Dr Dominika Gruszka: Publications

Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Nature Communications Springer Nature 6:1 (2015) 7271

Authors:

Dominika T Gruszka, Fiona Whelan, Oliver E Farrance, Herman KH Fung, Emanuele Paci, Cy M Jeffries, Dmitri I Svergun, Clair Baldock, Christoph G Baumann, David J Brockwell, Jennifer R Potts, Jane Clarke

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Corrigendum to “The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger” [J. Mol. Biol. 407 (2011) 149–170]

Journal of Molecular Biology Elsevier 419:3-4 (2012) 275-276

Authors:

Sebastian Eustermann, Hortense Videler, Ji-Chun Yang, Paul T Cole, Dominika Gruszka, Dmitry Veprintsev, David Neuhaus

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Staphylococcal biofilm-forming protein has a contiguous rod-like structure

Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences 109:17 (2012) e1011-e1018

Authors:

Dominika T Gruszka, Justyna A Wojdyla, Richard J Bingham, Johan P Turkenburg, Iain W Manfield, Annette Steward, Andrew P Leech, Joan A Geoghegan, Timothy J Foster, Jane Clarke, Jennifer R Potts

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The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger

Journal of Molecular Biology Elsevier 407:1 (2011) 149-170

Authors:

Sebastian Eustermann, Hortense Videler, Ji-Chun Yang, Paul T Cole, Dominika Gruszka, Dmitry Veprintsev, David Neuhaus

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Role of Surface Protein SasG in Biofilm Formation by Staphylococcus aureus

Journal of Bacteriology American Society for Microbiology 192:21 (2010) 5663-5673

Authors:

Joan A Geoghegan, Rebecca M Corrigan, Dominika T Gruszka, Pietro Speziale, James P O'Gara, Jennifer R Potts, Timothy J Foster

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Dr Dominika Gruszka

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Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Authors:

Corrigendum to “The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger” [J. Mol. Biol. 407 (2011) 149–170]

Authors:

Staphylococcal biofilm-forming protein has a contiguous rod-like structure

Authors:

The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger

Authors:

Role of Surface Protein SasG in Biofilm Formation by Staphylococcus aureus

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Dr Dominika Gruszka

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Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Authors:

Corrigendum to “The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger” [J. Mol. Biol. 407 (2011) 149–170]

Authors:

Staphylococcal biofilm-forming protein has a contiguous rod-like structure

Authors:

The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger

Authors:

Role of Surface Protein SasG in Biofilm Formation by Staphylococcus aureus

Authors: