Arun K. Shukla - Publications

Affiliations: 
Duke University, Durham, NC 
Area:
GPCRs

91 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2024 Yadav MK, Sarma P, Maharana J, Ganguly M, Mishra S, Zaidi N, Dalal A, Singh V, Saha S, Mahajan G, Sharma S, Chami M, Banerjee R, Shukla AK. Structure-guided engineering of biased-agonism in the human niacin receptor via single amino acid substitution. Nature Communications. 15: 1939. PMID 38431681 DOI: 10.1038/s41467-024-46239-2  0.47
2024 Maharana J, Sano FK, Sarma P, Yadav MK, Duan L, Stepniewski TM, Chaturvedi M, Ranjan A, Singh V, Saha S, Mahajan G, Chami M, Shihoya W, Selent J, Chung KY, ... ... Shukla AK, et al. Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. Science (New York, N.Y.). 383: 101-108. PMID 38175886 DOI: 10.1126/science.adj3347  0.501
2023 Yadav MK, Maharana J, Yadav R, Saha S, Sarma P, Soni C, Singh V, Saha S, Ganguly M, Li XX, Mohapatra S, Mishra S, Khant HA, Chami M, Woodruff TM, ... ... Shukla AK, et al. Molecular basis of anaphylatoxin binding, activation, and signaling bias at complement receptors. Cell. PMID 37852260 DOI: 10.1016/j.cell.2023.09.020  0.462
2023 Sarma P, Carino CMC, Seetharama D, Pandey S, Dwivedi-Agnihotri H, Rui X, Cao Y, Kawakami K, Kumari P, Chen YC, Luker KE, Yadav PN, Luker GD, Laporte SA, Chen X, ... ... Shukla AK, et al. Molecular insights into intrinsic transducer-coupling bias in the CXCR4-CXCR7 system. Nature Communications. 14: 4808. PMID 37558722 DOI: 10.1038/s41467-023-40482-9  0.553
2023 Isaikina P, Petrovic I, Jakob RP, Sarma P, Ranjan A, Baruah M, Panwalkar V, Maier T, Shukla AK, Grzesiek S. A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes. Molecular Cell. PMID 37244255 DOI: 10.1016/j.molcel.2023.05.002  0.452
2023 Maharana J, Sarma P, Yadav MK, Saha S, Singh V, Saha S, Chami M, Banerjee R, Shukla AK. Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation. Molecular Cell. PMID 37209686 DOI: 10.1016/j.molcel.2023.04.025  0.353
2023 Grimes J, Koszegi Z, Lanoiselée Y, Miljus T, O'Brien SL, Stepniewski TM, Medel-Lacruz B, Baidya M, Makarova M, Mistry R, Goulding J, Drube J, Hoffmann C, Owen DM, Shukla AK, et al. Plasma membrane preassociation drives β-arrestin coupling to receptors and activation. Cell. 186: 2238-2255.e20. PMID 37146613 DOI: 10.1016/j.cell.2023.04.018  0.385
2022 Sarma P, Shukla AK. Resonating with the signaling bias of CXCR7. Molecular Cell. 82: 3318-3320. PMID 36113411 DOI: 10.1016/j.molcel.2022.08.020  0.386
2022 Sarma P, Banerjee R, Shukla AK. Structural snapshot of a β-arrestin-biased receptor. Trends in Pharmacological Sciences. PMID 36057461 DOI: 10.1016/j.tips.2022.08.005  0.486
2022 Baidya M, Chaturvedi M, Dwivedi-Agnihotri H, Ranjan A, Devost D, Namkung Y, Stepniewski TM, Pandey S, Baruah M, Panigrahi B, Sarma P, Yadav MK, Maharana J, Banerjee R, Kawakami K, ... ... Shukla AK, et al. Allosteric modulation of GPCR-induced β-arrestin trafficking and signaling by a synthetic intrabody. Nature Communications. 13: 4634. PMID 35941121 DOI: 10.1038/s41467-022-32386-x  0.502
2022 Maharana J, Banerjee R, Yadav MK, Sarma P, Shukla AK. Emerging structural insights into GPCR-β-arrestin interaction and functional outcomes. Current Opinion in Structural Biology. 75: 102406. PMID 35738165 DOI: 10.1016/j.sbi.2022.102406  0.439
