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

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Niwa, Tomoko, Tetsuo Asaki, and Shinya Kimura. "NS-187 (INNO-406), a Bcr-Abl/Lyn Dual Tyrosine Kinase Inhibitor." Analytical Chemistry Insights 2 (January 2007): 117739010700200. http://dx.doi.org/10.4137/117739010700200008.

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Protein kinases catalyze the transfer of the γ-phosphoryl group of adenosine triphosphate (ATP) to the hydroxyl groups of protein side chains, and they play critical roles in regulating cellular signal transduction and other biochemical processes. They are attractive targets for today's drug discovery and development, and many pharmaceutical companies are intensively developing various kinds of protein kinase inhibitors. A good example is the recent success with the Bcr-Abl tyrosine kinase inhibitor imatinib mesylate (Gleevec™) in the treatment of chronic myeloid leukemia. Though imatinib has

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12

Adeleye, Samuel A., and Srujana S. Yadavalli. "Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator." PLOS Genetics 20, no. 5 (2024): e1011287. http://dx.doi.org/10.1371/journal.pgen.1011287.

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In many organisms, stress responses to adverse environments can trigger secondary functions of certain proteins by altering protein levels, localization, activity, or interaction partners. Escherichia coli cells respond to the presence of specific cationic antimicrobial peptides by strongly activating the PhoQ/PhoP two-component signaling system, which regulates genes important for growth under this stress. As part of this pathway, a biosynthetic enzyme called QueE, which catalyzes a step in the formation of queuosine (Q) tRNA modification is upregulated. When cellular QueE levels are high, it

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13

Cheng, Yu-Che, and Sheau-Yann Shieh. "Deubiquitinating enzyme USP3 controls CHK1 chromatin association and activation." Proceedings of the National Academy of Sciences 115, no. 21 (2018): 5546–51. http://dx.doi.org/10.1073/pnas.1719856115.

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Checkpoint kinase 1 (CHK1), a Ser/Thr protein kinase, is modified by the K63-linked ubiquitin chain in response to genotoxic stress, which promotes its nuclear localization, chromatin association, and activation. Interestingly, this bulky modification is linked to a critical residue, K132, at the kinase active site. It is unclear how this modification affects the kinase activity and how it is removed to enable the release of CHK1 from chromatin. Herein, we show that the K63-linked ubiquitin chain at CHK1’s K132 residue has an inhibitory effect on the kinase activity. Furthermore, we demonstrat

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14

Manahan, Carol L., Madhavi Patnana, Kendall J. Blumer та Maurine E. Linder. "Dual Lipid Modification Motifs in Gαand GγSubunits Are Required for Full Activity of the Pheromone Response Pathway inSaccharomyces cerevisiae". Molecular Biology of the Cell 11, № 3 (2000): 957–68. http://dx.doi.org/10.1091/mbc.11.3.957.

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To establish the biological function of thioacylation (palmitoylation), we have studied the heterotrimeric guanine nucleotide–binding protein (G protein) subunits of the pheromone response pathway of Saccharomyces cerevisiae. The yeast G protein γ subunit (Ste18p) is unusual among Gγsubunits because it is farnesylated at cysteine 107 and has the potential to be thioacylated at cysteine 106. Substitution of either cysteine results in a strong signaling defect. In this study, we found that Ste18p is thioacylated at cysteine 106, which depended on prenylation of cysteine 107. Ste18p was targeted

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15

Imam, Hasan, Mohsin Khan, Nandan S. Gokhale, et al. "N6-methyladenosine modification of hepatitis B virus RNA differentially regulates the viral life cycle." Proceedings of the National Academy of Sciences 115, no. 35 (2018): 8829–34. http://dx.doi.org/10.1073/pnas.1808319115.

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N6-methyladenosine (m6A) RNA methylation is the most abundant epitranscriptomic modification of eukaryotic messenger RNAs (mRNAs). Previous reports have found m6A on both cellular and viral transcripts and defined its role in regulating numerous biological processes, including viral infection. Here, we show that m6A and its associated machinery regulate the life cycle of hepatitis B virus (HBV). HBV is a DNA virus that completes its life cycle via an RNA intermediate, termed pregenomic RNA (pgRNA). Silencing of enzymes that catalyze the addition of m6A to RNA resulted in increased HBV protein

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16

Ma, Qi-Jun, Mei-Hong Sun, Jing Lu, et al. "Phosphorylation of a malate transporter promotes malate excretion and reduces cadmium uptake in apple." Journal of Experimental Botany 71, no. 12 (2020): 3437–49. http://dx.doi.org/10.1093/jxb/eraa121.

