@article{TuckerBoehningGaeseFaganetal.2018,
  author    = {Tucker, Marlee A. and Boehning-Gaese, Katrin and Fagan, William F. and Fryxell, John M. and Van Moorter, Bram and Alberts, Susan C. and Ali, Abdullahi H. and Allen, Andrew M. and Attias, Nina and Avgar, Tal and Bartlam-Brooks, Hattie and Bayarbaatar, Buuveibaatar and Belant, Jerrold L. and Bertassoni, Alessandra and Beyer, Dean and Bidner, Laura and van Beest, Floris M. and Blake, Stephen and Blaum, Niels and Bracis, Chloe and Brown, Danielle and de Bruyn, P. J. Nico and Cagnacci, Francesca and Calabrese, Justin M. and Camilo-Alves, Constanca and Chamaille-Jammes, Simon and Chiaradia, Andre and Davidson, Sarah C. and Dennis, Todd and DeStefano, Stephen and Diefenbach, Duane and Douglas-Hamilton, Iain and Fennessy, Julian and Fichtel, Claudia and Fiedler, Wolfgang and Fischer, Christina and Fischhoff, Ilya and Fleming, Christen H. and Ford, Adam T. and Fritz, Susanne A. and Gehr, Benedikt and Goheen, Jacob R. and Gurarie, Eliezer and Hebblewhite, Mark and Heurich, Marco and Hewison, A. J. Mark and Hof, Christian and Hurme, Edward and Isbell, Lynne A. and Janssen, Rene and Jeltsch, Florian and Kaczensky, Petra and Kane, Adam and Kappeler, Peter M. and Kauffman, Matthew and Kays, Roland and Kimuyu, Duncan and Koch, Flavia and Kranstauber, Bart and LaPoint, Scott and Leimgruber, Peter and Linnell, John D. C. and Lopez-Lopez, Pascual and Markham, A. Catherine and Mattisson, Jenny and Medici, Emilia Patricia and Mellone, Ugo and Merrill, Evelyn and Mourao, Guilherme de Miranda and Morato, Ronaldo G. and Morellet, Nicolas and Morrison, Thomas A. and Diaz-Munoz, Samuel L. and Mysterud, Atle and Nandintsetseg, Dejid and Nathan, Ran and Niamir, Aidin and Odden, John and Oliveira-Santos, Luiz Gustavo R. and Olson, Kirk A. and Patterson, Bruce D. and de Paula, Rogerio Cunha and Pedrotti, Luca and Reineking, Bjorn and Rimmler, Martin and Rogers, Tracey L. and Rolandsen, Christer Moe and Rosenberry, Christopher S. and Rubenstein, Daniel I. and Safi, Kamran and Said, Sonia and Sapir, Nir and Sawyer, Hall and Schmidt, Niels Martin and Selva, Nuria and Sergiel, Agnieszka and Shiilegdamba, Enkhtuvshin and Silva, Joao Paulo and Singh, Navinder and Solberg, Erling J. and Spiegel, Orr and Strand, Olav and Sundaresan, Siva and Ullmann, Wiebke and Voigt, Ulrich and Wall, Jake and Wattles, David and Wikelski, Martin and Wilmers, Christopher C. and Wilson, John W. and Wittemyer, George and Zieba, Filip and Zwijacz-Kozica, Tomasz and Mueller, Thomas},
  title     = {Moving in the Anthropocene},
  series = {Science},
  volume    = {359},
  journal   = {Science},
  number    = {6374},
  publisher = {American Assoc. for the Advancement of Science},
  address   = {Washington},
  issn      = {0036-8075},
  doi       = {10.1126/science.aam9712},
  pages     = {466 -- 469},
  year      = {2018},
  abstract  = {Animal movement is fundamental for ecosystem functioning and species survival, yet the effects of the anthropogenic footprint on animal movements have not been estimated across species. Using a unique GPS-tracking database of 803 individuals across 57 species, we found that movements of mammals in areas with a comparatively high human footprint were on average one-half to one-third the extent of their movements in areas with a low human footprint. We attribute this reduction to behavioral changes of individual animals and to the exclusion of species with long-range movements from areas with higher human impact. Global loss of vagility alters a key ecological trait of animals that affects not only population persistence but also ecosystem processes such as predator-prey interactions, nutrient cycling, and disease transmission.},