2022 Saha S, Ranjan A, Godara M, Shukla AK. In-cellulo chemical cross-linking to visualize protein-protein interactions. Methods in Cell Biology. 169: 295-307. PMID 35623708 DOI: 10.1016/bs.mcb.2021.12.024  0.303
2022 Dwivedi-Agnihotri H, Sarma P, Deeksha S, Kawakami K, Inoue A, Shukla AK. An intrabody sensor to monitor conformational activation of β-arrestins. Methods in Cell Biology. 169: 267-278. PMID 35623705 DOI: 10.1016/bs.mcb.2021.12.023  0.315
2022 Sarma P, Saha S, Shukla AK. Making the switch: The role of Gq in driving GRK selectivity at GPCRs. Science Signaling. 15: eabo4949. PMID 35316098 DOI: 10.1126/scisignal.abo4949  0.504
2022 Kolb P, Kenakin T, Alexander SPH, Bermudez M, Bohn LM, Breinholt CS, Bouvier M, Hill SJ, Kostenis E, Martemyanov K, Neubig RR, Onaran HO, Rajagopal S, Roth BL, Selent J, ... Shukla AK, et al. Community Guidelines for GPCR Ligand Bias: IUPHAR Review XX. British Journal of Pharmacology. PMID 35106752 DOI: 10.1111/bph.15811  0.717
2021 Shiraishi Y, Kofuku Y, Ueda T, Pandey S, Dwivedi-Agnihotri H, Shukla AK, Shimada I. Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR. Nature Communications. 12: 7158. PMID 34887409 DOI: 10.1038/s41467-021-27482-3  0.326
2021 Pandey S, Kumari P, Baidya M, Kise R, Cao Y, Dwivedi-Agnihotri H, Banerjee R, Li XX, Cui CS, Lee JD, Kawakami K, Maharana J, Ranjan A, Chaturvedi M, Jhingan GD, ... ... Shukla AK, et al. Intrinsic bias at non-canonical, β-arrestin-coupled seven transmembrane receptors. Molecular Cell. PMID 34582793 DOI: 10.1016/j.molcel.2021.09.007  0.562
2021 Zhang H, Luginina A, Mishin A, Baidya M, Shukla AK, Cherezov V. Structural insights into ligand recognition and activation of angiotensin receptors. Trends in Pharmacological Sciences. PMID 33985815 DOI: 10.1016/j.tips.2021.04.006  0.463
2021 Shukla AK. Emerging paradigms in activation, signaling, and regulation of G protein-coupled receptors. The Febs Journal. 288: 2458-2460. PMID 33818907 DOI: 10.1111/febs.15839  0.485
2020 Pandey S, Saha S, Shukla AK. Transmitting the Signal: Structure of the β1-Adrenergic Receptor-Gs Protein Complex. Molecular Cell. 80: 3-5. PMID 33007256 DOI: 10.1016/j.molcel.2020.09.016  0.513
2020 Dwivedi-Agnihotri H, Chaturvedi M, Baidya M, Stepniewski TM, Pandey S, Maharana J, Srivastava A, Caengprasath N, Hanyaloglu AC, Selent J, Shukla AK. Distinct phosphorylation sites in a prototypical GPCR differently orchestrate β-arrestin interaction, trafficking, and signaling. Science Advances. 6. PMID 32917711 DOI: 10.1126/Sciadv.Abb8368  0.562
2020 Baidya M, Kumari P, Dwivedi-Agnihotri H, Pandey S, Chaturvedi M, Stepniewski TM, Kawakami K, Cao Y, Laporte SA, Selent J, Inoue A, Shukla AK. Key phosphorylation sites in GPCRs orchestrate the contribution of β-Arrestin 1 in ERK1/2 activation. Embo Reports. e49886. PMID 32715625 DOI: 10.15252/Embr.201949886  0.553
2020 Min K, Yoon HJ, Park JY, Baidya M, Dwivedi-Agnihotri H, Maharana J, Chaturvedi M, Chung KY, Shukla AK, Lee HH. Crystal Structure of β-Arrestin 2 in Complex with CXCR7 Phosphopeptide. Structure (London, England : 1993). PMID 32579945 DOI: 10.1016/J.Str.2020.06.002  0.55
2020 Lee Y, Warne T, Nehmé R, Pandey S, Dwivedi-Agnihotri H, Chaturvedi M, Edwards PC, García-Nafría J, Leslie AGW, Shukla AK, Tate CG. Molecular basis of β-arrestin coupling to formoterol-bound β-adrenoceptor. Nature. PMID 32555462 DOI: 10.1038/S41586-020-2419-1  0.583
