@misc{HiggsHarrisHegeretal.2018, author = {Higgs, Eric S. and Harris, Jim A. and Heger, Tina and Hobbs, Richard J. and Murphy, Stephen D. and Suding, Katharine N.}, title = {Keep ecological restoration open and flexible}, series = {Nature Ecology \& Evolution}, volume = {2}, journal = {Nature Ecology \& Evolution}, number = {4}, publisher = {Nature Publ. Group}, address = {London}, issn = {2397-334X}, doi = {10.1038/s41559-018-0483-9}, pages = {580 -- 580}, year = {2018}, language = {en} } @misc{KramerLenhard2017, author = {Kramer, Elena M. and Lenhard, Michael}, title = {Shape and form in plant development}, series = {Seminars in cell \& developmental biology}, volume = {79}, journal = {Seminars in cell \& developmental biology}, publisher = {Elsevier}, address = {London}, issn = {1084-9521}, doi = {10.1016/j.semcdb.2017.11.004}, pages = {1 -- 2}, year = {2017}, language = {en} } @misc{BestZhengBorgiaetal.2018, author = {Best, Robert B. and Zheng, Wenwei and Borgia, Alessandro and Buholzer, Karin and Borgia, Madeleine B. and Hofmann, Hagen and Soranno, Andrea and Nettels, Daniel and Gast, Klaus and Grishaev, Alexander and Schuler, Benjamin}, title = {Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"}, series = {Science}, volume = {361}, journal = {Science}, number = {6405}, publisher = {American Assoc. for the Advancement of Science}, address = {Washington}, issn = {0036-8075}, doi = {10.1126/science.aar7101}, pages = {2}, year = {2018}, abstract = {Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Forster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction.}, language = {en} } @misc{SicardLenhard2018, author = {Sicard, Adrien and Lenhard, Michael}, title = {Capsella}, series = {Current biology}, volume = {28}, journal = {Current biology}, number = {17}, publisher = {Cell Press}, address = {Cambridge}, issn = {0960-9822}, doi = {10.1016/j.cub.2018.06.033}, pages = {R920 -- R921}, year = {2018}, language = {en} } @misc{AlbersUestuenWitzeletal.2018, author = {Albers, Philip and Uestuen, Suayib and Witzel, Katja and Bornke, Frederik}, title = {Identification of a novel target of the bacterial effector HopZ1a}, series = {Phytopathology}, volume = {108}, journal = {Phytopathology}, number = {10}, publisher = {American Phytopathological Society}, address = {Saint Paul}, issn = {0031-949X}, pages = {1}, year = {2018}, abstract = {The plant pathogen Pseudomonas syringae is a gram-negative bacterium which infects a wide range of plant species including important crops plants. To suppress plant immunity and cause disease P.syringae injects type-III effector proteins (T3Es) into the plant cell cytosol. In this study, we identified a novel target of the well characterized bacterial T3E HopZ1a. HopZ1a is an acetyltransferase that was shown to disrupt vesicle transport during innate immunity by acetylating tubulin. Using a yeast-two-hybrid screen approach, we identified a REMORIN (REM) protein from tobacco as a novel HopZ1a target. HopZ1a interacts with REM at the plasma membrane (PM) as shown by split-YFP experiments. Interestingly, we found that PBS1, a well-known kinase involved in plant immunity also interacts with REM in pull-down assays, and at the PM as shown by BiFC. Furthermore, we confirmed that REM is phosphorylated by PBS1 in vitro. Overexpression of REM provokes the upregulation of defense genes and leads to disease-like phenotypes pointing to a role of REM in plant immune signaling. Further protein-protein interaction studies reveal novel REM binding partners with a possible role in plant immune signaling. Thus, REM might act as an assembly hub for an immune signaling complex targeted by HopZ1a. Taken together, this is the first report describing that a REM protein is targeted by a bacterial effector. How HopZ1a might mechanistically manipulate the plant immune system through interfering with REM function will be discussed.