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Abstract Heavy metal contamination is a major environmental and human health hazard in many areas of the world. Organic acids sequester heavy metals and protect plant roots from the effects of toxicity; however, it is largely unknown how these acids are regulated in response to heavy metal stress. Here, protein kinase SOS2L1 from apple was functionally characterized. MdSOS2L1 was found to be involved in the regulation of malate excretion, and to inhibit cadmium uptake into roots. Using the DUAL membrane system in a screen of an apple cDNA library with MdSOS2L1 as bait, a malate transporter, Md

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17

Firmbach-Kraft, I., and R. Stick. "Analysis of nuclear lamin isoprenylation in Xenopus oocytes: isoprenylation of lamin B3 precedes its uptake into the nucleus." Journal of Cell Biology 129, no. 1 (1995): 17–24. http://dx.doi.org/10.1083/jcb.129.1.17.

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Protein prenylation is a posttranslational modification involving the covalent attachment of a prenyl lipid to a cysteine at or near the COOH terminus of a protein. It is required for membrane localization and efficient function of a number of cytoplasmic as well as nuclear proteins including the proto-oncogenic and activated forms of Ras. Farnesylation in conjunction with a nuclear localization signal has been shown to be necessary to target newly synthesized nuclear lamins to the inner nuclear envelope membrane. It is, however, not clear where in the cell isoprenylation of nuclear lamins tak

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18

To, Kenneth K. W., Enming Xing, Ross C. Larue, and Pui-Kai Li. "BET Bromodomain Inhibitors: Novel Design Strategies and Therapeutic Applications." Molecules 28, no. 7 (2023): 3043. http://dx.doi.org/10.3390/molecules28073043.

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The mammalian bromodomain and extra-terminal domain (BET) family of proteins consists of four conserved members (Brd2, Brd3, Brd4, and Brdt) that regulate numerous cancer-related and immunity-associated genes. They are epigenetic readers of histone acetylation with broad specificity. BET proteins are linked to cancer progression due to their interaction with numerous cellular proteins including chromatin-modifying factors, transcription factors, and histone modification enzymes. The spectacular growth in the clinical development of small-molecule BET inhibitors underscores the interest and imp

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19

Hirschman, Jodi E., та Duane D. Jenness. "Dual Lipid Modification of the Yeast Gγ Subunit Ste18p Determines Membrane Localization of Gβγ". Molecular and Cellular Biology 19, № 11 (1999): 7705–11. http://dx.doi.org/10.1128/mcb.19.11.7705.

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ABSTRACT The pheromone response in the yeast Saccharomyces cerevisiae is mediated by a heterotrimeric G protein. The Gβγ subunit (a complex of Ste4p and Ste18p) is associated with both internal and plasma membranes, and a portion is not stably associated with either membrane fraction. Like Ras, Ste18p contains a farnesyl-directing CaaX box motif (C-terminal residues 107 to 110) and a cysteine residue (Cys 106) that is a potential site for palmitoylation. Mutant Ste18p containing serine at position 106 (mutation ste18-C106S) migrated more rapidly than wild-type Ste18p during sodium dodecyl sulf

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20

Belousova, Natalya, Galina Mikheeva, Juri Gelovani, and Victor Krasnykh. "Modification of Adenovirus Capsid with a Designed Protein Ligand Yields a Gene Vector Targeted to a Major Molecular Marker of Cancer." Journal of Virology 82, no. 2 (2007): 630–37. http://dx.doi.org/10.1128/jvi.01896-07.

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ABSTRACT The future of genetic interventions in humans critically depends on the selectivity and efficiency of gene transfer to target tissues. The viral gene vectors explored to date cannot selectively transduce the desired targets. While substantial progress has been made in developing targeting strategies for adenovirus (Ad) vectors, future advances in this direction are severely limited by the shortage of naturally existing molecules available for use as targeting ligands. This shortage is due to fundamental and irresolvable differences at the level of both posttranslational modifications

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21

Ozols, J., and J. M. Caron. "Posttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation." Molecular Biology of the Cell 8, no. 4 (1997): 637–45. http://dx.doi.org/10.1091/mbc.8.4.637.