2020 Baidya M, Kumari P, Dwivedi-Agnihotri H, Pandey S, Sokrat B, Sposini S, Chaturvedi M, Srivastava A, Roy D, Hanyaloglu AC, Bouvier M, Shukla AK. Genetically encoded intrabody sensors report the interaction and trafficking of β-arrestin 1 upon activation of G protein-coupled receptors. The Journal of Biological Chemistry. PMID 32439801 DOI: 10.1074/Jbc.Ra120.013470  0.677
2020 Pandey S, Maharana J, Li XX, Woodruff TM, Shukla AK. Emerging Insights into the Structure and Function of Complement C5a Receptors. Trends in Biochemical Sciences. PMID 32402749 DOI: 10.1016/J.Tibs.2020.04.004  0.589
2020 Chaturvedi M, Maharana J, Shukla AK. Terminating G-Protein Coupling: Structural Snapshots of GPCR-β-Arrestin Complexes. Cell. 180: 1041-1043. PMID 32169216 DOI: 10.1016/J.Cell.2020.02.047  0.571
2020 Goncharuk MV, Roy D, Dubinnyi MA, Nadezhdin KD, Srivastava A, Baidya M, Dwivedi-Agnihotri H, Arseniev AS, Shukla AK. Purification of native CCL7 and its functional interaction with selected chemokine receptors. Protein Expression and Purification. 105617. PMID 32145391 DOI: 10.1016/J.Pep.2020.105617  0.55
2020 Shukla AK, Dwivedi-Agnihotri H. Structure and function of β-arrestins, their emerging role in breast cancer, and potential opportunities for therapeutic manipulation. Advances in Cancer Research. 145: 139-156. PMID 32089163 DOI: 10.1016/Bs.Acr.2020.01.001  0.455
2020 Dwivedi-Agnihotri H, Srivastava A, Shukla AK. Reversible biotinylation of purified proteins for measuring protein-protein interactions. Methods in Enzymology. 633: 281-294. PMID 32046851 DOI: 10.1016/Bs.Mie.2019.11.008  0.367
2020 Srivastava A, Baidya M, Dwivedi-Agnihotri H, Shukla AK. Site-directed labeling of β-arrestin with monobromobimane for measuring their interaction with G protein-coupled receptors. Methods in Enzymology. 633: 271-280. PMID 32046850 DOI: 10.1016/Bs.Mie.2019.11.009  0.526
2019 Saha S, Shukla AK. The Inside Story: Crystal Structure of the Chemokine Receptor CCR7 with an Intracellular Allosteric Antagonist. Biochemistry. PMID 31702904 DOI: 10.1021/Acs.Biochem.9B00893  0.469
2019 Ghosh E, Dwivedi H, Baidya M, Srivastava A, Kumari P, Stepniewski T, Kim HR, Lee MH, van Gastel J, Chaturvedi M, Roy D, Pandey S, Maharana J, Guixà-González R, Luttrell LM, ... ... Shukla AK, et al. Conformational Sensors and Domain Swapping Reveal Structural and Functional Differences between β-Arrestin Isoforms. Cell Reports. 28: 3287-3299.e6. PMID 31553900 DOI: 10.1016/J.Celrep.2019.08.053  0.713
2019 Pandey S, Maharana J, Shukla AK. The Gut Feeling: GPCRs Enlighten the Way. Cell Host & Microbe. 26: 160-162. PMID 31415748 DOI: 10.1016/J.Chom.2019.07.018  0.316
2019 Pandey S, Li XX, Srivastava A, Baidya M, Kumari P, Dwivedi H, Chaturvedi M, Ghosh E, Woodruff TM, Shukla AK. Partial ligand-receptor engagement yields functional bias at the human complement receptor, C5aR1. The Journal of Biological Chemistry. PMID 31036565 DOI: 10.1074/Jbc.Ra119.007485  0.535
2019 Kumari P, Dwivedi H, Baidya M, Shukla AK. Measuring agonist-induced ERK MAP kinase phosphorylation for G-protein-coupled receptors. Methods in Cell Biology. 149: 141-153. PMID 30616816 DOI: 10.1016/Bs.Mcb.2018.09.015  0.477
2019 Pandey S, Roy D, Shukla AK. Measuring surface expression and endocytosis of GPCRs using whole-cell ELISA. Methods in Cell Biology. 149: 131-140. PMID 30616815 DOI: 10.1016/Bs.Mcb.2018.09.014  0.462
