Mit einem Sternchen hervorgehoben sind Veröffentlichungen, in denen das MZP direkt zitiert wird; alle anderen wurden mit dem MZP oder seinem Schwesterinstitut ZIK HALOmem in Verbindung gebracht; außerdem wurde ein großer Teil dieser Veröffentlichungen durch die Finanzierung des Landes ermöglicht.
Highlighted with asterisk are publications directly citing MZP; All others have been associated to MZP or its sister institute, ZIK HALOmem; In addition, a large fraction of those publications have been possible by financing from the Land.
| 2023 | |
| 309 | Zhou, Y. et al. Solubilization, purification, and characterization of the hexameric form of phosphatidylserine synthase from Candida albicans. J. Biol. Chem. 299, doi:10.1016/j.jbc.2023.104756 (2023). |
| 308 | Zhang, Y. et al. Myr-Arf1 conformational flexibility at the membrane surface sheds light on the interactions with ArfGAP ASAP1. Nature Communications 14, doi:10.1038/s41467-023-43008-5 (2023). |
| 307 | Zahn, T. et al. Novel exotic alleles of EARLY FLOWERING 3 determine plant development in barley. J. Exp. Bot. 74, 3630-3650, doi:10.1093/jxb/erad127 (2023). |
| 306 | Weininger, S. et al. Early Stage UV-B Induced Molecular Modifications of Human Eye Lens γD-Crystallin. Macromol. Biosci. 23, doi:10.1002/mabi.202200526 (2023). |
| 305 | Voigt, B., Ott, M. & Balbach, J. A Competition of Secondary and Primary Nucleation Controls Amyloid Fibril Formation of the Parathyroid Hormone. Macromol. Biosci. 23, doi:10.1002/mabi.202200525 (2023). |
| 304 | Voigt, B. et al. The Prenucleation Equilibrium of the Parathyroid Hormone Determines the Critical Aggregation Concentration and Amyloid Fibril Nucleation. ChemPhysChem 24, doi:10.1002/cphc.202300439 (2023). |
| 303 | Tüting, C., Schmidt, L., Skalidis, I., Sinz, A. & Kastritis, P. L. Enabling cryo-EM density interpretation from yeast native cell extracts by proteomics data and AlphaFold structures. Proteomics 23, doi:10.1002/pmic.202200096 (2023). |
| 302 | Träger, T. & Kastritis, P. L. Cracking the code of cellular protein–protein interactions: Alphafold and whole-cell crosslinking to the rescue. Molecular Systems Biology 19, doi:10.15252/msb.202311587 (2023). |
| 301 | Träger, J., Meister, A., Hause, G., Harauz, G. & Hinderberger, D. Shaping membrane interfaces in lipid vesicles mimicking the cytoplasmic leaflet of myelin through variation of cholesterol and myelin basic protein contents. Biochim. Biophys. Acta Biomembr. 1865, doi:10.1016/j.bbamem.2023.184179 (2023). |
| 300 | Soulié, M. et al. Zwitterionic fluorinated detergents: From design to membrane protein applications. Biochimie 205, 40-52, doi:10.1016/j.biochi.2022.11.003 (2023). |
| 299 | Skalidis, I. et al. Structural analysis of an endogenous 4-megadalton succinyl-CoA-generating metabolon. Communications Biology 6, doi:10.1038/s42003-023-04885-0 (2023). |
| 298 | Sen, N., Haupt, C., Hause, G., Bacia, K. & Binder, W. H. Inhibition of the Fibrillation of Amyloid Aβ1-40 by Hybrid-Lipid-Polymer Vesicles. Macromol. Biosci. 23, doi:10.1002/mabi.202200522 (2023). |
| 297 | Semchonok, D. A., Kyrilis, F. L., Hamdi, F. & Kastritis, P. L. Cryo-EM of a heterogeneous biochemical fraction elucidates multiple protein complexes from a multicellular thermophilic eukaryote. J. Struct. Biol. X 8, doi:10.1016/j.yjsbx.2023.100094 (2023). |