  language  = {en}
}
@article{KirkKallen2006,
  author    = {Kirk, John M. and Kallen, Jeffrey L.},
  title     = {Irish standard English},
  series = {The Celtic Englishes IV : the interface between English and the Celtic languages ; proceedings of the fourth international colloquium on the "Celtic Englishes" held at the University of Potsdam in Golm (Germany) from 22-26 September 2004},
  journal   = {The Celtic Englishes IV : the interface between English and the Celtic languages ; proceedings of the fourth international colloquium on the "Celtic Englishes" held at the University of Potsdam in Golm (Germany) from 22-26 September 2004},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-40948},
  pages     = {88 -- 113},
  year      = {2006},
  abstract  = {Content: 1. Introduction 2. ICE-Ireland and the Irish Language 3. Grammatical Features 3.1. Perfective Aspect 3.2. Reflexive Pronouns 3.3. Inversion and Embedded Clauses 4. Conclusion},
  language  = {en}
}
@article{LimFriemelMarumetal.2013,
  author    = {Lim, Sze Chern and Friemel, Martin and Marum, Justine E. and Tucker, Elena J. and Bruno, Damien L. and Riley, Lisa G. and Christodoulou, John and Kirk, Edwin P. and Boneh, Avihu and DeGennaro, Christine M. and Springer, Michael and Mootha, Vamsi K. and Rouault, Tracey A. and Leimk{\"u}hler, Silke and Thorburn, David R. and Compton, Alison G.},
  title     = {Mutations in LYRM4, encoding ironsulfur cluster biogenesis factor ISD11, cause deficiency of multiple respiratory chain complexes},
  series = {Human molecular genetics},
  volume    = {22},
  journal   = {Human molecular genetics},
  number    = {22},
  publisher = {Oxford Univ. Press},
  address   = {Oxford},
  issn      = {0964-6906},
  doi       = {10.1093/hmg/ddt295},
  pages     = {4460 -- 4473},
  year      = {2013},
  abstract  = {Ironsulfur clusters (ISCs) are important prosthetic groups that define the functions of many proteins. Proteins with ISCs (called ironsulfur or FeS proteins) are present in mitochondria, the cytosol, the endoplasmic reticulum and the nucleus. They participate in various biological pathways including oxidative phosphorylation (OXPHOS), the citric acid cycle, iron homeostasis, heme biosynthesis and DNA repair. Here, we report a homozygous mutation in LYRM4 in two patients with combined OXPHOS deficiency. LYRM4 encodes the ISD11 protein, which forms a complex with, and stabilizes, the sulfur donor NFS1. The homozygous mutation (c.203GT, p.R68L) was identified via massively parallel sequencing of 1000 mitochondrial genes (MitoExome sequencing) in a patient with deficiency of complexes I, II and III in muscle and liver. These three complexes contain ISCs. Sanger sequencing identified the same mutation in his similarly affected cousin, who had a more severe phenotype and died while a neonate. Complex IV was also deficient in her skeletal muscle. Several other FeS proteins were also affected in both patients, including the aconitases and ferrochelatase. Mutant ISD11 only partially complemented for an ISD11 deletion in yeast. Our in vitro studies showed that the l-cysteine desulfurase activity of NFS1 was barely present when co-expressed with mutant ISD11. Our findings are consistent with a defect in the early step of ISC assembly affecting a broad variety of FeS proteins. The differences in biochemical and clinical features between the two patients may relate to limited availability of cysteine in the newborn period and suggest a potential approach to therapy.},
  language  = {en}
}