Mosaic Virus Movement Proteins Fused with the Green Fluorescent Protein from Aequorea victoria. United States Department of Agriculture, 1999. http://dx.doi.org/10.32747/1999.7573996.bard.

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The coordination and regulation of growth and development in multicellular organisms is dependent, in part, on the controlled short and long-distance transport of signaling molecule: In plants, symplastic communication is provided by trans-wall co-axial membranous tunnels termed plasmodesmata (Pd). Plant viruses spread cell-to-cell by altering Pd. This movement scenario necessitates a targeting mechanism that delivers the virus to a Pd and a transport mechanism to move the virion or viral nucleic acid through the Pd channel. The identity of host proteins with which MP interacts, the mechanism
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