N. Vasisht

发表

The Structure and Receptor Binding Properties of the 1918 Influenza Hemagglutinin

D. J. Stevens, J. Skehel, D. Wiley, 2004, Science.

Structure and catalytic mechanism of the human histone methyltransferase SET7/9

Geoff Kelly, Steven J. Gamblin, Jon R. Wilson, 2003, Nature.

Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica.

N. Vasisht, A. Bolhuis, G. W. Hutcheon, 2005, Extremophiles : life under extreme conditions.

The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain

R. Hartmann-Petersen, N. Vasisht, R. Spooner, 2013, The Biochemical journal.

Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria.

N. Vasisht, S. Mendel, C. F. Matos, 2011, Biochimica et biophysica acta.

Gamblin Hemagglutinin The Structure and Receptor Binding Properties of the 1918 Influenza

J. Skehel, D. Wiley, S. Gamblin, 2012 .

Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.

K. Henrick, M. Hirshberg, J. Corrie, 1998, Biochemistry.

Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores

J. V. van Dijl, N. Vasisht, Corinne J. Smith, 2013, Biochimica et biophysica acta.

Structure of TatA Paralog, TatE, Suggests a Structurally Homogeneous Form of Tat Protein Translocase That Transports Folded Proteins of Differing Diameter

N. Vasisht, Corinne J. Smith, C. Robinson, 2011, The Journal of Biological Chemistry.

Salt Sensitivity of Minimal Twin Arginine Translocases

J. V. van Dijl, N. Vasisht, René van der Ploeg, 2011, The Journal of Biological Chemistry.

Characterisation of a highly stable α-amylase from the halophilic archaeon Haloarcula hispanica

N. Vasisht, A. Bolhuis, G. W. Hutcheon, 2005, Extremophiles.

The crystal structure of the globular domain of sheep prion protein.

P. Bayley, E. Dodson, C. Verma, 2004, Journal of molecular biology.

Four distinct structural domains in Clostridium difficile toxin B visualized using SAXS.

N. Fairweather, D. Svergun, E. Carpenter, 2010, Journal of molecular biology.