Relevant bibliographies by topics / Site-selective protein dual modification

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Site-selective protein dual modification'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Site-selective protein dual modification"

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Matos, Maria J., Libby Brown, Barbara Bernardim, Ana Guerreiro, Gonzalo Jiménez-Osés, and Gonçalo J. L. Bernardes. "Sequential dual site-selective protein labelling enabled by lysine modification." Bioorganic & Medicinal Chemistry 28, no. 22 (2020): 115783. http://dx.doi.org/10.1016/j.bmc.2020.115783.

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Enrique, Gil de Montes, Jiménez-Moreno Ester, L. Oliveira Bruno, et al. "Azabicyclic vinyl sulfones for residue-specific dual protein labelling." Chem. Sci. 10 (March 18, 2019): 4515–22. https://doi.org/10.1039/C9SC00125E.

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We have developed [2.2.1]azabicyclic vinyl sulfone reagents that simultaneously enable cysteine-selective protein modification and introduce a handle for further bioorthogonal ligation. The reaction is fast and selective for cysteine relative to other amino acids that have nucleophilic side-chains, and the formed products are stable in human plasma and are moderately resistant to retro Diels–Alder degradation reactions. A model biotinylated [2.2.1]azabicyclic vinyl sulfone reagent was shown to efficiently label two cysteine-tagged proteins, ubiquitin and C2Am, under mild conditions (1&nd
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Kwan, Terence T. L., Omar Boutureira, Elizabeth C. Frye, et al. "Protein modification via alkyne hydrosilylation using a substoichiometric amount of ruthenium(ii) catalyst." Chemical Science 8, no. 5 (2017): 3871–78. http://dx.doi.org/10.1039/c6sc05313k.

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The development of site-specific modification of alkyne-functionalized proteins using dimethylarylsilanes and substoichiometric or low-loading of Ru(ii) catalysts is reported. Furthermore, the resultant gem-vinylsilane can undergo further targeted chemical modifications, highlighting its potential for single-site, dual-modification applications.
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Crochet, Amanda P., Mohiuddin M. Kabir, Matthew B. Francis, and Chad D. Paavola. "Site-selective dual modification of periplasmic binding proteins for sensing applications." Biosensors and Bioelectronics 26, no. 1 (2010): 55–61. http://dx.doi.org/10.1016/j.bios.2010.05.012.

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Nathani, Ramiz I., Paul Moody, Vijay Chudasama, Mark E. B. Smith, Richard J. Fitzmaurice, and Stephen Caddick. "A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification." Chemical Science 4, no. 9 (2013): 3455. http://dx.doi.org/10.1039/c3sc51333e.

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Gil de Montes, Enrique, Ester Jiménez-Moreno, Bruno L. Oliveira, et al. "Azabicyclic vinyl sulfones for residue-specific dual protein labelling." Chemical Science 10, no. 16 (2019): 4515–22. http://dx.doi.org/10.1039/c9sc00125e.

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Mühlberg, Michaela, Michael G. Hoesl, Christian Kuehne, Jens Dernedde, Nediljko Budisa, and Christian P. R. Hackenberger. "Orthogonal dual-modification of proteins for the engineering of multivalent protein scaffolds." Beilstein Journal of Organic Chemistry 11 (May 13, 2015): 784–91. http://dx.doi.org/10.3762/bjoc.11.88.

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To add new tools to the repertoire of protein-based multivalent scaffold design, we have developed a novel dual-labeling strategy for proteins that combines residue-specific incorporation of unnatural amino acids with chemical oxidative aldehyde formation at theN-terminus of a protein. Our approach relies on the selective introduction of two different functional moieties in a protein by mutually orthogonal copper-catalyzed azide–alkyne cycloaddition (CuAAC) and oxime ligation. This method was applied to the conjugation of biotin and β-linked galactose residues to yield an enzymatically active
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Gopalakrishna, R., and W. B. Anderson. "Ca2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain." Proceedings of the National Academy of Sciences 86, no. 17 (1989): 6758–62. http://dx.doi.org/10.1073/pnas.86.17.6758.