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As shown in the companion article, tubulin is posttranslationally modified in vivo by palmitoylation. Our goal in this study was to identify the palmitoylation sites by protein structure analysis. To obtain quantities of palmitoylated tubulin required for this analysis, a cell-free system for enzymatic [3H]palmitoylation was developed and characterized in our companion article. We then developed a methodology to examine directly the palmitoylation of all 451 amino acids of alpha-tubulin. 3H-labeled palmitoylated alpha-tubulin was cleaved with cyanogen bromide (CNBr). The CNBr digest was resolv

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22

Colombo, Sara, Renato Longhi, Stefano Alcaro, et al. "N-myristoylation determines dual targeting of mammalian NADH-cytochrome b(5) reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning." Journal of Cell Biology 168, no. 5 (2005): 735–45. http://dx.doi.org/10.1083/jcb.200407082.

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Mammalian NADH-cytochrome b(5) reductase (b5R) is an N-myristoylated protein that is dually targeted to ER and mitochondrial outer membranes. The N-linked myristate is not required for anchorage to membranes because a stretch of hydrophobic amino acids close to the NH2 terminus guarantees a tight interaction of the protein with the phospholipid bilayer. Instead, the fatty acid is required for targeting of b5R to mitochondria because a nonmyristoylated mutant is exclusively localized to the ER. Here, we have investigated the mechanism by which N-linked myristate affects b5R targeting. We find t

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23

Williamson, Chad D., and Anamaris M. Colberg-Poley. "Intracellular Sorting Signals for Sequential Trafficking of Human Cytomegalovirus UL37 Proteins to the Endoplasmic Reticulum and Mitochondria." Journal of Virology 84, no. 13 (2010): 6400–6409. http://dx.doi.org/10.1128/jvi.00556-10.

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ABSTRACT Human cytomegalovirus UL37 antiapoptotic proteins, including the predominant UL37 exon 1 protein (pUL37x1), traffic sequentially from the endoplasmic reticulum (ER) through the mitochondrion-associated membrane compartment to the mitochondrial outer membrane (OMM), where they inactivate the proapoptotic activity of Bax. We found that widespread mitochondrial distribution occurs within 1 h of pUL37x1 synthesis. The pUL37x1 mitochondrial targeting signal (MTS) spans its first antiapoptotic domain (residues 5 to 34) and consists of a weak hydrophobicity leader (MTSα) and proximal downstr

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24

Shimizu, Tatsuhiro, Takafumi Nomachi, Kunihiro Matsumoto, and Naoki Hisamoto. "A cytidine deaminase regulates axon regeneration by modulating the functions of the Caenorhabditis elegans HGF/plasminogen family protein SVH-1." PLOS Genetics 20, no. 7 (2024): e1011367. http://dx.doi.org/10.1371/journal.pgen.1011367.

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The pathway for axon regeneration in Caenorhabditis elegans is activated by SVH-1, a growth factor belonging to the HGF/plasminogen family. SVH-1 is a dual-function factor that acts as an HGF-like growth factor to promote axon regeneration and as a protease to regulate early development. It is important to understand how SVH-1 is converted from a protease to a growth factor for axon regeneration. In this study, we demonstrate that cytidine deaminase (CDD) SVH-17/CDD-2 plays a role in the functional conversion of SVH-1. We find that the codon exchange of His-755 to Tyr in the Asp–His–Ser cataly

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25

Malanchuk, Oksana, Anna Bdzhola, Sergii Palchevskyi, et al. "Investigating the Regulation of Ribosomal Protein S6 Kinase 1 by CoAlation." International Journal of Molecular Sciences 25, no. 16 (2024): 8747. http://dx.doi.org/10.3390/ijms25168747.

