% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Bertini:94201,
      author       = {Bertini, I. and Fragai, M. and Luchinat, C. and Melikian,
                      M. and Mylonas, E. and Sarti, N. and Svergun, D. I. and
                      DESY},
      title        = {{I}nterdomain flexibility in full-length matrix
                      metalloproteinase-1 ({MMP}-1)},
      journal      = {The journal of biological chemistry},
      volume       = {284},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PHPPUBDB-11922},
      pages        = {12821-12828},
      year         = {2009},
      abstract     = {The presence of extensive reciprocal conformational freedom
                      between the catalytic and the hemopexin-like domains of
                      full-length matrix metalloproteinase-1 (MMP-1) is
                      demonstrated by NMR and small angle x-ray scattering
                      experiments. This finding is discussed in relation to the
                      essentiality of the hemopexin-like domain for the
                      collagenolytic activity of MMP-1. The conformational freedom
                      experienced by the present system, having the shortest
                      linker between the two domains, when compared with similar
                      findings on MMP-12 and MMP-9 having longer and the longest
                      linker within the family, respectively, suggests this type
                      of conformational freedom to be a general property of all
                      MMPs.},
      keywords     = {Catalysis / Crystallography, X-Ray / Heme / Humans / Matrix
                      Metalloproteinase 1: chemistry / Matrix Metalloproteinase 1:
                      metabolism / Matrix Metalloproteinase 12: chemistry / Matrix
                      Metalloproteinase 9: chemistry / Models, Molecular / Nuclear
                      Magnetic Resonance, Biomolecular / Pliability / Protein
                      Conformation / Protein Structure, Tertiary / Recombinant
                      Proteins: chemistry / Recombinant Proteins: metabolism /
                      Recombinant Proteins (NLM Chemicals) / Heme (NLM Chemicals)
                      / Matrix Metalloproteinase 9 (NLM Chemicals) / Matrix
                      Metalloproteinase 12 (NLM Chemicals) / Matrix
                      Metalloproteinase 1 (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19282283},
      pmc          = {pmc:PMC2676012},
      UT           = {WOS:000265688300027},
      doi          = {10.1074/jbc.M809627200},
      url          = {https://bib-pubdb1.desy.de/record/94201},
}