2019 Shukla AK. Structural Basis of Partial Agonism at the β2-Adrenergic Receptor. Biochemistry. 58: 137-139. PMID 30596501 DOI: 10.1021/Acs.Biochem.8B01237  0.493
2018 Baidya M, Kumari P, Shukla AK. Entering the Pocket: Crystal Structure of a Prostaglandin D2 Receptor. Molecular Cell. 72: 3-6. PMID 30290148 DOI: 10.1016/J.Molcel.2018.09.024  0.409
2018 Safdari HA, Pandey S, Shukla AK, Dutta S. Illuminating GPCR Signaling by Cryo-EM. Trends in Cell Biology. PMID 29945844 DOI: 10.1016/J.Tcb.2018.06.002  0.447
2018 Sente A, Peer R, Srivastava A, Baidya M, Lesk AM, Balaji S, Shukla AK, Babu MM, Flock T. Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation. Nature Structural & Molecular Biology. 25: 538-545. PMID 29872229 DOI: 10.1038/S41594-018-0071-3  0.586
2018 Chaturvedi M, Schilling J, Beautrait A, Bouvier M, Benovic JL, Shukla AK. Emerging Paradigm of Intracellular Targeting of G Protein-Coupled Receptors. Trends in Biochemical Sciences. PMID 29735399 DOI: 10.1016/J.Tibs.2018.04.003  0.748
2018 Dwivedi H, Baidya M, Shukla AK. GPCR Signaling: The Interplay of Gαi and β-arrestin. Current Biology : Cb. 28: R324-R327. PMID 29614294 DOI: 10.1016/J.Cub.2018.02.027  0.611
2017 Shukla AK, Pyne NJ. Cellular signaling - Special Issue to celebrate 75th birthday of Prof. Robert J. Lefkowitz. Cellular Signalling. PMID 29101002 DOI: 10.1016/J.Cellsig.2017.10.015  0.31
2017 Ghosh E, Srivastava A, Baidya M, Kumari P, Dwivedi H, Nidhi K, Ranjan R, Dogra S, Koide A, Yadav PN, Sidhu SS, Koide S, Shukla AK. A synthetic intrabody-based selective and generic inhibitor of GPCR endocytosis. Nature Nanotechnology. PMID 28967893 DOI: 10.1038/Nnano.2017.188  0.503
2017 Ranjan R, Dwivedi H, Baidya M, Kumar M, Shukla AK. Novel Structural Insights into GPCR-β-Arrestin Interaction and Signaling. Trends in Cell Biology. PMID 28651823 DOI: 10.1016/J.Tcb.2017.05.008  0.608
2017 Baidya M, Dwivedi H, Shukla AK. Frozen in action: cryo-EM structure of a GPCR-G-protein complex. Nature Structural & Molecular Biology. 24: 500-502. PMID 28586324 DOI: 10.1038/Nsmb.3418  0.567
2017 Kumari P, Srivastava A, Ghosh E, Ranjan R, Dogra S, Yadav PN, Shukla AK. Core engagement with β-arrestin is dispensable for agonist induced vasopressin receptor endocytosis and ERK activation. Molecular Biology of the Cell. PMID 28228552 DOI: 10.1091/Mbc.E16-12-0818  0.63
2017 Cahill TJ, Thomsen AR, Tarrasch JT, Plouffe B, Nguyen AH, Yang F, Huang LY, Kahsai AW, Bassoni DL, Gavino BJ, Lamerdin JE, Triest S, Shukla AK, Berger B, Little J, et al. Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis. Proceedings of the National Academy of Sciences of the United States of America. PMID 28223524 DOI: 10.1073/Pnas.1701529114  0.839
2017 Ranjan R, Pandey S, Shukla AK. Biased Opioid Receptor Ligands: Gain without Pain. Trends in Endocrinology and Metabolism: Tem. PMID 28110810 DOI: 10.1016/J.Tem.2017.01.001  0.391
2016 Shukla AK, Wodak SJ. Editorial overview: Multi-protein assemblies in signaling. Current Opinion in Structural Biology. PMID 27889113 DOI: 10.1016/J.Sbi.2016.11.010  0.4
2016 Kumari P, Srivastava A, Banerjee R, Ghosh E, Gupta P, Ranjan R, Chen X, Gupta B, Gupta C, Jaiman D, Shukla AK. Functional competence of a partially engaged GPCR-β-arrestin complex. Nature Communications. 7: 13416. PMID 27827372 DOI: 10.1038/Ncomms13416  0.635
