Dagan C. Marx - Publications

Affiliations: 
Weill Cornell Medical College, New York, NY, United States 

23 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
2023 Lee J, Gonzalez-Hernandez AJ, Kristt M, Abreu N, Roßmann K, Arefin A, Marx DC, Broichhagen J, Levitz J. Distinct beta-arrestin coupling and intracellular trafficking of metabotropic glutamate receptor homo- and heterodimers. Science Advances. 9: eadi8076. PMID 38055809 DOI: 10.1126/sciadv.adi8076  0.731
2023 Mancinelli C, Marx DC, Gonzalez-Hernandez AJ, Mancinelli L, Khelashvilli G, Levitz J, Eliezer D. Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains. Biorxiv : the Preprint Server For Biology. PMID 37645938 DOI: 10.1101/2023.08.16.553551  0.751
2023 Strauss A, Gonzalez-Hernandez AJ, Lee J, Abreu N, Selvakumar P, Salas-Estrada L, Kristt M, Marx DC, Gilliland K, Melancon BJ, Filizola M, Meyerson J, Levitz J. Structural basis of allosteric modulation of metabotropic glutamate receptor activation and desensitization. Biorxiv : the Preprint Server For Biology. PMID 37645747 DOI: 10.1101/2023.08.13.552748  0.638
2023 Devlin T, Marx DC, Roskopf MA, Bubb QR, Plummer AM, Fleming KG. FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface. Protein Science : a Publication of the Protein Society. e4592. PMID 36775935 DOI: 10.1002/pro.4592  0.623
2021 Marx DC, Fleming KG. Membrane proteins enter the fold. Current Opinion in Structural Biology. 69: 124-130. PMID 33975156 DOI: 10.1016/j.sbi.2021.03.006  0.611
2021 Mahling R, Hovey L, Isbell HM, Marx DC, Miller MS, Kilpatrick AM, Weaver LD, Yoder JB, Kim EH, Andresen CNJ, Li S, Shea MA. Na1.2 EFL domain allosterically enhances Ca binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD. Structure (London, England : 1993). PMID 33770503 DOI: 10.1016/j.str.2021.03.002  0.628
2021 Vorobieva AA, White P, Liang B, Horne JE, Bera AK, Chow CM, Gerben S, Marx S, Kang A, Stiving AQ, Harvey SR, Marx DC, Khan GN, Fleming KG, Wysocki VH, et al. De novo design of transmembrane β barrels. Science (New York, N.Y.). 371. PMID 33602829 DOI: 10.1126/science.abc8182  0.563
2021 Marx DC, Fleming KG. Local Bilayer Hydrophobicity Modulates Membrane Protein Stability. Journal of the American Chemical Society. 143: 764-772. PMID 33412852 DOI: 10.1021/jacs.0c09412  0.605
2020 Huysmans GHM, Marx DC, Radford SE, Fleming KG. Determining the Free Energies of Outer Membrane Proteins in Lipid Bilayers. Methods in Molecular Biology (Clifton, N.J.). 2168: 217-232. PMID 33582994 DOI: 10.1007/978-1-0716-0724-4_10  0.615
2020 Marx DC, Plummer AM, Faustino AM, Devlin T, Roskopf MA, Leblanc MJ, Lessen HJ, Amann BT, Fleming PJ, Krueger S, Fried SD, Fleming KG. SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 33093201 DOI: 10.1073/pnas.2008175117  0.716
2020 Marx DC, Leblanc MJ, Plummer AM, Krueger S, Fleming KG. Domain Interactions Determine the Conformational Ensemble of the Periplasmic Chaperone SurA. Protein Science : a Publication of the Protein Society. PMID 32748422 DOI: 10.1002/Pro.3924  0.608
2020 Marx DC, Fleming KG. Towards Understanding How Water Modulates Membrane Protein Stability Biophysical Journal. 118: 26a-27a. DOI: 10.1016/J.Bpj.2019.11.325  0.577
2020 Roskopf MA, Marx DC, Fleming KG. Energetics of Dimeric FkpA Binding to a Native Unfolded Membrane Protein Client Biophysical Journal. 118: 366a. DOI: 10.1016/J.Bpj.2019.11.2101  0.641
2019 Roskopf MA, Marx DC, Plummer AM, Bubb QR, Fleming KG. Dimeric FkpA Acts as an Anti-Aggregase on a Native Unfolded Membrane Protein Client Biophysical Journal. 116: 497a-498a. DOI: 10.1016/J.Bpj.2018.11.2683  0.596
2019 Marx DC, Fleming KG. Bilayer Depth Dependence of Hydrophobic Amino Acid Transfer Free Energies Biophysical Journal. 116: 497a. DOI: 10.1016/J.Bpj.2018.11.2680  0.516
2017 Marx DC, Fleming KG. Influence of Protein Scaffold on Side-Chain Transfer Free Energies. Biophysical Journal. 113: 597-604. PMID 28793214 DOI: 10.1016/J.Bpj.2017.06.032  0.578
2017 Hovey L, Fowler CA, Mahling R, Lin Z, Miller MS, Marx DC, Yoder JB, Kim EH, Tefft KM, Waite BC, Feldkamp MD, Yu L, Shea MA. Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaV1.2. Biophysical Chemistry. 224: 1-19. PMID 28343066 DOI: 10.1016/J.Bpc.2017.02.006  0.632
2017 Marx D, Fleming K. Side Chain Hydrophobicity Scale using the Tilted Beta-Barrel Protein PagP Biophysical Journal. 112: 205a. DOI: 10.1016/J.Bpj.2016.11.1134  0.607
2015 Hovey L, Andresen C, Marx D, Shea M. Recruitment of Calmodulin to the Tail of the Voltage-Gated Sodium Channel Nav1.2 Biophysical Journal. 108: 577a. DOI: 10.1016/J.Bpj.2014.11.3152  0.662
2014 Hovey L, Miller MS, Marx DC, Tefft KM, Kim E, Yoder JB, Shea MA. Determinants of Preferential Binding of Apo Calmodulin to the IQ Motif of Neuronal Sodium Channel NaV1.2 Biophysical Journal. 106: 679a. DOI: 10.1016/J.Bpj.2013.11.3758  0.657
2014 Marx DC, Miller MS, Hovey L, Tefft KM, Yoder JB, Kim E, Martin SC, Feldkamp MD, Shea MA. Specificity of Calmodulin Recognition of Human Voltage-Gated Sodium Channels Biophysical Journal. 106: 326a. DOI: 10.1016/J.Bpj.2013.11.1876  0.649
2013 Marx DC, Kim EH, Miller MS, Yoder JB, Martin SC, Tarleton D, Waite BC, Feldkamp MD, Shea MA. Two Classes of Calmodulin Binding to IQ Motifs of Voltage-Gated Sodium Channels Biophysical Journal. 104: 100a. DOI: 10.1016/J.Bpj.2012.11.589  0.658
2012 Shea MA, Miller MS, Yoder JB, Martin SC, Marx DC, Kim E, Tarleton A, Miller ES, Waite BC, Wold AO, Feldkamp MD. Calmodulin Discrimination Between Voltage-Dependent Sodium Channel IQ Motifs Biophysical Journal. 102: 325a. DOI: 10.1016/J.Bpj.2011.11.1784  0.647
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