| 296 | Sachan, S., Moya, C. G., Voigt, B., Köhn, M. & Balbach, J. The pro-sequence of parathyroid hormone prevents premature amyloid fibril formation. FEBS Lett. 597, 995-1006, doi:10.1002/1873-3468.14587 (2023). |
| 295 | Opatíková, M. et al. Cryo-EM structure of a plant photosystem II supercomplex with light-harvesting protein Lhcb8 and α-tocopherol. Nature Plants 9, 1359-1369, doi:10.1038/s41477-023-01483-0 (2023). |
| 294 | Hua, L. et al. Vesicle budding caused by lysolipid-induced asymmetry stress. Biophys. J. 122, 4011-4022, doi:10.1016/j.bpj.2023.08.023 (2023). |
| 293 | Hassan, A. H. et al. The structural principles underlying molybdenum insertase complex assembly. Protein Sci. 32, doi:10.1002/pro.4753 (2023). |
| 292 | Di Ianni, A. et al. Structural assessment of the full-length wild-type tumor suppressor protein p53 by mass spectrometry-guided computational modeling. Sci. Rep. 13, doi:10.1038/s41598-023-35437-5 (2023). |
| 291 | Demisli, S. et al. Encapsulation of cannabidiol in oil-in-water nanoemulsions and nanoemulsion-filled hydrogels: A structure and biological assessment study. J. Colloid Interface Sci. 634, 300-313, doi:10.1016/j.jcis.2022.12.036 (2023). |
| 290 | Belapure, J., Sorokina, M. & Kastritis, P. L. IRAA: A statistical tool for investigating a protein–protein interaction interface from multiple structures. Protein Sci. 32, doi:10.1002/pro.4523 (2023). |
| 289 | Balbach, J. & Stubbs, M. T. Coupling proteins, with deadly consequences. Science 381, 126-127, doi:10.1126/science.adi7571 (2023). |
| 2022 | |
| 288 | Wurl, A. et al. Filling the Gap with Long n-Alkanes: Incorporation of C20 and C30 into Phospholipid Membranes. Langmuir 38, 8595-8606, doi:10.1021/acs.langmuir.2c00872 (2022). |
| 287 | Tafur, L. et al. Cryo-EM structure of the SEA complex. Nature 611, 399-404, doi:10.1038/s41586-022-05370-0 (2022). |
| 286 | Sorokina, M. et al. An Electrostatically-steered Conformational Selection Mechanism Promotes SARS-CoV-2 Spike Protein Variation. Journal of Molecular Biology 434, doi:10.1016/j.jmb.2022.167637 (2022). |
| 285 | Skalidis, I. et al. Cryo-EM and artificial intelligence visualize endogenous protein community members. Structure 30, 575-589.e576, doi:10.1016/j.str.2022.01.001 (2022). |
| 284 | Semchonok, D. A. et al. Cryo-EM structure of a tetrameric photosystem I from Chroococcidiopsis TS-821, a thermophilic, unicellular, non-heterocyst-forming cyanobacterium. Plant Commun. 3, doi:10.1016/j.xplc.2021.100248 (2022). |
| 283 | Prasad, A. et al. Mechanism of chorismate dehydratase MqnA, the first enzyme of the futalosine pathway, proceeds via substrate-assisted catalysis. J. Biol. Chem. 298, doi:10.1016/j.jbc.2022.102601 (2022). |
| 282 | Piersimoni, L., Kastritis, P. L., Arlt, C. & Sinz, A. Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein-Protein Interactions-A Method for All Seasons. Chemical Reviews 122, 7500-7531, doi:10.1021/acs.chemrev.1c00786 (2022). |
| 281 | Marusic, N. et al. Increased efficiency of charge-mediated fusion in polymer/lipid hybrid membranes. Proc. Natl. Acad. Sci. U. S. A. 119, doi:10.1073/pnas.2122468119 (2022). |
| 280 | Marske, F. et al. Shape-stabilization of organic phase change materials as mechanically stable silica boards with high latent heats synthesized via sol-gel route. J. Build. Eng. 60, doi:10.1016/j.jobe.2022.105198 (2022). |
