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21 - 26 of 26 search results for KA :PC53 |u:www-vendruscolo.ch.cam.ac.uk where 0 match all words and 26 match some words.
  1. Results that match 1 of 2 words

  2. Nanobodies raised against monomeric ɑ-synuclein inhibit fibril…

    www-vendruscolo.ch.cam.ac.uk/iljina2017bmcb.pdf
    17 Sep 2017: RESEARCH ARTICLE Open Access. Nanobodies raised against monomericɑ-synuclein inhibit fibril formation anddestabilize toxic oligomeric speciesMarija Iljina1†, Liu Hong1,2, Mathew H. Horrocks1,3, Marthe H. Ludtmann4, Minee L. Choi4, Craig D. Hughes5
  3. Submitted 16 March 2018Accepted 8 June 2018Published 4 July ...

    www-vendruscolo.ch.cam.ac.uk/papaleo2018pj.pdf
    23 Sep 2018: Submitted 16 March 2018Accepted 8 June 2018Published 4 July 2018. Corresponding authorKresten Lindorff-Larsen,lindorff@bio.ku.dk. Academic editorCamillo Rosano. Additional Information andDeclarations can be found onpage 16. DOI 10.7717/peerj.5125.
  4. Cyclophilin A catalyzes proline isomerization by anelectrostatic…

    www-vendruscolo.ch.cam.ac.uk/camilloni2014pnas.pdf
    12 Aug 2014: J Am Chem Soc 132(4):1220–1221.31. Robustelli P, Stafford KA, Palmer AG, 3rd (2012) Interpreting protein structural dy-.
  5. bi5b00345 1..12

    www-vendruscolo.ch.cam.ac.uk/pustovalova2015b.pdf
    28 Nov 2015: Probing the Residual Structure of the Low Populated DenaturedState of ADA2h under Folding Conditions by Relaxation DispersionNuclear Magnetic Resonance SpectroscopyYulia Pustovalova,† Predrag Kukic,‡ Michele Vendruscolo,‡ and Dmitry M. Korzhnev
  6. pnas201213624 132..140

    www-vendruscolo.ch.cam.ac.uk/ciryam13pnas.pdf
    10 Jan 2013: In vivo translation rates can substantially delay thecotranslational folding of the Escherichia colicytosolic proteomePrajwal Ciryama,b, Richard I. Morimotob, Michele Vendruscoloa, Christopher M. Dobsona, and Edward P. O’Briena,1. aDepartment of
  7. 14945019074674 1..31

    www-vendruscolo.ch.cam.ac.uk/kitevski-leblanc2017elife.pdf
    17 Sep 2017: For correspondence: durocher@. lunenfeld.ca (DD); kay@pound. med.utoronto.ca (LEK). †These authors contributed. equally to this work‡These authors also contributed. equally to this work. Present address: The Francis. Crick Research Institute,

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