2016 Thomsen AR, Plouffe B, Cahill TJ, Shukla AK, Tarrasch JT, Dosey AM, Kahsai AW, Strachan RT, Pani B, Mahoney JP, Huang L, Breton B, Heydenreich FM, Sunahara RK, Skiniotis G, et al. GPCR-G Protein-β-Arrestin Super-Complex Mediates Sustained G Protein Signaling. Cell. PMID 27499021 DOI: 10.1016/J.Cell.2016.07.004  0.818
2016 Shukla AK. G Protein-Coupled Receptors (GPCRs). The International Journal of Biochemistry & Cell Biology. PMID 27179793 DOI: 10.1016/J.Biocel.2016.05.008  0.578
2016 Ranjan R, Gupta P, Shukla AK. GPCR Signaling: β-arrestins Kiss and Remember. Current Biology : Cb. 26: R285-8. PMID 27046816 DOI: 10.1016/J.Cub.2016.02.056  0.505
2015 Kumari P, Ghosh E, Shukla AK. Emerging Approaches to GPCR Ligand Screening for Drug Discovery. Trends in Molecular Medicine. 21: 687-701. PMID 26481827 DOI: 10.1016/J.Molmed.2015.09.002  0.449
2015 Srivastava A, Gupta B, Gupta C, Shukla AK. Emerging Functional Divergence of β-Arrestin Isoforms in GPCR Function. Trends in Endocrinology and Metabolism: Tem. 26: 628-42. PMID 26471844 DOI: 10.1016/J.Tem.2015.09.001  0.476
2015 Shukla AK, Gupta C, Srivastava A, Jaiman D. Antibody fragments for stabilization and crystallization of G protein-coupled receptors and their signaling complexes. Methods in Enzymology. 557: 247-58. PMID 25950968 DOI: 10.1016/Bs.Mie.2015.01.010  0.475
2015 Shukla AK, Kumari P, Ghosh E, Nidhi K. From Recombinant Expression to Crystals: A Step-by-Step Guide to GPCR Crystallography. Methods in Enzymology. 556: 549-61. PMID 25857799 DOI: 10.1016/Bs.Mie.2015.01.017  0.449
2015 Ghosh E, Kumari P, Jaiman D, Shukla AK. Methodological advances: the unsung heroes of the GPCR structural revolution. Nature Reviews. Molecular Cell Biology. 16: 69-81. PMID 25589408 DOI: 10.1038/Nrm3933  0.493
2014 Ghosh E, Nidhi K, Shukla AK. SnapShot: GPCR-Ligand Interactions. Cell. 159: 1712, 1712.e1. PMID 25525884 DOI: 10.1016/J.Cell.2014.12.008  0.573
2014 Shukla AK, Singh G, Ghosh E. Emerging structural insights into biased GPCR signaling. Trends in Biochemical Sciences. 39: 594-602. PMID 25458114 DOI: 10.1016/J.Tibs.2014.10.001  0.597
2014 Shukla AK, Westfield GH, Xiao K, Reis RI, Huang LY, Tripathi-Shukla P, Qian J, Li S, Blanc A, Oleskie AN, Dosey AM, Su M, Liang CR, Gu LL, Shan JM, et al. Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature. 512: 218-22. PMID 25043026 DOI: 10.1038/Nature13430  0.769
2014 Shukla AK. Biasing GPCR signaling from inside. Science Signaling. 7: pe3. PMID 24473194 DOI: 10.1126/Scisignal.2005021  0.55
2013 Aristotelous T, Ahn S, Shukla AK, Gawron S, Sassano MF, Kahsai AW, Wingler LM, Zhu X, Tripathi-Shukla P, Huang XP, Riley J, Besnard J, Read KD, Roth BL, Gilbert IH, et al. Discovery of β2 Adrenergic Receptor Ligands Using Biosensor Fragment Screening of Tagged Wild-Type Receptor. Acs Medicinal Chemistry Letters. 4: 1005-1010. PMID 24454993 DOI: 10.1021/Ml400312J  0.812
2013 Shukla AK, Manglik A, Kruse AC, Xiao K, Reis RI, Tseng WC, Staus DP, Hilger D, Uysal S, Huang LY, Paduch M, Tripathi-Shukla P, Koide A, Koide S, Weis WI, et al. Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature. 497: 137-41. PMID 23604254 DOI: 10.1038/Nature12120  0.854
2012 Reiter E, Ahn S, Shukla AK, Lefkowitz RJ. Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors. Annual Review of Pharmacology and Toxicology. 52: 179-97. PMID 21942629 DOI: 10.1146/Annurev.Pharmtox.010909.105800  0.841