| 279 | Marske, F. et al. Influence of surfactants and organic polymers on monolithic shape-stabilized phase change materials synthesized via sol-gel route. J. Energy Storage 49, doi:10.1016/j.est.2022.104127 (2022). |
| 278 | Li, F. et al. Investigating bolalipids as solubilizing agents for poorly soluble drugs: Effects of alkyl chain length on solubilization and cytotoxicity. Colloids Surf. B Biointerfaces 212, doi:10.1016/j.colsurfb.2022.112369 (2022). |
| 277 | Lauth, L. M. et al. Heparin promotes rapid fibrillation of the basic parathyroid hormone at physiological pH. FEBS Lett. 596, 2928-2939, doi:10.1002/1873-3468.14455 (2022). |
| 276 | Kumar, A. & Balbach, J. Inactivation of Parathyroid Hormone: Perspectives of Drug Discovery to Combating Hyperparathyroidism. Curr. Mol. Pharmacol. 15, 292-305, doi:10.2174/1874467214666210126112839 (2022). |
| 275 | Korn, P. et al. Azide- and diazirine-modified membrane lipids: Physicochemistry and applicability to study peptide/lipid interactions via cross-linking/mass spectrometry. Biochim. Biophys. Acta Biomembr. 1864, doi:10.1016/j.bbamem.2022.184004 (2022). |
| 274 | Kastritis, P. L. An Integrative Approach to Probing Transient Protein Structures in Cell Extracts. Genet. Eng. Biotechnol. News 42, 68-70, doi:10.1089/gen.42.09.22 (2022). |
| 273 | Janson, K. et al. Cryo-Electron Microscopy Snapshots of Eukaryotic Membrane Proteins in Native Lipid-Bilayer Nanodiscs. Biomacromolecules 23, 5084-5094, doi:10.1021/acs.biomac.2c00935 (2022). |
| 272 | Gruber, T. et al. Macromolecular Crowding Induces a Binding Competent Transient Structure in Intrinsically Disordered Gab1. Journal of Molecular Biology 434, doi:10.1016/j.jmb.2021.167407 (2022). |
| 271 | Glueck, D. et al. Electroneutral Polymer Nanodiscs Enable Interference-Free Probing of Membrane Proteins in a Lipid-Bilayer Environment. Small 18, doi:10.1002/smll.202202492 (2022). |
| 270 | Dreydoppel, M., Balbach, J. & Weininger, U. Monitoring protein unfolding transitions by NMR-spectroscopy. J. Biomol. NMR 76, 3-15, doi:10.1007/s10858-021-00389-3 (2022). |
| 269 | Danielczak, B. et al. A bioinspired glycopolymer for capturing membrane proteins in native-like lipid-bilayer nanodiscs. Nanoscale 14, 1855-1867, doi:10.1039/d1nr03811g (2022). |
| 2021 | |
| 268 | Tüting, C. et al. Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction. Nature Communications 12, doi:10.1038/s41467-021-27287-4 (2021). |
| 267 | Taudte, N. et al. Mammalian-like type II glutaminyl cyclases in Porphyromonas gingivalis and other oral pathogenic bacteria as targets for treatment of periodontitis. J. Biol. Chem. 296, doi:10.1016/j.jbc.2021.100263 (2021). |
| 266 | Sorzano, C. O. S. et al. Algorithmic robustness to preferred orientations in single particle analysis by CryoEM. Journal of Structural Biology 213, doi:10.1016/j.jsb.2020.107695 (2021). |
| 265 | Schüller, M., Meister, A., Green, M. & Dailey, L. A. Investigating conjugated polymer nanoparticle formulations for lateral flow immunoassays. RSC Adv. 11, 29816-29825, doi:10.1039/d1ra05212h (2021). |
| 264 | Rehkamp, A. et al. First 3D-Structural Data of Full-Length Guanylyl Cyclase 1 in Rod-Outer-Segment Preparations of Bovine Retina by Cross-Linking/Mass Spectrometry. Journal of Molecular Biology 433, doi:10.1016/j.jmb.2021.166947 (2021). |