}, language = {en} } @misc{MesserschmidtMachensHochreinetal.2018, author = {Messerschmidt, Katrin and Machens, Fabian and Hochrein, Lena and Naseri, Gita}, title = {Orthogonal, light-inducible protein expression platform in yeast Sacchararomyces cerevisiae}, series = {New biotechnology}, volume = {44}, journal = {New biotechnology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1871-6784}, doi = {10.1016/j.nbt.2018.05.153}, pages = {S19 -- S19}, year = {2018}, language = {en} } @misc{Graef2018, author = {Gr{\"a}f, Ralph}, title = {Comparative Biology of Centrosomal Structures in Eukaryotes}, series = {Cells}, volume = {7}, journal = {Cells}, number = {11}, publisher = {MDPI}, address = {Basel}, issn = {2073-4409}, doi = {10.3390/cells7110202}, pages = {9}, year = {2018}, abstract = {The centrosome is not only the largest and most sophisticated protein complex within a eukaryotic cell, in the light of evolution, it is also one of its most ancient organelles. This special issue of "Cells" features representatives of three main, structurally divergent centrosome types, i.e., centriole-containing centrosomes, yeast spindle pole bodies (SPBs), and amoebozoan nucleus-associated bodies (NABs). Here, I discuss their evolution and their key-functions in microtubule organization, mitosis, and cytokinesis. Furthermore, I provide a brief history of centrosome research and highlight recently emerged topics, such as the role of centrioles in ciliogenesis, the relationship of centrosomes and centriolar satellites, the integration of centrosomal structures into the nuclear envelope and the involvement of centrosomal components in non-centrosomal microtubule organization.}, language = {en} } @misc{BalazadehMuellerRoeber2018, author = {Balazadeh, Salma and M{\"u}ller-R{\"o}ber, Bernd}, title = {A balance to death}, series = {Nature plants}, volume = {4}, journal = {Nature plants}, number = {11}, publisher = {Nature Publ. Group}, address = {London}, issn = {2055-026X}, doi = {10.1038/s41477-018-0279-6}, pages = {863 -- 864}, year = {2018}, abstract = {Leaf senescence plays a crucial role in nutrient recovery in late-stage plant development and requires vast transcriptional reprogramming by transcription factors such as ORESARA1 (ORE1). A proteolytic mechanism is now found to control ORE1 degradation, and thus senescence, during nitrogen starvation.}, language = {en} } @misc{BarlowShengLaietal.2018, author = {Barlow, Axel and Sheng, Gui-Lian and Lai, Xu-Long and Hofreiter, Michael and Paijmans, Johanna L. A.}, title = {Once lost, twice found: Combined analysis of ancient giant panda sequences characterises extinct clade}, series = {Journal of biogeography}, volume = {46}, journal = {Journal of biogeography}, number = {1}, publisher = {Wiley}, address = {Hoboken}, issn = {0305-0270}, doi = {10.1111/jbi.13486}, pages = {251 -- 253}, year = {2018}, language = {en} } @misc{DierschkeHeinken2019, author = {Dierschke, Hartmut and Heinken, Thilo}, title = {Vorwort}, series = {Tuexenia : Mitteilungen der Floristisch-Soziologischen Arbeitsgemeinschaft}, journal = {Tuexenia : Mitteilungen der Floristisch-Soziologischen Arbeitsgemeinschaft}, number = {39}, publisher = {Floristisch-Soziologische Arbeitsgemeinschaft}, address = {G{\"o}ttingen}, issn = {0722-494X}, pages = {7 -- 7}, year = {2019}, language = {de} } @misc{HermanussenSchefflerGrothetal.2019, author = {Hermanussen, Michael and Scheffler, Christiane and Groth, Detlef and Bogin, Barry}, title = {Student work on trends in infant and child growth}, series = {Journal of biological and clinical anthropology : Anthropologischer Anzeiger : Mitteilungsorgan der Gesellschaft f{\"u}r Anthropologie}, volume = {76}, journal = {Journal of biological and clinical anthropology : Anthropologischer Anzeiger : Mitteilungsorgan der Gesellschaft f{\"u}r Anthropologie}, number = {5}, publisher = {Schweizerbart}, address = {Stuttgart}, issn = {0003-5548}, doi = {10.1127/anthranz/2019/1052}, pages = {363 -- 364}, year = {2019}, language = {en} } @misc{deVeraAlawiBackhausetal.2019, author = {de Vera, Jean-Pierre Paul and Alawi, Mashal and Backhaus, Theresa and Baque, Mickael and Billi, Daniela and Boettger, Ute and Berger, Thomas and Bohmeier, Maria and Cockell, Charles and Demets, Rene and de la Torre Noetzel, Rosa and Edwards, Howell and Elsaesser, Andreas and Fagliarone, Claudia and Fiedler, Annelie and Foing, Bernard and Foucher, Frederic and Fritz, J{\"o}rg and Hanke, Franziska and Herzog, Thomas and Horneck, Gerda and H{\"u}bers, Heinz-Wilhelm and Huwe, Bj{\"o}rn and Joshi, Jasmin Radha and Kozyrovska, Natalia and