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Results: 1-21 |
Results: 21
Unraveling the Cu2+ binding sites in the C-terminal domain of the murine prion protein: A pulse EPR and ENDOR study
Authors: Van Doorslaer, S Cereghetti, GM Glockshuber, R Schweiger, A
Citation: S. Van Doorslaer et al., Unraveling the Cu2+ binding sites in the C-terminal domain of the murine prion protein: A pulse EPR and ENDOR study, J PHYS CH B, 105(8), 2001, pp. 1631-1639
Folding dynamics and energetics of recombinant prion proteins
Authors: Glockshuber, R
Citation: R. Glockshuber, Folding dynamics and energetics of recombinant prion proteins, ADV PROTEIN, 57, 2001, pp. 83
Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: evidence from in vitro FimH binding
Authors: Zhou, G Mo, WJ Sebbel, P Min, GW Neubert, TA Glockshuber, R Wu, XR Sun, TT Kong, XP
Citation: G. Zhou et al., Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: evidence from in vitro FimH binding, J CELL SCI, 114(22), 2001, pp. 4095-4103
Protein folding and assembly
Authors: Glockshuber, R
Citation: R. Glockshuber, Protein folding and assembly, CHIMIA, 55(4), 2001, pp. 281-285
Electron paramagnetic resonance evidence far binding of Cu2+ to the C-terminal domain of the murine prion protein
Authors: Cereghetti, GM Schweiger, A Glockshuber, R Van Doorslaer, S
Citation: Gm. Cereghetti et al., Electron paramagnetic resonance evidence far binding of Cu2+ to the C-terminal domain of the murine prion protein, BIOPHYS J, 81(1), 2001, pp. 516-525
Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA
Authors: Winter, J Neubauer, P Glockshuber, R Rudolph, R
Citation: J. Winter et al., Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA, J BIOTECH, 84(2), 2000, pp. 175-185
Influence of the pK(a) value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases
Authors: Mossner, E Iwai, H Glockshuber, R
Citation: E. Mossner et al., Influence of the pK(a) value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases, FEBS LETTER, 477(1-2), 2000, pp. 21-26
Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli
Authors: Hermanns, U Sebbel, P Eggli, V Glockshuber, R
Citation: U. Hermanns et al., Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli, BIOCHEM, 39(38), 2000, pp. 11564-11570
Structural biology of prion proteins
Authors: Wuthrich, K Riek, R Wider, G Garcia, FL Liu, A Zahn, R Billeter, M Hornemann, S Glockshuber, R
Citation: K. Wuthrich et al., Structural biology of prion proteins, TRANSF CL B, 6(1), 1999, pp. 31-31
Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates
Authors: Wildegger, G Liemann, S Glockshuber, R
Citation: G. Wildegger et al., Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates, NAT ST BIOL, 6(6), 1999, pp. 550-553
Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR
Authors: Pellecchia, M Sebbel, P Hermanns, U Wuthrich, K Glockshuber, R
Citation: M. Pellecchia et al., Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR, NAT ST BIOL, 6(4), 1999, pp. 336-339
Fluorescence quenching in the DsbA protein from Escherichia coli: Completepicture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan
Authors: Sillen, A Hennecke, J Roethlisberger, D Glockshuber, R Engelborghs, Y
Citation: A. Sillen et al., Fluorescence quenching in the DsbA protein from Escherichia coli: Completepicture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan, PROTEINS, 37(2), 1999, pp. 253-263
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm
Authors: Jonda, S Huber-Wunderlich, M Glockshuber, R Mossner, E
Citation: S. Jonda et al., Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm, EMBO J, 18(12), 1999, pp. 3271-3281
Protein folding - Where do the electrons go?
Authors: Glockshuber, R
Citation: R. Glockshuber, Protein folding - Where do the electrons go?, NATURE, 401(6748), 1999, pp. 30-31
Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
Authors: Hennecke, J Sebbel, P Glockshuber, R
Citation: J. Hennecke et al., Random circular permutation of DsbA reveals segments that are essential for protein folding and stability, J MOL BIOL, 286(4), 1999, pp. 1197-1215
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli
Authors: Mossner, E Huber-Wunderlich, M Rietsch, A Beckwith, J Glockshuber, R Aslund, F
Citation: E. Mossner et al., Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli, J BIOL CHEM, 274(36), 1999, pp. 25254-25259
Circularly permuted variants of the green fluorescent protein
Authors: Topell, S Hennecke, J Glockshuber, R
Citation: S. Topell et al., Circularly permuted variants of the green fluorescent protein, FEBS LETTER, 457(2), 1999, pp. 283-289
Peptides and proteins in neurodegenerative disease: Helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy
Authors: Liu, AZ Riek, P Zahn, R Hornemann, S Glockshuber, R Wuthrich, K
Citation: Az. Liu et al., Peptides and proteins in neurodegenerative disease: Helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy, BIOPOLYMERS, 51(2), 1999, pp. 145-152
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
Authors: Liemann, S Glockshuber, R
Citation: S. Liemann et R. Glockshuber, Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein, BIOCHEM, 38(11), 1999, pp. 3258-3267
Conversion of a catalytic into a structural disulfide bond by circular permutation
Authors: Hennecke, J Glockshuber, R
Citation: J. Hennecke et R. Glockshuber, Conversion of a catalytic into a structural disulfide bond by circular permutation, BIOCHEM, 37(50), 1998, pp. 17590-17597
Folding and three-dimensional NMR structure of the recombinant cellular prion protein from the mouse
Authors: Glockshuber, R Hornemann, S Riek, R Billeter, M Wider, G Liemann, S Zahn, R Wuthrich, K
Citation: R. Glockshuber et al., Folding and three-dimensional NMR structure of the recombinant cellular prion protein from the mouse, PRIONS: MOLECULAR AND CELLULAR BIOLOGY, 1997, pp. 1-25
Risultati: 1-21 |