| 263 | Otrin, L. et al. En route to dynamic life processes by SNARE-mediated fusion of polymer and hybrid membranes. Nature Communications 12, doi:10.1038/s41467-021-25294-z (2021). |
| 2020 | |
| 262 | Niemeyer, M. et al. Author Correction: Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies (Nature Communications, (2020), 11, 1, (2277), 10.1038/s41467-020-16147-2). Nature Communications 12, doi:10.1038/s41467-021-22151-x (2021). |
| 261 | Nalbadis, A. et al. Selection and incorporation of siRNA carrying non-viral vector for sustained delivery from gellan gum hydrogels. Pharmaceutics 13, doi:10.3390/pharmaceutics13101546 (2021). |
| 260 | Mahler, F., Meister, A., Vargas, C., Durand, G. & Keller, S. Self-Assembly of Protein-Containing Lipid-Bilayer Nanodiscs from Small-Molecule Amphiphiles. Small 17, doi:10.1002/smll.202103603 (2021). |
| 259 | Li, Y. et al. Coupling proteomics and metabolomics for the unsupervised identification of protein–metabolite interactions in Chaetomium thermophilum. PLoS ONE 16, doi:10.1371/journal.pone.0254429 (2021). |
| 258 | Kyrilis, F. L. et al. Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts. Cell Reports 34, doi:10.1016/j.celrep.2021.108727 (2021). |
| 257 | Kyrilis, F. L., Belapure, J. & Kastritis, P. L. Detecting Protein Communities in Native Cell Extracts by Machine Learning: A Structural Biologist’s Perspective. Front. Mol. Biosci. 8, doi:10.3389/fmolb.2021.660542 (2021). |
| 256 | Kumar, A. & Balbach, J. Folding and stability of ankyrin repeats control biological protein function. Biomolecules 11, doi:10.3390/biom11060840 (2021). |
| 255 | Klein, M. E. et al. Towards the development of long circulating phosphatidylserine (Ps)‐ and phosphatidylglycerol (pg)‐enriched anti‐inflammatory liposomes: Is pegylation effective? Pharmaceutics 13, 1-16, doi:10.3390/pharmaceutics13020282 (2021). |
| 254 | Janson, K. et al. Solubilization of artificial mitochondrial membranes by amphiphilic copolymers of different charge. Biochim. Biophys. Acta Biomembr. 1863, doi:10.1016/j.bbamem.2021.183725 (2021). |
| 253 | Jänicke, P. et al. Fluorescent spherical mesoporous silica nanoparticles loaded with emodin: Synthesis, cellular uptake and anticancer activity. Mater. Sci. Eng. C 119, doi:10.1016/j.msec.2020.111619 (2021). |
| 252 | Hoffmann, M. et al. Nanoscale Model System for the Human Myelin Sheath. Biomacromolecules 22, 3901-3912, doi:10.1021/acs.biomac.1c00714 (2021). |
| 251 | Fratini, M. et al. Plasma membrane nano-organization specifies phosphoinositide effects on Rho-GTPases and actin dynamics in tobacco pollen tubes. Plant Cell 33, 642-670, doi:10.1093/plcell/koaa035 (2021). |
| 250 | Fratini, M. et al. Erratum: Plasma membrane nano-organization specifies phosphoinositide effects on Rho-GTPases and actin dynamics in tobacco pollen tubes (Plant Cell (2021) 33 (642-670) DOI: 10.1093/plcell/koaa035). Plant Cell 33, 3176, doi:10.1093/plcell/koab160 (2021). |
| 249 | Drikos, I., Boutou, E., Kastritis, P. L. & Vorgias, C. E. BRCA1-BRCT mutations alter the subcellular localization of BRCA1 in vitro. Anticancer Res. 41, 2953-2962, doi:10.21873/anticanres.15077 (2021). |
| 248 | Dorner, J. et al. A Diazirine-Modified Membrane Lipid to Study Peptide/Lipid Interactions – Chances and Challenges. Chem. Eur. J. 27, 14586-14593, doi:10.1002/chem.202102048 (2021). |