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The susceptibility of purified protein kinase C to oxidative inactivation by H2O2 was found to be increased by Ca2+ either alone at a high (5 mM) concentration or at a low (approximately 50 microM) concentration along with phosphatidylserine and diacylglycerol and by tumor-promoting phorbol esters even in the absence of Ca2+. This suggested that the membrane-bound and/or catalytically active form of protein kinase C is relatively more susceptible to oxidative inactivation. Although both the regulatory and catalytic domains of protein kinase C were susceptible to oxidative inactivation, a selec
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Li, Na, Jiren Xu, Boheng Liu, Jeevithan Elango, and Wenhui Wu. "Highly Soluble Mussel Foot Protein Enhances Antioxidant Defense and Cytoprotection via PI3K/Akt and Nrf2/HO-1 Pathways." Antioxidants 14, no. 6 (2025): 644. https://doi.org/10.3390/antiox14060644.

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Mussel foot protein is a bioadhesive protein with potential biomedical applications, but its limited solubility and poor biological stability hinder its widespread use. In this study, highly soluble mussel foot protein (HMFP) was successfully extracted using a stepwise selective enzymatic digestion method, with a molecular weight in the range of 11–17 kDa. Furthermore, a dual-functional polyethylene glycol (PEG) derivative of HMFP, designated HMFP-PEG, was synthesized. FTIR analysis confirmed the successful modification of HMFP with PEG, while TGA analysis and SEM observations demonstrated tha
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Liu, Haidong, Xiao Li, Yin Shi, Zu Ye, and Xiangdong Cheng. "Protein Tyrosine Phosphatase PRL-3: A Key Player in Cancer Signaling." Biomolecules 14, no. 3 (2024): 342. http://dx.doi.org/10.3390/biom14030342.

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Protein phosphatases are primarily responsible for dephosphorylation modification within signal transduction pathways. Phosphatase of regenerating liver-3 (PRL-3) is a dual-specific phosphatase implicated in cancer pathogenesis. Understanding PRL-3’s intricate functions and developing targeted therapies is crucial for advancing cancer treatment. This review highlights its regulatory mechanisms, expression patterns, and multifaceted roles in cancer progression. PRL-3’s involvement in proliferation, migration, invasion, metastasis, angiogenesis, and drug resistance is discussed. Regulatory mecha
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Dissertations / Theses on the topic "Site-selective protein dual modification"

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Lin, Yuya Angel. "Olefin metathesis for site-selective protein modification." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:37d998f6-c1cd-4e2c-9f9f-89d197d21016.

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Site-selective protein modification has become an important tool to study protein functions in chemical biology. In the preliminary work, allyl sulfides were found to be reactive substrates in aqueous cross-metathesis (CM) enabling the first examples of protein modification via this approach. In order to access the enhanced CM reactivity of allyl sulfide on proteins, facile chemical methods to install S-allyl cysteine on protein surface were developed. In particular, a cysteine-specific allylating reagent – allyl selenocyanate was used on protein substrate for the first time. The substrate sco
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Lee, Maximillian. "Pyridazinediones : versatile scaffolds for site-selective protein modification." Thesis, University College London (University of London), 2018. http://discovery.ucl.ac.uk/10040797/.

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Disulfide bonds represent an important target for site-selective protein modification, particularly via the strategy of functional re-bridging. Reduction of interchain disulfide bonds, followed by their re-bridging allows proteins to be functionalised in a site-selective manner whilst retaining the stability and integrity offered by the original bridge. This work describes the design and development of two distinct pyridazinedione-based technologies that, through the conduit of functional disulfide re-bridging, enable the synthesis of antibody – drug conjugates with hitherto unmet levels of co
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Andersson, Linda K. "Exploring protein functionalisation : the site-selective modification of designed four-helix bundle scaffolds /." Göteborg : Göteborg university, 2001. http://catalogue.bnf.fr/ark:/12148/cb40110915c.

