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25 results on '"Sadhukhan, Ramkrishna"'

1. IL11-mediated stromal cell activation may not be the master regulator of pro-fibrotic signaling downstream of TGFβ

Author

Tan, Yunhao, primary, Mosallanejad, Kenta, additional, Zhang, Qingxiu, additional, O’Brien, Stephen, additional, Clements, Meghan, additional, Perper, Stuart, additional, Wilson, Sarah, additional, Chaulagain, Sudiksha, additional, Wang, Jing, additional, Abdalla, Mary, additional, Al-Saidi, Helen, additional, Butt, Danyal, additional, Clabbers, Anca, additional, Ofori, Kwasi, additional, Dillon, Beth, additional, Harvey, Bohdan, additional, Memmott, John, additional, Negron, Christopher, additional, Winarta, David, additional, Tan, Catherine, additional, Biswas, Amlan, additional, Dong, Feng, additional, Morales-Tirado, Vanessa, additional, Lu, Xiaoqing, additional, Singh, Gurminder, additional, White, Michael, additional, Ashley, Shanna, additional, Knight, Heather, additional, Westmoreland, Susan, additional, Phillips, Lucy, additional, Carr, Tracy, additional, Reinke-Breen, Lauren, additional, Singh, Rajeeva, additional, Xu, Jianwen, additional, Wu, Kan, additional, Rinaldi, Lisa, additional, Stoll, Brian, additional, He, Yupeng David, additional, Hazelwood, Lisa, additional, Karman, Jozsef, additional, McCluskey, Andrew, additional, Stine, William, additional, Correia, Ivan, additional, Gauld, Stephen, additional, Levesque, Marc C., additional, Veldman, Geertruida, additional, Hubeau, Cedric, additional, Radstake, Timothy, additional, Sadhukhan, Ramkrishna, additional, and Fiebiger, Edda, additional

Published
2024
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4. Small Molecule IL-36γ Antagonist as a Novel Therapeutic Approach for Plaque Psoriasis

Author

Todorović, Viktor, Su, Zhi, Putman, C. Brent, Kakavas, Stevan J., Salte, Katherine M., McDonald, Heath A., Wetter, Joseph B., Paulsboe, Stephanie E., Sun, Qi, Gerstein, Clare E., Medina, Limary, Sielaff, Bernhard, Sadhukhan, Ramkrishna, Stockmann, Henning, Richardson, Paul L., Qiu, Wei, Argiriadi, Maria A., Henry, Rodger F., Herold, J. Martin, Shotwell, J. Brad, McGaraughty, Steve P., Honore, Prisca, Gopalakrishnan, Sujatha M., Sun, Chaohong C., and Scott, Victoria E.

Published
2019
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5. CTLA4-Ig–Based Bifunctional Costimulation Inhibitor Blocks CD28 and ICOS Signaling to Prevent T Cell Priming and Effector Function

Author

Goenka, Radhika, primary, Xu, Zhenghai, additional, Samayoa, Josue, additional, Banach, David, additional, Beam, Christine, additional, Bose, Sahana, additional, Dooner, Gerri, additional, Forsyth, Charles M., additional, Lu, Xiaoqing, additional, Medina, Limary, additional, Sadhukhan, Ramkrishna, additional, Sielaff, Bernhard, additional, Sousa, Silvino, additional, Tao, Qingfeng, additional, Touw, Debra, additional, Wu, Fei, additional, Kingsbury, Gillian A., additional, and Akamatsu, Yoshiko, additional

Published
2021
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7. IL-36 receptor antagonistic antibodies inhibit inflammatory responses in preclinical models of psoriasiform dermatitis

Author

Su, Zhi, primary, Paulsboe, Stephanie, additional, Wetter, Joseph, additional, Salte, Katherine, additional, Kannan, Arun, additional, Mathew, Sheeba, additional, Horowitz, Amanda, additional, Gerstein, Clare, additional, Namovic, Marian, additional, Todorović, Viktor, additional, Seagal, Jane, additional, Edelmayer, Rebecca M., additional, Viner, Michelle, additional, Rinaldi, Lisa, additional, Zhou, Li, additional, Leys, Laura, additional, Huang, Susan, additional, Wang, Leyu, additional, Sadhukhan, Ramkrishna, additional, Honore, Prisca, additional, McGaraughty, Steve, additional, and Scott, Victoria E., additional