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Ribosomal protein S6 kinases belong to a family of highly conserved enzymes in eukaryotes that regulate cell growth, proliferation, survival, and the stress response. It is well established that the activation and downstream signalling of p70S6Ks involve multiple phosphorylation events by key regulators of cell growth, survival, and energy metabolism. Here, we report for the first time the covalent modification of p70S6K1 by coenzyme A (CoA) in response to oxidative stress, which regulates its kinase activity. The site of CoA binding (CoAlation) was mapped by mass spectrometry to cysteine 217

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26

Lee, Choong-Eun, Tam Tran, Seol-Hee Kim, Ki-Sa Sung, and Cheol-Yong Choi. "Regulation of IL-4-induced STAT6 activation by SUMOylation (P6307)." Journal of Immunology 190, no. 1_Supplement (2013): 184.15. http://dx.doi.org/10.4049/jimmunol.190.supp.184.15.

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Abstract As a key signaling molecule in the cytokine-mediated transcriptional activation STATs are shown to undergo PTMs including phosphorylation, acetylation, methylation, ubiquitination and SUMOylation. The SUMO-modification of STAT1 has been implicated in the regulation of protein stability, nuclear translocation, and transcriptional activation, probably through the reduction of the formation and life-span of the active dimer. As a part of regulation of IL-4 signaling mechanism, we have investigated the role of SUMOylation on STAT6 activation. We have identified potential SUMOylation sites

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EVANS, Paul C., Huib OVAA, Maureen HAMON, et al. "Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity." Biochemical Journal 378, no. 3 (2004): 727–34. http://dx.doi.org/10.1042/bj20031377.

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Ubiquitination regulates the stability and/or activity of numerous cellular proteins. The corollary is that de-ubiquitinating enzymes, which ‘trim’ polyubiquitin chains from specific substrate proteins, play key roles in controlling fundamental cellular activities. Ubiquitin is essential at several stages during the activation of NF-κB (nuclear factor κB), a central co-ordinator of inflammation and other immune processes. Ubiquitination is known to cause degradation of the inhibitory molecule IκBα (inhibitor of κB). In addition, activation of TRAF (tumour-necrosis-factor-receptor-associated fa

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28

Mebatsion, Teshome, Stefan Verstegen, Leonarda T. C. De Vaan, Angela Römer-Oberdörfer, and Carla C. Schrier. "A Recombinant Newcastle Disease Virus with Low-Level V Protein Expression Is Immunogenic and Lacks Pathogenicity for Chicken Embryos." Journal of Virology 75, no. 1 (2001): 420–28. http://dx.doi.org/10.1128/jvi.75.1.420-428.2001.

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ABSTRACT Newcastle disease virus (NDV) edits its P-gene mRNA by inserting a nontemplated G residue(s) at a conserved editing site (3′-UUUUUCCC-template strand). In the wild-type virus, three amino-coterminal P-gene-derived proteins, P, V, and W, are produced at frequencies of approximately 68, 29, and 2%, respectively. By applying the reverse genetics technique, editing-defective mutants were generated in cell culture. Compared to the wild-type virus, mutants lacking either six nucleotides of the conserved editing site or the unique C-terminal part of the V protein produced as much as 5,000-fo

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29

Gantz, Valentino M., Nijole Jasinskiene, Olga Tatarenkova, et al. "Highly efficient Cas9-mediated gene drive for population modification of the malaria vector mosquito Anopheles stephensi." Proceedings of the National Academy of Sciences 112, no. 49 (2015): E6736—E6743. http://dx.doi.org/10.1073/pnas.1521077112.

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Genetic engineering technologies can be used both to create transgenic mosquitoes carrying antipathogen effector genes targeting human malaria parasites and to generate gene-drive systems capable of introgressing the genes throughout wild vector populations. We developed a highly effective autonomous Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)-associated protein 9 (Cas9)-mediated gene-drive system in the Asian malaria vector Anopheles stephensi, adapted from the mutagenic chain reaction (MCR). This specific system results in progeny of males and females derived from tran

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30

Zimmer, Markus, Siegfried Scherer та Martin J. Loessner. "Genomic Analysis of Clostridium perfringens Bacteriophage φ3626, Which Integrates into guaA and Possibly Affects Sporulation". Journal of Bacteriology 184, № 16 (2002): 4359–68. http://dx.doi.org/10.1128/jb.184.16.4359-4368.2002.

