Nina Morgner

Summary

Affiliation: University of Oxford
Country: UK

Publications

  1. doi request reprint Massign: an assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies
    Nina Morgner
    Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK
    Anal Chem 84:2939-48. 2012
  2. pmc Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
    Carla Schmidt
    Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK
    Nat Commun 4:1985. 2013
  3. pmc Mass spectrometry--from peripheral proteins to membrane motors
    Nina Morgner
    Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 5QY, UK
    J Mol Biol 423:1-13. 2012
  4. pmc Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes
    Ima Obong Ebong
    Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3TA, United Kingdom
    Proc Natl Acad Sci U S A 108:17939-44. 2011
  5. pmc Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding
    Min Zhou
    Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK
    Science 334:380-5. 2011
  6. doi request reprint Linking structural change with functional regulation-insights from mass spectrometry
    Nina Morgner
    Department of Chemistry, University of Oxford, United Kingdom
    Curr Opin Struct Biol 22:44-51. 2012

Collaborators

Detail Information

Publications6

  1. doi request reprint Massign: an assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies
    Nina Morgner
    Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK
    Anal Chem 84:2939-48. 2012
    ..Using a rotary ATPase as a working example, we show how this assignment strategy is capable of determining the stoichiometry and interactions of the 8 different subunits within this 29-subunit assembly...
  2. pmc Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
    Carla Schmidt
    Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK
    Nat Commun 4:1985. 2013
    ....
  3. pmc Mass spectrometry--from peripheral proteins to membrane motors
    Nina Morgner
    Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 5QY, UK
    J Mol Biol 423:1-13. 2012
    ..In this perspective, we track these developments and suggest explanations for the various discoveries made during this research...
  4. pmc Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes
    Ima Obong Ebong
    Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3TA, United Kingdom
    Proc Natl Acad Sci U S A 108:17939-44. 2011
    ..In this case, the K(D) values afford insights into the assembly of ten Hsp90-containing complexes and provide a rationale for the cellular heterogeneity and prevalence of intermediates in the Hsp90 chaperone cycle...
  5. pmc Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding
    Min Zhou
    Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK
    Science 334:380-5. 2011
    ..Consequently, we can link specific lipid and nucleotide binding with distinct regulatory roles...
  6. doi request reprint Linking structural change with functional regulation-insights from mass spectrometry
    Nina Morgner
    Department of Chemistry, University of Oxford, United Kingdom
    Curr Opin Struct Biol 22:44-51. 2012
    ..In this review we focus on recent developments of mass spectrometry (MS) that allow us to unravel the functional 'secrets' of non-covalent molecular machines...