2012 Xiao K, Sun J, Kim J, Rajagopal S, Zhai B, Villén J, Haas W, Kovacs JJ, Shukla AK, Hara MR, Hernandez M, Lachmann A, Zhao S, Lin Y, Cheng Y, et al. Global phosphorylation analysis of β-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR) (Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 34 (15299-15304) doi:10.1073/pnas.1008461107) Proceedings of the National Academy of Sciences of the United States of America. 109: 13464. DOI: 10.1073/Pnas.1211889109  0.793
2011 Nobles KN, Xiao K, Ahn S, Shukla AK, Lam CM, Rajagopal S, Strachan RT, Huang TY, Bressler EA, Hara MR, Shenoy SK, Gygi SP, Lefkowitz RJ. Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. Science Signaling. 4: ra51. PMID 21868357 DOI: 10.1126/Scisignal.2001707  0.767
2011 Kahsai AW, Xiao K, Rajagopal S, Ahn S, Shukla AK, Sun J, Oas TG, Lefkowitz RJ. Multiple ligand-specific conformations of the β2-adrenergic receptor. Nature Chemical Biology. 7: 692-700. PMID 21857662 DOI: 10.1038/Nchembio.634  0.863
2011 Shukla AK, Xiao K, Lefkowitz RJ. Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling. Trends in Biochemical Sciences. 36: 457-69. PMID 21764321 DOI: 10.1016/J.Tibs.2011.06.003  0.736
2010 Xiao K, Sun J, Kim J, Rajagopal S, Zhai B, Villén J, Haas W, Kovacs JJ, Shukla AK, Hara MR, Hernandez M, Lachmann A, Zhao S, Lin Y, Cheng Y, et al. Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR). Proceedings of the National Academy of Sciences of the United States of America. 107: 15299-304. PMID 20686112 DOI: 10.1073/Pnas.1008461107  0.813
2010 Shukla AK, Kim J, Ahn S, Xiao K, Shenoy SK, Liedtke W, Lefkowitz RJ. Arresting a transient receptor potential (TRP) channel: beta-arrestin 1 mediates ubiquitination and functional down-regulation of TRPV4. The Journal of Biological Chemistry. 285: 30115-25. PMID 20650893 DOI: 10.1074/Jbc.M110.141549  0.838
2010 Mangmool S, Shukla AK, Rockman HA. beta-Arrestin-dependent activation of Ca(2+)/calmodulin kinase II after beta(1)-adrenergic receptor stimulation. The Journal of Cell Biology. 189: 573-87. PMID 20421423 DOI: 10.1083/Jcb.200911047  0.453
2010 Mangmool S, Shukla AK, Rockman HA. β-Arrestin–dependent activation of Ca2+/calmodulin kinase II after β1–adrenergic receptor stimulation The Journal of General Physiology. 135: i5-i5. DOI: 10.1085/Jgp1356Oia5  0.425
2009 Shenoy SK, Modi AS, Shukla AK, Xiao K, Berthouze M, Ahn S, Wilkinson KD, Miller WE, Lefkowitz RJ. Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2. Proceedings of the National Academy of Sciences of the United States of America. 106: 6650-5. PMID 19363159 DOI: 10.1073/Pnas.0901083106  0.826
2009 Walters RW, Shukla AK, Kovacs JJ, Violin JD, DeWire SM, Lam CM, Chen JR, Muehlbauer MJ, Whalen EJ, Lefkowitz RJ. beta-Arrestin1 mediates nicotinic acid-induced flushing, but not its antilipolytic effect, in mice. The Journal of Clinical Investigation. 119: 1312-21. PMID 19349687 DOI: 10.1172/Jci36806  0.759
2008 Shukla AK, Violin JD, Whalen EJ, Gesty-Palmer D, Shenoy SK, Lefkowitz RJ. Distinct conformational changes in beta-arrestin report biased agonism at seven-transmembrane receptors. Proceedings of the National Academy of Sciences of the United States of America. 105: 9988-93. PMID 18621717 DOI: 10.1073/Pnas.0804246105  0.85
2008 Lefkowitz RJ, Sun JP, Shukla AK. A crystal clear view of the beta2-adrenergic receptor. Nature Biotechnology. 26: 189-91. PMID 18259173 DOI: 10.1038/Nbt0208-189  0.704
