| Year |
Citation |
Score |
| 2024 |
Bjarnason S, McIvor JAP, Prestel A, Demény KS, Bullerjahn JT, Kragelund BB, Mercadante D, Heidarsson PO. DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2. Nature Communications. 15: 1445. PMID 38365983 DOI: 10.1038/s41467-024-45847-2 |
0.663 |
|
| 2022 |
Buholzer KJ, McIvor J, Zosel F, Teppich C, Nettels D, Mercadante D, Schuler B. Multilayered allosteric modulation of coupled folding and binding by phosphorylation, peptidyl-prolyl cis/trans isomerization, and diversity of interaction partners. The Journal of Chemical Physics. 157: 235102. PMID 36550025 DOI: 10.1063/5.0128273 |
0.605 |
|
| 2022 |
Heidarsson PO, Mercadante D, Sottini A, Nettels D, Borgia MB, Borgia A, Kilic S, Fierz B, Best RB, Schuler B. Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein. Nature Chemistry. PMID 34992286 DOI: 10.1038/s41557-021-00839-3 |
0.656 |
|
| 2021 |
Bjarnason S, Ruidiaz SF, McIvor J, Mercadante D, Heidarsson PO. Protein intrinsic disorder on a dynamic nucleosomal landscape. Progress in Molecular Biology and Translational Science. 183: 295-354. PMID 34656332 DOI: 10.1016/bs.pmbts.2021.06.006 |
0.676 |
|
| 2018 |
Zosel F, Mercadante D, Nettels D, Schuler B. A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction. Nature Communications. 9: 3332. PMID 30127362 DOI: 10.1016/J.Bpj.2018.11.994 |
0.639 |
|
| 2018 |
Irani AH, Mercadante D, Williams MAK. On the electrophoretic mobilities of partially-charged oligosaccharides as a function of charge patterning and degree of polymerisation. Electrophoresis. PMID 29603292 DOI: 10.1002/Elps.201800050 |
0.305 |
|
| 2018 |
Tan PS, Aramburu IV, Mercadante D, Tyagi S, Chowdhury A, Spitz D, Shammas SL, Gräter F, Lemke EA. Two Differential Binding Mechanisms of FG-Nucleoporins and Nuclear Transport Receptors. Cell Reports. 22: 3660-3671. PMID 29590630 DOI: 10.1016/J.Celrep.2018.03.022 |
0.438 |
|
| 2018 |
Mercadante D, Gräter F, Daday C. CONAN: A Tool to Decode Dynamical Information from Molecular Interaction Maps. Biophysical Journal. 114: 1267-1273. PMID 29590584 DOI: 10.1016/J.Bpj.2018.01.033 |
0.368 |
|
| 2017 |
Sénéchal F, Habrylo O, Hocq L, Domon JM, Marcelo P, Lefebvre V, Pelloux J, Mercadante D. Structural and dynamical characterization of the pH-dependence of the pectin methylesterase-pectin methylesterase inhibitor complex. The Journal of Biological Chemistry. 292: 21538-21547. PMID 29109147 DOI: 10.1074/Jbc.Ra117.000197 |
0.34 |
|
| 2017 |
Mercadante D, Wagner JA, Aramburu IV, Lemke EA, Gräter F. Sampling long versus short range interactions defines the ability of force fields to reproduce the dynamics of intrinsically disordered proteins. Journal of Chemical Theory and Computation. PMID 28805390 DOI: 10.1021/Acs.Jctc.7B00143 |
0.411 |
|
| 2017 |
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, et al. Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proceedings of the National Academy of Sciences of the United States of America. PMID 28716919 DOI: 10.1073/Pnas.1704692114 |
0.336 |
|
| 2017 |
Irani AH, Owen JL, Mercadante D, Williams MA. Molecular dynamics simulations illuminate the role of counterion condensation in the electrophoretic transport of homogalacturonans. Biomacromolecules. PMID 28060493 DOI: 10.1021/Acs.Biomac.6B01599 |
0.355 |
|
| 2016 |
Hocq L, Sénéchal F, Lefebvre V, Lehner A, Domon JM, Mollet JC, Dehors J, Pageau K, Marcelo P, Guerineau F, Kolsek K, Mercadante D, Pelloux J. Combined Experimental and computational approaches reveal distinct pH-dependence of pectin methyl esterase inhibitors. Plant Physiology. PMID 28034952 DOI: 10.1104/Pp.16.01790 |
0.348 |
|
| 2016 |
Mercadante D, Milles S, Fuertes G, Svergun D, Lemke EA, Gräter F. Rescuing the Over-Collapse of Intrinsically Disordered Proteins using a Force Field Derived by a New Paradigm Biophysical Journal. 110: 556a. DOI: 10.1016/J.Bpj.2015.11.2974 |
0.406 |
|
| 2016 |
Valle Aramburu I, Mercadante D, Milles S, Ringkjøbing M, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M, Gräter F, Lemke EA. Plasticity of Nucleoporin Nuclear Transport Receptor Interactions - Molecular Description of a Highly Dynamic, Ultrafast Interaction Mechanism Biophysical Journal. 110: 357a. DOI: 10.1016/J.Bpj.2015.11.1927 |
0.468 |
|
| 2015 |
Kent LM, Loo TS, Melton LD, Mercadante D, Williams MA, Jameson GB. Structure and Properties of Non-Processive, Salt-Requiring, Acidophilic Pectin Methylesterases from Aspergillus niger Provides Insights into the Key Determinants of Processivity Control. The Journal of Biological Chemistry. PMID 26567911 DOI: 10.1074/Jbc.M115.673152 |
0.352 |
|
| 2015 |
Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M, Gräter F, Lemke EA. Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors. Cell. 163: 734-45. PMID 26456112 DOI: 10.1016/J.Cell.2015.09.047 |
0.464 |
|
| 2015 |
Mercadante D, Milles S, Fuertes G, Svergun DI, Lemke EA, Gräter F. Kirkwood-Buff Approach Rescues Overcollapse of a Disordered Protein in Canonical Protein Force Fields. The Journal of Physical Chemistry. B. 119: 7975-84. PMID 26030189 DOI: 10.1021/Acs.Jpcb.5B03440 |
0.417 |
|
| 2015 |
Beckmann A, Xiao S, Müller JP, Mercadante D, Nüchter T, Kröger N, Langhojer F, Petrich W, Holstein TW, Benoit M, Gräter F, Özbek S. A fast recoiling silk-like elastomer facilitates nanosecond nematocyst discharge. Bmc Biology. 13: 3. PMID 25592740 DOI: 10.1186/S12915-014-0113-1 |
0.371 |
|
| 2015 |
Mercadante D, Milles S, Lemke EA, Gräter F. A New and Un-Conventional Ultrafast Binding Mechanism of Intrinsically Disordered Proteins to Structured Partners Biophysical Journal. 108: 193a. DOI: 10.1016/J.Bpj.2014.11.1067 |
0.504 |
|
| 2014 |
Mercadante D, Melton LD, Jameson GB, Williams MA. Processive pectin methylesterases: the role of electrostatic potential, breathing motions and bond cleavage in the rectification of Brownian motions. Plos One. 9: e87581. PMID 24503943 DOI: 10.1371/Journal.Pone.0087581 |
0.367 |
|
| 2013 |
Mercadante D, Melton LD, Jameson GB, Williams MA, De Simone A. Substrate dynamics in enzyme action: rotations of monosaccharide subunits in the binding groove are essential for pectin methylesterase processivity. Biophysical Journal. 104: 1731-9. PMID 23601320 DOI: 10.1016/J.Bpj.2013.02.049 |
0.378 |
|
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