| 247 | Auerswald, J. et al. Measuring protein insertion areas in lipid monolayers by fluorescence correlation spectroscopy. Biophys. J. 120, 1333-1342, doi:10.1016/j.bpj.2021.02.011 (2021). |
| 246 | Zhou, Y. et al. Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 117, 22157-22166, doi:10.1073/pnas.2005301117 (2020). |
| 245 | Vasco, A. V. et al. Insights into the secondary structures of lactamN-substituted stapled peptides. Org. Biomol. Chem. 18, 3838-3842, doi:10.1039/d0ob00767f (2020). |
| 244 | Tüting, C., Iacobucci, C., Ihling, C. H., Kastritis, P. L. & Sinz, A. Structural analysis of 70S ribosomes by cross-linking/mass spectrometry reveals conformational plasticity. Sci. Rep. 10, doi:10.1038/s41598-020-69313-3 (2020). |
| 243 | Sorokina, M. et al. Structural models of human ACE2 variants with SARS-CoV-2 Spike protein for structure-based drug design. Sci. Data 7, doi:10.1038/s41597-020-00652-6 (2020). |
| 242 | Skalidis, I., Tüting, C. & Kastritis, P. L. Unstructured regions of large enzymatic complexes control the availability of metabolites with signaling functions. Cell Communication and Signaling 18, doi:10.1186/s12964-020-00631-9 (2020). |
| 241 | Rodrigues, J. P. G. L. M. et al. Insights on cross-species transmission of SARS-CoV-2 from structural modeling. PLoS Comput. Biol. 16, doi:10.1371/journal.pcbi.1008449 (2020). |
| 240 | Pinnapireddy, S. R. et al. A triple chain polycationic peptide-mimicking amphiphile-efficient DNA-transfer without co-lipids. Biomater. Sci. 8, 232-249, doi:10.1039/c9bm01093a (2020). |
| 239 | Niemeyer, M. et al. Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies. Nature Communications 11, doi:10.1038/s41467-020-16147-2 (2020). |
| 238 | Modicano, P. et al. Enhanced optical imaging properties of lipid nanocapsules as vehicles for fluorescent conjugated polymers. Eur. J. Pharm. Biopharm. 154, 297-308, doi:10.1016/j.ejpb.2020.07.017 (2020). |
| 237 | Marušič, N. et al. Constructing artificial respiratory chain in polymer compartments: Insights into the interplay between bo3 oxidase and the membrane. Proc. Natl. Acad. Sci. U. S. A. 117, 15006-15017, doi:10.1073/pnas.1919306117 (2020). |
| 236 | Klein, M. E. et al. Phosphatidylserine (PS) and phosphatidylglycerol (PG) enriched mixed micelles (MM): A new nano-drug delivery system with anti-inflammatory potential? Eur. J. Pharm. Sci. 152, doi:10.1016/j.ejps.2020.105451 (2020). |
| 235 | Klein, M. E. et al. Phosphatidylserine (PS) and phosphatidylglycerol (PG) nanodispersions as potential anti-inflammatory therapeutics: Comparison of in vitro activity and impact of pegylation. Nanomed. Nanotechnol. Biol. Med. 23, doi:10.1016/j.nano.2019.102096 (2020). |
| 234 | Heinz, D., Meister, A., Hussain, H., Busse, K. & Kressler, J. Triphilic pentablock copolymers with perfluoroalkyl segment in central position. J. Polym. Sci. 58, 3322-3335, doi:10.1002/pol.20200582 (2020). |
| 233 | Hamdi, F. et al. 2.7 Å cryo-EM structure of vitrified M. Musculus H-chain apoferritin from a compact 200 keV cryo-microscope. PLoS ONE 15, doi:10.1371/journal.pone.0232540 (2020). |
| 232 | Gruhle, K. et al. Synthesis and aggregation behaviour of single-chain, 1,32-alkyl-branched bis(phosphocholines)-part 2: Lateral chain length triggers self-assembling from sheets to fibres to vesicles. Org. Biomol. Chem. 18, 3585-3598, doi:10.1039/d0ob00534g (2020). |