Published
2018
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8. Engineering elastic properties into an anti-TNFα monoclonal antibody

Author

Sadhukhan, Ramkrishna, primary, Brown, Nathan, additional, Ouellette, David, additional, Banach, David, additional, Filoti, Dana I., additional, Winarta, David, additional, Raghavendra, Reema, additional, Sousa, Silvino, additional, Darcy, Anhdao, additional, Alessandri, Leslie, additional, Ivanov, Alexander, additional, Bose, Sahana, additional, Eaton, Lucia, additional, Preston, Gregory, additional, Freeman, Jeremy, additional, and Correia, Ivan, additional

Published
2018
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9. Quantitative ligand and receptor binding studies reveal the mechanism of interleukin-36 (IL-36) pathway activation

Author

Zhou, Li, primary, Todorovic, Viktor, additional, Kakavas, Steve, additional, Sielaff, Bernhard, additional, Medina, Limary, additional, Wang, Leyu, additional, Sadhukhan, Ramkrishna, additional, Stockmann, Henning, additional, Richardson, Paul L., additional, DiGiammarino, Enrico, additional, Sun, Chaohong, additional, and Scott, Victoria, additional

Published
2018
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10. Cell-Surface Receptor–Ligand Interaction Analysis with Homogeneous Time-Resolved FRET and Metabolic Glycan Engineering: Application to Transmembrane and GPI-Anchored Receptors

Author

Stockmann, Henning, primary, Todorovic, Viktor, additional, Richardson, Paul L., additional, Marin, Violeta, additional, Scott, Victoria, additional, Gerstein, Clare, additional, Lake, Marc, additional, Wang, Leyu, additional, Sadhukhan, Ramkrishna, additional, and Vasudevan, Anil, additional

Published
2017
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11. Cell-Surface Receptor–Ligand Interaction Analysis with Homogeneous Time-Resolved FRET and Metabolic Glycan Engineering: Application to Transmembrane and GPI-Anchored Receptors

Author

Stockmann, Henning, Todorovic, Viktor, Richardson, Paul L., Marin, Violeta, Scott, Victoria, Gerstein, Clare, Lake, Marc, Wang, Leyu, Sadhukhan, Ramkrishna, and Vasudevan, Anil

Abstract

Ligand-binding assays are the linchpin of drug discovery and medicinal chemistry. Cell-surface receptors and their ligands have traditionally been characterized by radioligand-binding assays, which have low temporal and spatial resolution and entail safety risks. Here, we report a powerful alternative (GlycoFRET), where terbium-labeled fluorescent reporters are irreversibly attached to receptors by metabolic glycan engineering. For the first time, we show time-resolved fluorescence resonance energy transfer between receptor glycans and fluorescently labeled ligands. We describe GlycoFRET for a GPI-anchored receptor, a G-protein-coupled receptor, and a heterodimeric cytokine receptor in living cells with excellent sensitivity and high signal-to-background ratios. In contrast to previously described methods, GlycoFRET does not require genetic engineering or antibodies to label receptors. Given that all cell-surface receptors are glycosylated, we expect that GlycoFRET can be generalized with applications in chemical biology and biotechnology, such as target engagement, receptor pharmacology, and high-throughput screening.

Published
2024
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12. Generation and characterization of ABBV642, a dual variable domain immunoglobulin molecule (DVD-Ig) that potently neutralizes VEGF and PDGF-BB and is designed for the treatment of exudative age-related macular degeneration

Author

Ding, Kun, primary, Eaton, Lucia, additional, Bowley, Diana, additional, Rieser, Matthew, additional, Chang, Qing, additional, Harris, Maria C., additional, Clabbers, Anca, additional, Dong, Feng, additional, Shen, Jikui, additional, Hackett, Sean F., additional, Touw, Debra S., additional, Bixby, Jacqueline, additional, Zhong, Suju, additional, Benatuil, Lorenzo, additional, Bose, Sahana, additional, Grinnell, Christine, additional, Preston, Gregory M., additional, Iyer, Ramesh, additional, Sadhukhan, Ramkrishna, additional, Marchie, Susan, additional, Overmeyer, Gary, additional, Ghayur, Tariq, additional, van Riet, Deborah A., additional, Tang, Shibo, additional, Campochario, Peter A., additional, and Gu, Jijie, additional

Published
2016
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13. Generation and characterization of ABBV642, a dual variable domain immunoglobulin molecule (DVD-Ig) that potently neutralizes VEGF and PDGF-BB and is designed for the treatment of exudative age-related macular degeneration.