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Maruani, A. G. F. "Pyridazinediones : a novel class of tuneable reagents for the selective dual modification of proteins." Thesis, University College London (University of London), 2016. http://discovery.ucl.ac.uk/1474437/.

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Antibody–drug conjugates (ADCs) are a particularly promising class of antibody-based therapeutics. They are commonly referred to as “magic-bullet” therapy due to the ability to seek and destroy primarily diseased cells within the body (e.g. cancer cells). Critical to this strategy is the availability of effective methodologies to link an antibody to other molecules (e.g. cytotoxic drugs, prodrugs). Although current approaches offer great promise for the development of ADC constructs, they often are not selective and yield heterogeneous product mixtures. Other strategies require mutations with
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Chooi, Kok Phin. "Synthetic phosphorylation of kinases for functional studies in vitro." Thesis, University of Oxford, 2014. https://ora.ox.ac.uk/objects/uuid:2adc517a-2876-4a0b-8ead-e9bf164ebc6f.

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The activity of protein kinases is heavily dependent on the phosphorylation state of the protein. Kinase phosphorylation states have been prepared through biological or enzymatic means for biochemical evaluation, but the use of protein chemical modification as an investigative tool has not been addressed. By chemically reacting a genetically encoded cysteine, phosphocysteine was installed via dehydroalanine as a reactive intermediate. The installed phosphocysteine was intended as a surrogate to the naturally occurring phosphothreonine or phosphoserine of a phosphorylated protein kinase. Two mo
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Kitowski, Annabel Katharina. "Bio-orthogonal site-selective labelling of carbohydrates and proteins." Doctoral thesis, 2019. http://hdl.handle.net/10451/44169.

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Carbohydrates and proteins represent two large groups of biomolecules which are tremendously important for biological processes in health and disease state. Although protein-structures are encoded in the genome, cellular glycan structures are template independent and can only be addressed in an indirect manner. The development of metabolic oligosaccharide engineering (MOE) gave rise to new methods to study carbohydrate structures in the context of different disease settings and in different organisms. While in many cases mannose derivatives are used to study the sialic acid structures in cance
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Book chapters on the topic "Site-selective protein dual modification"

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Spicer, Christopher D., and Benjamin G. Davis. "Palladium-Mediated Site-Selective Suzuki-Miyaura Protein Modification." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_575.

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Yokogawa, Takashi, Satoshi Ohno, and Kazuya Nishikawa. "Incorporation of 3-Azidotyrosine into Proteins Through Engineering Yeast Tyrosyl-tRNA Synthetase and Its Application to Site-Selective Protein Modification." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-331-2_19.

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Ingale, Suvarna P., Rupali Patil, and Aman B. Upaganlawar. "Cysteine in Alzheimer's Disease." In Quality Control of Cellular Protein in Neurodegenerative Disorders. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1317-0.ch013.

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Alzheimer's disease (AD) is characterized by selective loss of neurons in the hippocampus and neocortex due to abnormalities in proteins, mainly Aβ peptide and tau protein, in the form of abnormal protein aggregations or depositions in neurons. Recently oxidative/nitrosative stress has been identified as an important facilitator of neurodegeneration in AD. Cysteine-dependent proteins are known to be associated with the neurodegenerative process. Such cysteine-dependent enzyme proteins are proteases, antioxidant enzymes, kinases, phosphatases, and also non-enzymatic proteins such that utilize c
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Jackson, Peter K. "An Introduction to Posttranslational Control by Ubiquitin-Dependent Proteolysis." In Inborn Errors Of Development. Oxford University PressNew York, NY, 2008. http://dx.doi.org/10.1093/oso/9780195306910.003.0129.

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Abstract Posttranslational modification of proteins allows an expansion of the side-chain chemistry of the translationally encoded amino acids to widen the range of protein activities. The ability to reversibly modify proteins at specific times provides a flexible means for regulating protein function on a wide range of time scales. A selective list of post- translational modifications is provided in Table 129–1. To create this broad repertoire, a large number of protein-modifying enzymes and cofactors evolved to catalyze these additions, typically on specific consensus sites within target pro
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