| 231 | Grimmer, M. & Bacia, K. Giant Endoplasmic Reticulum vesicles (GERVs), a novel model membrane tool. Sci. Rep. 10, doi:10.1038/s41598-020-59700-1 (2020). |
| 230 | Evgrafova, Z. et al. Synthesis and Aggregation of Polymer-Amyloid β Conjugates. Macromol. Rapid Commun. 41, doi:10.1002/marc.201900378 (2020). |
| 229 | Drescher, S. et al. Tuning the Thickness of a Biomembrane by Stapling Diamidophospholipids with Bolalipids. Langmuir 36, 8610-8616, doi:10.1021/acs.langmuir.0c01522 (2020). |
| 228 | Auerswald, A., Gruber, T., Balbach, J. & Meister, A. Lipid-Dependent Interaction of Human N-BAR Domain Proteins with Sarcolemma Mono- And Bilayers. Langmuir 36, 8695-8704, doi:10.1021/acs.langmuir.0c00649 (2020). |
| 2019 | |
| 227 | Wägele, J., De Sio, S., Voigt, B., Balbach, J. & Ott, M. How Fluorescent Tags Modify Oligomer Size Distributions of the Alzheimer Peptide. Biophys. J. 116, 227-238, doi:10.1016/j.bpj.2018.12.010 (2019). |
| 226 | Vasco, A. V. et al. A Multicomponent Stapling Approach to Exocyclic Functionalized Helical Peptides: Adding Lipids, Sugars, PEGs, Labels, and Handles to the Lactam Bridge. Bioconjugate Chem. 30, 253-259, doi:10.1021/acs.bioconjchem.8b00906 (2019). |
| 225 | Müller, S. et al. Azide-Modified Membrane Lipids: Miscibility with Saturated Phosphatidylcholines. Langmuir 35, 12439-12450, doi:10.1021/acs.langmuir.9b01842 (2019). |
| 224 | Müller, S. et al. Mixing behaviour of bilayer-forming phosphatidylcholines with single-chain alkyl-branched bolalipids: effect of lateral chain length. Biophys. Chem. 244, 1-10, doi:10.1016/j.bpc.2018.10.003 (2019). |
| 223 | Müller, S., Gruhle, K., Meister, A., Hause, G. & Drescher, S. Bolalipid-doped liposomes: Can bolalipids increase the integrity of liposomes exposed to gastrointestinal fluids? Pharmaceutics 11, doi:10.3390/pharmaceutics11120646 (2019). |
| 222 | Kyrilis, F. L., Meister, A. & Kastritis, P. L. Integrative biology of native cell extracts: A new era for structural characterization of life processes. Biol. Chem. 400, 831-846, doi:10.1515/hsz-2018-0445 (2019). |
| *221 | Kumar, A., Kuhn, L. T. & Balbach, J. In-cell NMR: Analysis of protein–small molecule interactions, metabolic processes, and protein phosphorylation. Int. J. Mol. Sci. 20, doi:10.3390/ijms20020378 (2019). |
| 220 | Klamt, A., Nagarathinam, K., Tanabe, M., Kumar, A. & Balbach, J. Hyperbolic Pressure-Temperature Phase Diagram of the Zinc-Finger Protein apoKti11 Detected by NMR Spectroscopy. J Phys Chem B 123, 792-801, doi:10.1021/acs.jpcb.8b11019 (2019). |
| 219 | Hampoelz, B., Andres-Pons, A., Kastritis, P. & Beck, M. in Annu. Rev. Biophys. Vol. 48 515-536 (Annual Reviews Inc., 2019). |
| 218 | Graf, G., Drescher, S., Meister, A., Garamus, V. M. & Blume, A. Nanofiber formation and polymerization of bolalipids with diacetylene-modified single alkyl chains. J Phys Chem B 123, 1566-1577, doi:10.1021/acs.jpcb.8b11945 (2019). |
| 217 | Evgrafova, Z. et al. Modulation of amyloid β peptide aggregation by hydrophilic polymers. Phys. Chem. Chem. Phys. 21, 20999-21006, doi:10.1039/c9cp02683e (2019). |
| 216 | Evgrafova, Z. et al. Probing Polymer Chain Conformation and Fibril Formation of Peptide Conjugates. ChemPhysChem 20, 236-240, doi:10.1002/cphc.201800867 (2019). |
