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@ARTICLE{Lapkouski:276466,
      author       = {Lapkouski, Mikalai and Haellberg, Martin},
      title        = {{S}tructure of mitochondrial poly({A}) {RNA} polymerase
                      reveals the structural basis for dimerization, {ATP}
                      selectivity and the {SPAX}4 disease phenotype.},
      journal      = {Nucleic acids symposium series},
      volume       = {43},
      number       = {18},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press8619},
      reportid     = {PUBDB-2015-04674},
      pages        = {9065 - 9075},
      year         = {2015},
      abstract     = {Polyadenylation, performed by poly(A) polymerases (PAPs),
                      is a ubiquitous post-transcriptional modification that plays
                      key roles in multiple aspects of RNA metabolism. Although
                      cytoplasmic and nuclear PAPs have been studied extensively,
                      the mechanism by which mitochondrial PAP (mtPAP) selects
                      adenosine triphosphate over other nucleotides is unknown.
                      Furthermore, mtPAP is unique because it acts as a dimer.
                      However, mtPAPs dimerization requirement remains enigmatic.
                      Here, we show the structural basis for mtPAPs nucleotide
                      selectivity, dimerization and catalysis. Our structures
                      reveal an intricate dimerization interface that features an
                      RNA-recognition module formed through strand
                      complementation. Further, we propose the structural basis
                      for the N478D mutation that drastically reduces the length
                      of poly(A) tails on mitochondrial mRNAs in patients with
                      spastic ataxia 4 (SPAX4), a severe and progressive
                      neurodegenerative disease.},
      cin          = {KI / EMBL / CSSB-KI-MH},
      ddc          = {540},
      cid          = {I:(DE-H253)KI-20130912 / I:(DE-H253)EMBL-20120731 /
                      I:(DE-H253)CSSB-KI-MH-20210520},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G3 - PETRA III (POF3-622) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G3 /
                      G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26319014},
      pmc          = {pmc:PMC4605311},
      UT           = {WOS:000366406500043},
      doi          = {10.1093/nar/gkv861},
      url          = {https://bib-pubdb1.desy.de/record/276466},
}