Author

Ding, Kun, Eaton, Lucia, Bowley, Diana, Rieser, Matthew, Chang, Qing, Harris, Maria C., Clabbers, Anca, Dong, Feng, Shen, Jikui, Hackett, Sean F., Touw, Debra S., Bixby, Jacqueline, Zhong, Suju, Benatuil, Lorenzo, Bose, Sahana, Grinnell, Christine, Preston, Gregory M., Iyer, Ramesh, Sadhukhan, Ramkrishna, and Marchie, Susan

Published
2017
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14. 2,4-Diaminopyrimidine MK2 inhibitors. Part I: Observation of an unexpected inhibitor binding mode

Author

Argiriadi, Maria A., Ericsson, Anna M., Harris, Christopher M., Banach, David L., Borhani, David W., Calderwood, David J., Demers, Megan D., DiMauro, Jennifer, Dixon, Richard W., Hardman, Jennifer, Kwak, Silvia, Li, Biqin, Mankovich, John A., Marcotte, Douglas, Mullen, Kelly D., Ni, Baofu, Pietras, M., Sadhukhan, Ramkrishna, Sousa, Silvino, Tomlinson, Medha J., Wang, Lu, Xiang, Tao, and Talanian, Robert V.

Published
2010
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15. Enabling structure-based drug design of Tyk2 through co-crystallization with a stabilizing aminoindazole inhibitor

Author

Argiriadi, Maria A, primary, Goedken, Eric R, additional, Banach, David, additional, Borhani, David W, additional, Burchat, Andrew, additional, Dixon, Richard W, additional, Marcotte, Doug, additional, Overmeyer, Gary, additional, Pivorunas, Valerie, additional, Sadhukhan, Ramkrishna, additional, Sousa, Silvino, additional, Moore, Nigel St, additional, Tomlinson, Medha, additional, Voss, Jeffrey, additional, Wang, Lu, additional, Wishart, Neil, additional, Woller, Kevin, additional, and Talanian, Robert V, additional

Published
2012
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16. Rational mutagenesis to support structure-based drug design: MAPKAP kinase 2 as a case study

Author

Argiriadi, Maria A, primary, Sousa, Silvino, additional, Banach, David, additional, Marcotte, Douglas, additional, Xiang, Tao, additional, Tomlinson, Medha J, additional, Demers, Megan, additional, Harris, Christopher, additional, Kwak, Silvia, additional, Hardman, Jennifer, additional, Pietras, Margaret, additional, Quinn, Lisa, additional, DiMauro, Jennifer, additional, Ni, Baofu, additional, Mankovich, John, additional, Borhani, David W, additional, Talanian, Robert V, additional, and Sadhukhan, Ramkrishna, additional

Published
2009
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24. Quantitative ligand and receptor binding studies reveal the mechanism of interleukin-36 (IL-36) pathway activation.

Author

Li Zhou, Todorovic, Viktor, Kakavas, Steve, Sielaff, Bernhard, Medina, Limary, Leyu Wang, Sadhukhan, Ramkrishna, Stockmann, Henning, Richardson, Paul L., DiGiammarino, Enrico, Chaohong Sun, and Scott, Victoria

Subjects
*INTERLEUKIN receptors, *LIGAND binding (Biochemistry), *CYTOKINES, *SURFACE plasmon resonance, *BINDING site assay
Abstract

