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ja407951x 1..10
www-vendruscolo.ch.cam.ac.uk/biedermann2013jacs.pdf4 Oct 2013: J.; Friesner, R. A. Proc.Natl. Acad. Sci. U.S.A. 2007, 104, 808.(36) Wang, L.; Berne, B. -
201112197 21057..21062
www-vendruscolo.ch.cam.ac.uk/desimone11pnas.pdf15 Jan 2012: rates. Nature 424:805–808. 2. Richardson JS, Richardson DC (2002) Natural beta-sheet proteins use negative designto avoid edge-to-edge aggregation. -
RSC_mb_c0mb00155d 1..12
www-vendruscolo.ch.cam.ac.uk/szczepankiewicz11mbs.pdf4 Feb 2011: Stefani, N. Taddei, G. Ramponi and C. M. Dobson,Nature, 2003, 424, 805–808. -
Reversible inhibition of the ClpP protease via an N-terminal…
www-vendruscolo.ch.cam.ac.uk/vahidi2018pnas.pdf23 Sep 2018: Reversible inhibition of the ClpP protease via anN-terminal conformational switchSiavash Vahidia,b,c,d,1, Zev A. Ripsteinb,d,1, Massimiliano Bonomie, Tairan Yuwena,b,c,d, Mark F. Mabanglob,Jordan B. Juravskyd, Kamran Rizzolob, Algirdas Velyvisa,b,c,d -
Using NMR Chemical Shifts as Structural Restraints in Molecular…
www-vendruscolo.ch.cam.ac.uk/robustelli10s.pdf19 Aug 2010: Structure. Article. Using NMR Chemical Shifts as Structural Restraintsin Molecular Dynamics Simulations of ProteinsPaul Robustelli,1 Kai Kohlhoff,1 Andrea Cavalli,1 and Michele Vendruscolo1,1Department of Chemistry, University of Cambridge Lensfield -
Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes
www-vendruscolo.ch.cam.ac.uk/Bhardwaj-2023-NC.pdf28 Feb 2023: Article https://doi.org/10.1038/s41467-023-36234-4. Amyloidogenic proteins in the SARS-CoV andSARS-CoV-2 proteomes. Taniya Bhardwaj1, Kundlik Gadhave 1, Shivani K. Kapuganti1, Prateek Kumar1,Zacharias Faidon Brotzakis2, Kumar Udit Saumya1, -
Third generation antibody discovery methods: in silico rational design
www-vendruscolo.ch.cam.ac.uk/sormanni2018csr.pdf18 Dec 2018: This journal is The Royal Society of Chemistry 2018 Chem. Soc. Rev., 2018, 47, 9137--9157 | 9137. Cite this: Chem. Soc. Rev., 2018,47, 9137. Third generation antibody discovery methods:in silico rational design. Pietro Sormanni, Francesco A. Aprile -
The amyloid state and its association with protein misfolding diseases
www-vendruscolo.ch.cam.ac.uk/knowles2014nrmcb.pdf16 Jun 2014: The conversion of normally soluble peptides and proteins into intractable amyloid deposits has emerged in recent years as a subject of fundamental importance in scien-tific disciplines ranging from physics and chemistry to biology and medicine1–11
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