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ABSTRACT Two temperate viruses, φ3626 and φ8533, have been isolated from lysogenic Clostridium perfringens strains. Phage φ3626 was chosen for detailed analysis and was inspected by electron microscopy, protein profiling, and host range determination. For the first time, the nucleotide sequence of a bacteriophage infecting Clostridium species was determined. The virus belongs to the Siphoviridae family of the tailed phages, the order Caudovirales. Its genome consists of a linear double-stranded DNA molecule of 33,507 nucleotides, with invariable 3′-protruding cohesive ends of nine residues. Fi

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Pattabiraman, Vijaya R., Matilde Arévalo Ruiz, Régis Boehringer, et al. "Abstract 2138: Creating next-generation biologics using a novel chemistry platform technology." Cancer Research 82, no. 12_Supplement (2022): 2138. http://dx.doi.org/10.1158/1538-7445.am2022-2138.

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Abstract Bright Peak Therapeutics is developing a portfolio of differentiated biotherapeutics using chemistry for applications in immuno-oncology and autoimmune diseases. Our unique chemical protein synthesis and engineering platform allows us to fine-tune cytokines and other proteins to interrogate and modulate biological functions by incorporating new functional modifications. Standard recombinant bacterial or cellular expression systems used to produce proteins are largely restricted to using canonical amino acids, which limits access to diverse modifications that can bestow additional func

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Albitar, Obaida, Crystal M. D’Souza, and Ernest A. Adeghate. "Effects of Lipoproteins on Metabolic Health." Nutrients 16, no. 13 (2024): 2156. http://dx.doi.org/10.3390/nu16132156.

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Lipids are primarily transported in the bloodstream by lipoproteins, which are macromolecules of lipids and conjugated proteins also known as apolipoproteins. The processes of lipoprotein assembly, secretion, transportation, modification, and clearance are crucial components of maintaining a healthy lipid metabolism. Disruption in any of these steps results in pathophysiological abnormalities such as dyslipidemia, obesity, insulin resistance, inflammation, atherosclerosis, peripheral artery disease, and cardiovascular diseases. By studying these genetic mutations, researchers can gain valuable

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Deng, Ou, Xueli Li, Vinayak C. Palve, Bin Fang, Damon R. Reed, and Uwe Rix. "Abstract C054: PARP16 modulates MYC expression and susceptibility of Ewing’s Sarcoma cells to PARP1 inhibition." Molecular Cancer Therapeutics 22, no. 12_Supplement (2023): C054. http://dx.doi.org/10.1158/1535-7163.targ-23-c054.

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Abstract BACKGROUND: Ewing’s sarcoma (EWS) is a highly aggressive bone and soft tissue tumor with poor prognosis and an urgent need for novel therapies. We have identified that silencing of mono-ADP-ribosyltransferase PARP16 enhanced sensitivity of EWS cell lines to PARP1 inhibition. In this study, we explored the molecular mechanism of EWS vulnerability towards PARP16 targeting, alone and in conjunction with PARP1 inhibition, which may lead to development of PARP16-selective or dual targeting PARP1/16 inhibitors as new drugs for EWS. METHODS: The effect of PARP16 on cell viability was analyze

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Nakamura, Fumihiko, Laiqiang Huang, Kersi Pestonjamasp, Elizabeth J. Luna, and Heinz Furthmayr. "Regulation of F-Actin Binding to Platelet Moesin In Vitro by Both Phosphorylation of Threonine 558 and Polyphosphatidylinositides." Molecular Biology of the Cell 10, no. 8 (1999): 2669–85. http://dx.doi.org/10.1091/mbc.10.8.2669.

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Activation of human platelets with thrombin transiently increases phosphorylation at558threonine of moesin as determined with phosphorylation state-specific antibodies. This specific modification is completely inhibited by the kinase inhibitor staurosporine and maximally promoted by the phosphatase inhibitor calyculin A, making it possible to purify the two forms of moesin to homogeneity. Blot overlay assays with F-actin probes labeled with either [32P]ATP or125I show that only phosphorylated moesin interacts with F-actin in total platelet lysates, in moesin antibody immunoprecipitates, and wh

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Evans, J. L., B. Quistorff, and L. A. Witters. "Hepatic zonation of acetyl-CoA carboxylase activity." Biochemical Journal 270, no. 3 (1990): 665–72. http://dx.doi.org/10.1042/bj2700665.

