Nigel J. Darby

Biochemistry, Genetics and Molecular Biology · Life Sciences

30h-index3.2kcitations52works0.02yr avg
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Research Topics

Endoplasmic Reticulum Stress and Disease(19), Protein Structure and Dynamics(11), Cellular transport and secretion(11), Biochemical and Structural Characterization(10), Redox biology and oxidative stress(7)

Publications52 total

Errata
Neuroendocrinology·2008Open Access
Disulfide Bonds in Protein Folding and Stability
Humana Press eBooks·2003· 89 cited
Sequential 1H assignments for BPTI-R52 (= BPTI with Met to Arg mutation at position 52)
Journal of Back and Musculoskeletal Rehabilitation·2000Open Access
Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the a′ domain of protein disulfide isomerase
Journal of Biomolecular NMR·1999· 23 cited
The structure in solution of the b domain of protein disulfide isomerase*
Journal of Biomolecular NMR·1999· 69 cited
Identifying and characterizing a second structural domain of protein disulfide isomerase
FEBS Letters·1999· 27 cited
Functional properties of the two redox-active sites in yeast protein disulphide isomerase in Vitro and in Vivo 1 1Edited by G. Von Heijne
Journal of Molecular Biology·1999· 29 cited
PROTEIN DISULFIDE ISOMERASE
1999
HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES
1998
The functional properties of DsbG, a thiol‐disulfide oxidoreductase from the periplasm of <i>Escherichia coli</i>
FEBS Letters·1998· 35 citedOpen Access
Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57
Journal of Biological Chemistry·1998· 334 citedOpen Access
The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
Journal of Molecular Biology·1998· 167 cited
Contributions of Substrate Binding to the Catalytic Activity of DsbC
Biochemistry·1998· 56 cited
The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
Current Biology·1997· 216 citedOpen Access
Probing protein folding and stability using disulfide bonds
Molecular Biotechnology·1997· 29 cited
The roles of partly folded intermediates in protein folding
The FASEB Journal·1996· 134 cited
Identifying and Characterizing a Structural Domain of Protein Disulfide Isomerase
Biochemistry·1996· 88 cited
Structure Determination of the N-Terminal Thioredoxin-like Domain of Protein Disulfide Isomerase Using Multidimensional Heteronuclear <sup>13</sup>C/<sup>15</sup>N NMR Spectroscopy
Biochemistry·1996· 192 cited
Electrostatic Interactions in the Active Site of the N-Terminal Thioredoxin-like Domain of Protein Disulfide Isomerase
Biochemistry·1996· 120 cited
Nuclear magnetic resonance characterization of the N‐terminal thioredoxin‐like domain of protein disulfide isomerase
Protein Science·1995· 46 citedOpen Access
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Frequent Co-authors

Thomas E. Creighton(28), Johan Kemmink(10), Carlo P. M. van Mierlo(8), David Neuhaus(6), Derek G. Smyth(6), A. Lodola(6), F. R. Burnet(6), Klaas Dijkstra(5), Michaël Nilges(3), Elke Penka(3), Ruud M. Scheek(3), Monique van Straaten(3), Kamala Maruthainar(3), André Zapun(2), Renaud Vincentelli(2), D.G. Smyth(2), Robert B. Freedman(2), Satish Raina(2), K. Maruthainar(2), Lloyd D. Fricker(2)