2013

Crystal structure of the entire respiratory complex I

Baradaran, R., Berrisford J. M., Minhas G. S., and Sazanov L. A.

Nature. Volume 494, Number Issue 7438, (2013), p.443-448 doi: 10.1038/nature11871

Report of the wwPDB Small-Angle Scattering Task Force: Data Requirements for Biomolecular Modeling and the PDB

Trewhella, J., Henrickson W. A., KLEYWEGT G. J., Sali A., Sato M., Schwede T., Svergun D. I., Tainer J. A., Westbrook J., and Berman H. M.

Structure. Volume 21, Number Issue 6, (2013), p.875-881 doi: 10.1016/j.str.2013.04.020

2012

Structure of the signal transduction protein TRAP (target of RNAIII-activating protein)

Henrick, K., and Hirshberg M.

Acta Crystallographica Section F. Volume 68, Number Part 7, (2012), p.744-750 doi: 10.1107/S1744309112020167

Protein Structure Validation Using Side-Chain Chemical Shifts

Sahakyan, A. B., Cavalli A., VRANKEN W. F., and Vendruscolo M.

The Journal of Physical Chemistry B. Volume 116, Number 16, (2012), p.4754-4759 doi: 10.1021/jp2122054

Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts

Camilloni, C., Simone De A., VRANKEN W. F., and Vendruscolo M.

Biochemistry. Volume 51, Number 11, (2012), p.2224-2231 doi: 10.1021/bi3001825

2011

A novel strategy for NMR resonance assignment and protein structure determination

Lemak, A., GUTMANAS A., Chitayat S., Karra M., Farès C., Sunnerhagen M., and Arrowsmith C. H.

Journal of Biomolecular NMR. Volume 49, Number Issue 1, (2011), p.27-38 doi: 10.1007/s10858-010-9458-0

Assymetric synthesis and conformational analysis by NMR spectroscopy and MD of Aba- and α-MeAba-containing demorphin analogues

Vandormael, B., De Wachter R., Martins J. C., Hendrickx P. M. S., Keresztes A., Ballet S., Mallareddy J. R., Tóth F., Tóth G., and Tourwé D.

ChemMedChem. Volume 6, Number Issue 11, (2011), p.2035-2047 doi: 10.1002/cmdc.201100314

Bayesian estimation of NMR restraint potential and weight: a validation on a representative set of protein structures

Bernard, A., VRANKEN W. F., Bardiaux B., Nilges M., and Malliavin T. E.

Proteins. Volume 79, (2011), p.1525-1537 doi: 10.1002/prot.22980

Structure-based prediction of methyl chemical shifts in proteins

Sahakyan, A. B., VRANKEN W. F., Cavalli A., and Vendruscolo M.

Journal of Biomolecular NMR. Volume 50, Number (Issue 4), (2011), p.331-346 doi: 10.1007/s10858-011-9524-2

Structures of sequential open states in a symmetrical opening transition of the TolC exit duct

Pei, X-Y, Hinchliffe P., SYMMONS M. F., Koronakis E., Benz R., Hughes C., and Koronakis V.

Proceedings of the National Academy of Sciences. Volume 108, Issue 5, (2011), p.2112-2117 doi: 10.1073/pnas.1012588108

Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures

Sahakyan, A. B., VRANKEN W. F., Cavalli A., and Vendruscolo M.

Angewandte Chemie International Edition. Volume 50, (2011), p.9620-9623 doi: 10.1002/anie.201101641

2010

Diversity of monomers in non-ribosomal peptides

CABOCHE, S., Leclère V., Pupin M., Kucherov G., and Jacques P.

Journal of Bacteriology. Volume 192, Number Issue 19, (2010), p.5143-5150 doi: 10.1128/JB.00315-10

Validation of archived chemical shifts through atomic coordinates

Rieping, W., and VRANKEN W. F.

Proteins. Volume 78, Number Issue 3, (2010), p.2482-2489 doi: 10.1002/prot.22756

2009

Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins

Simone, De A., Cavalli A., Hsu S. T., VRANKEN W. F., and Vendruscolo M.

Journal of the American Chemical Society. Volume 131, Number Issue 45, (2009), p.16332-16333 doi: 10.1021/ja904937a