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The activities of several hepatic enzymes are preferentially zonated to the periportal or perivenous cells of the liver acinus. Employing dual-digitonin-pulse perfusion of rat liver in the study of acetyl-CoA carboxylase (ACC), we have identified a heretofore unrecognized feature of hepatic zonation, namely an intrahepatic gradient in enzyme specific activity. ACC activity shows a relative periportal localization in normally feeding rats, even when corrected for ACC protein mass. In contrast with results previously reported by us [Evans, Quistorff & Witters (1989) Biochem. J. 259, 821-829]

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Hoyt, Emily A., Pedro M. S. D. Cal, Bruno L. Oliveira, and Gonçalo J. L. Bernardes. "Contemporary approaches to site-selective protein modification." Nature Reviews Chemistry 3, no. 3 (2019): 147–71. http://dx.doi.org/10.1038/s41570-019-0079-1.

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Lin, Yuya A., Justin M. Chalker, and Benjamin G. Davis. "Olefin Metathesis for Site-Selective Protein Modification." ChemBioChem 10, no. 6 (2009): 959–69. http://dx.doi.org/10.1002/cbic.200900002.

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Gordon, Britten, Elizabeth Muhowski, Janani Ravikrishnan, et al. "Targeting Covalent and Non-Covalent Btki-Resistant CLL Using the Dual Irreversible/Reversible 4 th Generation BTK Inhibitor LP-168." Blood 142, Supplement 1 (2023): 416. http://dx.doi.org/10.1182/blood-2023-178259.

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Background: Treatment of chronic lymphocytic leukemia (CLL) has been transformed with targeted therapies including inhibitors of Bruton's tyrosine kinase (BTKi). Currently three covalent BTK inhibitors (cBTKi) are approved for CLL, but most patients eventually relapse, commonly through acquisition of the C481S BTK mutation (Woyach et al. 2014). Pirtobrutinib and nemtabrutinib are non-covalent BTK inhibitors (ncBTKi) developed to target and inhibit C481S mutant BTK. However novel secondary site mutations in BTK, namely T474I and L528W, have been found to confer resistance to both cBTKi and ncBT

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Brewster, Richard C., and Alison N. Hulme. "Halomethyl-Triazoles for Rapid, Site-Selective Protein Modification." Molecules 26, no. 18 (2021): 5461. http://dx.doi.org/10.3390/molecules26185461.

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Post-translational modifications (PTMs) are used by organisms to control protein structure and function after protein translation, but their study is complicated and their roles are not often well understood as PTMs are difficult to introduce onto proteins selectively. Designing reagents that are both good mimics of PTMs, but also only modify select amino acid residues in proteins is challenging. Frequently, both a chemical warhead and linker are used, creating a product that is a misrepresentation of the natural modification. We have previously shown that biotin-chloromethyl-triazole is an ef

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Hamdy, Rania, Bahgat Fayed, Ahmed Mostafa, et al. "Iterated Virtual Screening-Assisted Antiviral and Enzyme Inhibition Assays Reveal the Discovery of Novel Promising Anti-SARS-CoV-2 with Dual Activity." International Journal of Molecular Sciences 22, no. 16 (2021): 9057. http://dx.doi.org/10.3390/ijms22169057.

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Unfortunately, COVID-19 is still a threat to humankind and has a dramatic impact on human health, social life, the world economy, and food security. With the limited number of suggested therapies under clinical trials, the discovery of novel therapeutic agents is essential. Here, a previously identified anti-SARS-CoV-2 compound named Compound 13 (1,2,5-Oxadiazole-3-carboximidic acid, 4,4′-(methylenediimino) bis,bis[[(2-hydroxyphenyl)methylene]hydrazide) was subjected to an iterated virtual screening against SARS-CoV-2 Mpro using a combination of Ligand Designer and PathFinder. PathFinder, a co

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Keijzer, Jordi F., Judith Firet, and Bauke Albada. "Site-selective and inducible acylation of thrombin using aptamer-catalyst conjugates." Chemical Communications 57, no. 96 (2021): 12960–63. http://dx.doi.org/10.1039/d1cc05446e.

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Functionalizing a protein-binding aptamer with an acylation catalyst leads to site-selective modification of the target protein in proximity to the aptamer–protein interface. This protein modification can be switched ON or OFF by an external trigger.