IL-36 cytokines signal through the IL-36 re-ceptor (IL-36R) and a shared subunit, IL-1 receptor accessory protein (IL-1RAcP). The activation mechanism for the IL-36 pathway is proposed to be similar to that of IL-1 in that an IL-36R agonist (IL-36α, IL-36β, or IL-36γ) forms a binary complex with IL-36R, which then recruits IL-1RAcP. Recent studies have shown that IL-36R interacts with IL-1RAcP even in the absence of an agonist. To elucidate the IL-36 activation mechanism, we considered all possible binding events for IL-36 ligands/receptors and examined these events in direct binding assays. Our results indicated that the agonists bind the IL-36R extracellular domain with micromolar affinity, but do not detectably bind IL-1RAcP. Using surface plasmon resonance (SPR), we found that IL-1RAcP also does not bind IL-36R when no agonist is present. In the presence of IL-36α, however, IL-1RAcP bound IL-36R strongly. These results suggested that the main pathway to IL-36R/IL-36α/IL-1RAcP ternary complex is through the IL-36R/IL-36α binary complex, which recruits IL-1RAcP. We could not measure the binding affinity of IL-36R to IL-1RAcP directly, so we engineered a fragment crystallizable (Fc) linked construct to induce IL-36R-IL-1RAcP heterodimerization and predicted the binding affinity during a complete thermodynamic cycle to be 74 μM. The SPR analysis also indicated that the IL-36R antagonist IL-36Ra binds IL-36R with higher affinity and a much slower off rate than the IL-36R agonists, shedding light on IL-36 pathway inhibition. Our results reveal the landscape of IL-36 ligand and receptor interactions, improving our understanding of IL-36 pathway activation and inhibition. [ABSTRACT FROM AUTHOR]

Published
2018
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25. IL-36 receptor antagonistic antibodies inhibit inflammatory responses in preclinical models of psoriasiform dermatitis.

Author

Su Z, Paulsboe S, Wetter J, Salte K, Kannan A, Mathew S, Horowitz A, Gerstein C, Namovic M, Todorović V, Seagal J, Edelmayer RM, Viner M, Rinaldi L, Zhou L, Leys L, Huang S, Wang L, Sadhukhan R, Honore P, McGaraughty S, and Scott VE

Subjects
Animals, Antibodies, Monoclonal therapeutic use, Chemokine CXCL1 metabolism, Cytokines metabolism, Dermatitis therapy, Disease Models, Animal, Female, Gene Expression Profiling, Inflammation metabolism, Interleukin-1 immunology, Interleukin-23 pharmacology, Ligands, Mice, Mice, Inbred C57BL, NIH 3T3 Cells, Psoriasis therapy, Rats, Rats, Sprague-Dawley, Receptors, Interleukin immunology, Receptors, Interleukin-1 immunology, Signal Transduction, Skin metabolism, Skin pathology, Th17 Cells cytology, Antibodies, Monoclonal immunology, Dermatitis immunology, Inflammation immunology, Interleukins immunology, Psoriasis immunology, Receptors, Interleukin antagonists & inhibitors
Abstract

Psoriasis vulgaris (PV) results from activation of IL-23/Th17 immune pathway and is further amplified by cytokines/chemokines from skin cells. Among skin-derived pro-inflammatory cytokines, IL-36 family members are highly upregulated in PV patients and play a critical role in general pustular psoriasis. However, there is limited data showing crosstalk between the IL-23 and IL-36 pathways in PV. Herein, potential attenuation of skin inflammation in the IL-23-induced mouse model of psoriasiform dermatitis by functional inhibition of IL-36 receptor (IL-36R) was interrogated. Anti-mouse IL-36R monoclonal antibodies (mAbs) were generated and validated in vitro by inhibiting IL-36α-induced secretion of CXCL1 from NIH 3T3 cells. Antibody target engagement was demonstrated by inhibition of CXCL1 production in a novel acute model of IL-36α systemic injection in mice. In addition, anti-IL-36R mAbs inhibited tissue inflammation and inflammatory gene expression in an IL-36α ear injection model of psoriasiform dermatitis demonstrating engagement of the target in the ear skin. To elucidate the possible role of IL-36 signalling in IL-23/Th17 pathway, the ability of anti-IL-36R mAbs to inhibit skin inflammation in an IL-23 ear injection model was assessed. Inhibiting the IL-36 pathway resulted in significant attenuation of skin thickening and psoriasis-relevant gene expression. Taken together, these data suggest a role for IL-36 signalling in the IL-23/Th17 signalling axis in PV., (© 2018 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.)

Published
2019
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