Kruchten, Martha and Lasch, Peter and Lee, Natuschka and Leuko, Stefan and Leya, Thomas and Lorek, Andreas and Martinez-Frias, Jesus and Meessen, Joachim and Moritz, Sophie and Moeller, Ralf and Olsson-Francis, Karen and Onofri, Silvano and Ott, Sieglinde and Pacelli, Claudia and Podolich, Olga and Rabbow, Elke and Reitz, G{\"u}nther and Rettberg, Petra and Reva, Oleg and Rothschild, Lynn and Garcia Sancho, Leo and Schulze-Makuch, Dirk and Selbmann, Laura and Serrano, Paloma and Szewzyk, Ulrich and Verseux, Cyprien and Wadsworth, Jennifer and Wagner, Dirk and Westall, Frances and Wolter, David and Zucconi, Laura}, title = {Limits of life and the habitability of Mars}, series = {Astrobiology}, volume = {19}, journal = {Astrobiology}, number = {2}, publisher = {Liebert}, address = {New Rochelle}, issn = {1531-1074}, doi = {10.1089/ast.2018.1897}, pages = {145 -- 157}, year = {2019}, abstract = {BIOMEX (BIOlogy and Mars EXperiment) is an ESA/Roscosmos space exposure experiment housed within the exposure facility EXPOSE-R2 outside the Zvezda module on the International Space Station (ISS). The design of the multiuser facility supports-among others-the BIOMEX investigations into the stability and level of degradation of space-exposed biosignatures such as pigments, secondary metabolites, and cell surfaces in contact with a terrestrial and Mars analog mineral environment. In parallel, analysis on the viability of the investigated organisms has provided relevant data for evaluation of the habitability of Mars, for the limits of life, and for the likelihood of an interplanetary transfer of life (theory of lithopanspermia). In this project, lichens, archaea, bacteria, cyanobacteria, snow/permafrost algae, meristematic black fungi, and bryophytes from alpine and polar habitats were embedded, grown, and cultured on a mixture of martian and lunar regolith analogs or other terrestrial minerals. The organisms and regolith analogs and terrestrial mineral mixtures were then exposed to space and to simulated Mars-like conditions by way of the EXPOSE-R2 facility. In this special issue, we present the first set of data obtained in reference to our investigation into the habitability of Mars and limits of life. This project was initiated and implemented by the BIOMEX group, an international and interdisciplinary consortium of 30 institutes in 12 countries on 3 continents. Preflight tests for sample selection, results from ground-based simulation experiments, and the space experiments themselves are presented and include a complete overview of the scientific processes required for this space experiment and postflight analysis. The presented BIOMEX concept could be scaled up to future exposure experiments on the Moon and will serve as a pretest in low Earth orbit.}, language = {en} } @misc{SowemimoBorcherdsKnoxBrownetal.2019, author = {Sowemimo, Oluwakemi and Borcherds, Wade and Knox-Brown, Patrick and Rindfleisch, Tobias and Thalhammer, Anja and Daughdrill, Gary}, title = {Evolution of Transient Helicity and Disorder in Late Embryogenesis Abundant Protein COR15A}, series = {Biophysical journal}, volume = {116}, journal = {Biophysical journal}, number = {3}, publisher = {Cell Press}, address = {Cambridge}, issn = {0006-3495}, doi = {10.1016/j.bpj.2018.11.2553}, pages = {473A -- 473A}, year = {2019}, abstract = {Cold regulated protein 15A (COR15A) is a nuclear encoded, intrinsically disordered protein that is found in Arabidopsis thaliana. It belongs to the Late Embryogenesis Abundant (LEA) family of proteins and is responsible for increased freezing tolerance in plants. COR15A is intrinsically disordered in dilute solutions and adopts a helical structure upon dehydration or in the presence of co-solutes such as TFE and ethylene glycol. This helical structure is thought to be important for protecting plants from dehydration induced by freezing. Multiple protein sequence alignments revealed the presence of several conserved glycine residues that we hypothesize keeps COR15A from becoming helical in dilute solutions. Using AGADIR, the change in helical content of COR15A when these conserved glycine residues were mutated to alanine residues was predicted. Based on the predictions, glycine to alanine mutants were made