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Rosen, Christian B., and Matthew B. Francis. "Targeting the N terminus for site-selective protein modification." Nature Chemical Biology 13, no. 7 (2017): 697–705. http://dx.doi.org/10.1038/nchembio.2416.

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ANTOS, J., and M. FRANCIS. "Transition metal catalyzed methods for site-selective protein modification." Current Opinion in Chemical Biology 10, no. 3 (2006): 253–62. http://dx.doi.org/10.1016/j.cbpa.2006.04.009.

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Cai, Mengyuan, Peng Yin, Ziwen Wang, et al. "Abstract 4401: Dual regulation of frizzled receptors (FZD1/7) by IGF2BP3: A novel oncogenic event promotes stem-like properties and reduces carboplatin chemosensitivity in Triple-negative breast cancer." Cancer Research 85, no. 8_Supplement_1 (2025): 4401. https://doi.org/10.1158/1538-7445.am2025-4401.

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Abstract Background: Triple-negative breast cancer (TNBC) is primarily driven by cancer stem cells (CSCs), resulting in treatment resistance after chemotherapy. Emerging evidence suggests that TNBC-CSC transformation is strongly dependent on m6A modification. We aim to characterize the specific m6A regulatory factor in TNBC-CSCs and its underlying mechanism. Methods: Transcriptome-based screening was used to determine the main m6A regulator in TNBC-CSCs. Mammosphere formation assay and flow cytometry were used to evaluate the role of insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3

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Moody, Paul, Vijay Chudasama, Ramiz I. Nathani, et al. "A rapid, site-selective and efficient route to the dual modification of DARPins." Chem. Commun. 50, no. 38 (2014): 4898–900. http://dx.doi.org/10.1039/c4cc00053f.

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Herein we describe a rapid, simple method for dual modification of DARPins by introduction of cysteine mutations at specific positions that results in a vast difference in their thiol nucleophilicity, allowing for sequential modification.

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Scumaci, Domenica, Erika Olivo, Claudia Vincenza Fiumara, et al. "DJ-1 Proteoforms in Breast Cancer Cells: The Escape of Metabolic Epigenetic Misregulation." Cells 9, no. 9 (2020): 1968. http://dx.doi.org/10.3390/cells9091968.

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Enhanced glycolysis is a hallmark of breast cancer. In cancer cells, the high glycolytic flux induces carbonyl stress, a damaging condition in which the increase of reactive carbonyl species makes DNA, proteins, and lipids more susceptible to glycation. Together with glucose, methylglyoxal (MGO), a byproduct of glycolysis, is considered the main glycating agent. MGO is highly diffusible, enters the nucleus, and can react with easily accessible lysine- and arginine-rich tails of histones. Glycation adducts on histones undergo oxidization and further rearrange to form stable species known as adv

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Abbas, Sk Jahir, Sabina Yesmin, Sandeepa K. Vittala, et al. "Target Bioconjugation of Protein Through Chemical, Molecular Dynamics, and Artificial Intelligence Approaches." Metabolites 14, no. 12 (2024): 668. https://doi.org/10.3390/metabo14120668.

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Covalent modification of proteins at specific, predetermined sites is essential for advancing biological and biopharmaceutical applications. Site-selective labeling techniques for protein modification allow us to effectively track biological function, intracellular dynamics, and localization. Despite numerous reports on modifying target proteins with functional chemical probes, unique organic reactions that achieve site-selective integration without compromising native functional properties remain a significant challenge. In this review, we delve into site-selective protein modification using

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Chalker, Justin M., Gonçalo J. L. Bernardes, and Benjamin G. Davis. "A “Tag-and-Modify” Approach to Site-Selective Protein Modification." Accounts of Chemical Research 44, no. 9 (2011): 730–41. http://dx.doi.org/10.1021/ar200056q.

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Shadish, Jared A., and Cole A. DeForest. "Site-Selective Protein Modification: From Functionalized Proteins to Functional Biomaterials." Matter 2, no. 1 (2020): 50–77. http://dx.doi.org/10.1016/j.matt.2019.11.011.

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ElSohly, Adel M., and Matthew B. Francis. "Development of Oxidative Coupling Strategies for Site-Selective Protein Modification." Accounts of Chemical Research 48, no. 7 (2015): 1971–78. http://dx.doi.org/10.1021/acs.accounts.5b00139.

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