| 215 | Danielczak, B., Meister, A. & Keller, S. Influence of Mg 2+ and Ca 2+ on nanodisc formation by diisobutylene/maleic acid (DIBMA) copolymer. Chem. Phys. Lipids 221, 30-38, doi:10.1016/j.chemphyslip.2019.03.004 (2019). |
| 214 | Canalp, M. B., Meister, A. & Binder, W. H. Secondary structure of end group functionalized oligomeric-l-lysines: Investigations of solvent and structure dependent helicity. RSC Adv. 9, 21707-21714, doi:10.1039/c9ra03099a (2019). |
| 213 | Camilles, M., Link, S., Balbach, J., Saalwächter, K. & Krushelnitsky, A. Corrigendum to quantitative NMR study of heat-induced aggregation of eye-lens crystallin proteins under crowding conditions.(BBA – Proteins and Proteomics (2018) 1866(10) (1055–1061), (S1570963918301195), (10.1016/j.bbapap.2018.07.007)). Biochim. Biophys. Acta Proteins Proteomics 1867, 453-454, doi:10.1016/j.bbapap.2019.02.001 (2019). |
| 212 | Bonnet, C. et al. Hybrid double-chain maltose-based detergents: Synthesis and colloidal and biochemical evaluation. J. Org. Chem. 84, 10606-10614, doi:10.1021/acs.joc.9b00873 (2019). |
| 2018 | |
| 211 | Wersig, T. et al. Indomethacin functionalised poly(glycerol adipate) nanospheres as promising candidates for modified drug release. Eur. J. Pharm. Sci. 123, 350-361, doi:10.1016/j.ejps.2018.07.053 (2018). |
| 210 | Werner, S., Ebenhan, J., Haupt, C. & Bacia, K. A Quantitative and Reliable Calibration Standard for Dual-Color Fluorescence Cross-Correlation Spectroscopy. ChemPhysChem 19, 3436-3444, doi:10.1002/cphc.201800576 (2018). |
| 209 | Prochaska, H. et al. A conserved motif promotes HpaB-regulated export of type III effectors from Xanthomonas. Mol. Plant Pathol. 19, 2473-2487, doi:10.1111/mpp.12725 (2018). |
| 208 | Nagarathinam, K. et al. Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism. Nature Communications 9, doi:10.1038/s41467-018-06306-x (2018). |
| 207 | Müller, S., Meister, A., Otto, C., Hause, G. & Drescher, S. Mixing behaviour of asymmetrical glycerol diether bolalipids with saturated and unsaturated phosphatidylcholines. Biophys. Chem. 238, 39-48, doi:10.1016/j.bpc.2018.04.005 (2018). |
| 206 | Lechner, B. D. et al. Controlling the Miscibility of X-Shaped Bolapolyphiles in Lipid Membranes by Varying the Chemical Structure and Size of the Polyphile Polar Headgroup. J Phys Chem B 122, 10861-10871, doi:10.1021/acs.jpcb.8b08582 (2018). |
| 205 | Kumar, A., Kuhn, L. T. & Balbach, J. A Cu2+ complex induces the aggregation of human papillomavirus oncoprotein E6 and stabilizes p53. FEBS J. 285, 3013-3025, doi:10.1111/febs.14591 (2018). |
| 204 | Kumar, A. et al. Phosphorylation-induced unfolding regulates p19INK4d during the human cell cycle. Proc. Natl. Acad. Sci. U. S. A. 115, 3344-3349, doi:10.1073/pnas.1719774115 (2018). |
| 203 | Kastritis, P. L. & Gavin, A. C. Enzymatic complexes across scales. Essays Biochem. 62, 501-514, doi:10.1042/EBC20180008 (2018). |
| 202 | Gruhle, K., Müller, S., Meister, A. & Drescher, S. Synthesis and aggregation behaviour of single-chain, 1,32-alkyl branched bis(phosphocholines): Effect of lateral chain length. Org. Biomol. Chem. 16, 2711-2724, doi:10.1039/c8ob00424b (2018). |
| 201 | Dreydoppel, M. et al. Equilibrium and Kinetic Unfolding of GB1: Stabilization of the Native State by Pressure. J Phys Chem B 122, 8846-8852, doi:10.1021/acs.jpcb.8b06888 (2018). |
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