2008 Shukla AK, Sun JP, Lefkowitz RJ. Crystallizing thinking about the beta2-adrenergic receptor. Molecular Pharmacology. 73: 1333-8. PMID 18239031 DOI: 10.1124/Mol.108.045849  0.728
2008 Lopez JJ, Shukla AK, Reinhart C, Schwalbe H, Michel H, Glaubitz C. The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy. Angewandte Chemie (International Ed. in English). 47: 1668-71. PMID 18236494 DOI: 10.1002/Anie.200704282  0.487
2008 Roy A, Shukla AK, Haase W, Michel H. Employing Rhodobacter sphaeroides to functionally express and purify human G protein-coupled receptors. Biological Chemistry. 389: 69-78. PMID 18095871 DOI: 10.1515/Bc.2008.001  0.534
2008 Lopez J, Shukla A, Reinhart C, Schwalbe H, Michel H, Glaubitz C. Innentitelbild: The Structure of the Neuropeptide Bradykinin Bound to the Human G-Protein Coupled Receptor Bradykinin B2 as Determined by Solid-State NMR Spectroscopy (Angew. Chem. 9/2008) Angewandte Chemie. 120: 1548-1548. DOI: 10.1002/Ange.200890030  0.487
2007 Shukla AK, Haase W, Reinhart C, Michel H. Heterologous expression and characterization of the recombinant bradykinin B2 receptor using the methylotrophic yeast Pichia pastoris. Protein Expression and Purification. 55: 1-8. PMID 17711791 DOI: 10.1016/J.Pep.2007.02.021  0.482
2007 Shenoy SK, Barak LS, Xiao K, Ahn S, Berthouze M, Shukla AK, Luttrell LM, Lefkowitz RJ. Ubiquitination of beta-arrestin links seven-transmembrane receptor endocytosis and ERK activation. The Journal of Biological Chemistry. 282: 29549-62. PMID 17666399 DOI: 10.1074/Jbc.M700852200  0.811
2007 Xiao K, McClatchy DB, Shukla AK, Zhao Y, Chen M, Shenoy SK, Yates JR, Lefkowitz RJ. Functional specialization of beta-arrestin interactions revealed by proteomic analysis. Proceedings of the National Academy of Sciences of the United States of America. 104: 12011-6. PMID 17620599 DOI: 10.1073/Pnas.0704849104  0.811
2007 Shukla AK, Haase W, Reinhart C, Michel H. Heterologous expression and comparative characterization of the human neuromedin U subtype II receptor using the methylotrophic yeast Pichia pastoris and mammalian cells. The International Journal of Biochemistry & Cell Biology. 39: 931-42. PMID 17445746 DOI: 10.1016/J.Biocel.2007.01.016  0.499
2006 Shukla AK, Reinhart C, Michel H. Comparative analysis of the human angiotensin II type 1a receptor heterologously produced in insect cells and mammalian cells. Biochemical and Biophysical Research Communications. 349: 6-14. PMID 16963356 DOI: 10.1016/J.Bbrc.2006.07.210  0.465
2006 Shukla AK, Reinhart C, Michel H. Dimethylsulphoxide as a tool to increase functional expression of heterologously produced GPCRs in mammalian cells. Febs Letters. 580: 4261-5. PMID 16831432 DOI: 10.1016/J.Febslet.2006.05.064  0.453
2006 Shukla AK, Haase W, Reinhart C, Michel H. Biochemical and pharmacological characterization of the human bradykinin subtype 2 receptor produced in mammalian cells using the Semliki Forest virus system. Biological Chemistry. 387: 569-76. PMID 16740128 DOI: 10.1515/Bc.2006.073  0.533
2006 Shukla AK, Haase W, Reinhart C, Michel H. Functional overexpression and characterization of human bradykinin subtype 2 receptor in insect cells using the baculovirus system. Journal of Cellular Biochemistry. 99: 868-77. PMID 16721823 DOI: 10.1002/Jcb.20976  0.529
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