at position 68, and 54,68,81, and 84. Labeled samples of wildtype COR15A and mutant proteins were purified and NMR experiments were performed to examine any structural changes induced by the mutations. To test the effects of dehydration on the structure of COR15A, trifluoroethanol, an alcohol based co solvent that is proposed to induce/stabilize helical structure in peptides was added to the NMR samples, and the results of the experiment showed an increase in helical content, compared to the samples without TFE. To test the functional differences between wild type and the mutants, liposome leakage assays were performed. The results from these assays suggest the more helical mutants may augment membrane stability.}, language = {en} } @misc{Arnold2019, author = {Arnold, Patrick}, title = {The origin of morphological integration and modularity in the Mammalian Neck}, series = {Journal of morphology}, volume = {280}, journal = {Journal of morphology}, publisher = {Wiley}, address = {Hoboken}, issn = {0362-2525}, doi = {10.1002/jmor.21003}, pages = {S13 -- S13}, year = {2019}, language = {en} } @misc{RadchukKramerSchadtGrimm2019, author = {Radchuk, Viktoriia and Kramer-Schadt, Stephanie and Grimm, Volker}, title = {Transferability of mechanistic ecological models is about emergence}, series = {Trends in ecology and evolution}, volume = {34}, journal = {Trends in ecology and evolution}, number = {6}, publisher = {Elsevier}, address = {London}, issn = {0169-5347}, doi = {10.1016/j.tree.2019.01.010}, pages = {487 -- 488}, year = {2019}, language = {en} } @misc{NumbergerDreierVullioudetal.2019, author = {Numberger, Daniela and Dreier, Carola and Vullioud, Colin and Gabriel, Guelsah and Greenwood, Alex D. and Grossart, Hans-Peter}, title = {Correction: Recovery of influenza A viruses from lake water and sediments by experimental inoculation (vol 14, e0216880, 2019)}, series = {PLoS one}, volume = {14}, journal = {PLoS one}, number = {6}, publisher = {PLoS}, address = {San Fransisco}, issn = {1932-6203}, doi = {10.1371/journal.pone.0218882}, pages = {1}, year = {2019}, language = {en} } @misc{MogaRobinsonLeimkuehler2019, author = {Moga, A. and Robinson, T. and Leimk{\"u}hler, Silke}, title = {Towards reconstituting a biosynthetic pathway within compartmentalized GUVs}, series = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, volume = {48}, journal = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, publisher = {Springer}, address = {New York}, issn = {0175-7571}, pages = {S218 -- S218}, year = {2019}, language = {en} } @misc{LucknerDunsingDruekeetal.2019, author = {Luckner, Madlen and Dunsing, Valentin and Dr{\"u}ke, Markus and Zuehlke, B. and Petazzi, Roberto Arturo and Chiantia, Salvatore and Herrmann, A.}, title = {Quantifying protein oligomerization directly in living cells}, series = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, volume = {48}, journal = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, publisher = {Springer}, address = {New York}, issn = {0175-7571}, pages = {S183 -- S183}, year = {2019}, language = {en} } @misc{DunsingIrmscherBarbirzetal.2019, author = {Dunsing, Valentin and Irmscher, Tobias and Barbirz, Stefanie and Chiantia, Salvatore}, title = {Microviscosity of bacterial biofilm matrix characterized by fluorescence correlation spectroscopy and single particle tracking}, series = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, volume = {48}, journal = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, publisher = {Springer}, address = {New York}, issn = {0175-7571}, doi = {https://doi.org/10.1007/s00249-019-01373-4}, pages = {S115 -- S115}, year = {2019}, language = {en} } @misc{RodriguezSillkeSteinhoffBojarskietal.2019, author = {Rodriguez-Sillke, Yasmina and Steinhoff, U. and Bojarski, Christian and Lissner, Donata and Schumann, Michael and Branchi, F. and Siegmund, Britta and Glauben, Rainer}, title = {Deep immune profiling of human Peyer´s Patches in patients of inflammatory bowel diseases}, series = {European journal of immunology}, volume = {49}, journal = {European journal of immunology}, publisher = {Wiley}, address = {Weinheim}, issn = {0014-2980}, doi = {10.1002/eji.201970300}, pages = {203 -- 204}, year = {2019}, language = {en} }