Stanley Dunn
Stanley Dunn
Distinguished University Professor, Department of Biochemistry, University of Western Ontario
Verified email at - Homepage
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Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies
SD Dunn
Analytical biochemistry 157 (1), 144-153, 1986
Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction
SD Dunn, LM Wahl, GB Gloor
Bioinformatics 24 (3), 333-340, 2008
Reconstitution of a functional coupling factor from the isolated subunits of Escherichia coli F1 ATPase
SD Dunn
Using information theory to search for co-evolving residues in proteins
LC Martin, GB Gloor, SD Dunn, LM Wahl
Bioinformatics 21 (22), 4116-4124, 2005
Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions
GB Gloor, LC Martin, LM Wahl, SD Dunn
Biochemistry 44 (19), 7156-7165, 2005
Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase.
S Wilkens, SD Dunn, J Chandler, FW Dahlquist, RA Capaldi
Nature Structural Biology 4 (3), 198-201, 1997
Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function
DA Christie, CD Lemke, IM Elias, LA Chau, MG Kirchhof, B Li, EH Ball, ...
Molecular and cellular biology 31 (18), 3845-3856, 2011
The polar domain of the b subunit of Escherichia coli F1F0-ATPase forms an elongated dimer that interacts with the F1 sector.
SD Dunn
Journal of Biological Chemistry 267 (11), 7630-7636, 1992
Properties and functions of the subunits of the Escherichia coli coupling factor ATPase
SD Dunn, LA Heppel
Archives of Biochemistry and Biophysics 210 (2), 421-436, 1981
The NH2-terminal portion of the alpha subunit of Escherichia coli F1 ATPase is required for binding the delta subunit.
SD Dunn, LA Heppel, CS Fullmer
The Journal of Biological Chemistry 255 (14), 6891-6896, 1980
The isolated gamma subunit of Escherichia coli F1 ATPase binds the epsilon subunit.
SD Dunn
Journal of Biological Chemistry 257 (13), 7354-7359, 1982
36° step size of proton‐driven c‐ring rotation in FoF1‐ATP synthase
MG Düser, N Zarrabi, DJ Cipriano, S Ernst, GD Glick, SD Dunn, M Börsch
The EMBO journal 28 (18), 2689-2696, 2009
The second stalk of Escherichia coli ATP synthase
SD Dunn, DT McLachlin, M Revington
Biochimica et Biophysica Acta (BBA)-Bioenergetics 1458 (2-3), 356-363, 2000
The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions
DT McLachlin, JA Bestard, SD Dunn
Journal of Biological Chemistry 273 (24), 15162-15168, 1998
Domain compliance and elastic power transmission in rotary FOF1-ATPase
H Sielaff, H Rennekamp, A Wächter, H Xie, F Hilbers, K Feldbauer, ...
Proceedings of the National Academy of Sciences 105 (46), 17760-17765, 2008
The “Second Stalk” of Escherichia coli ATP Synthase:  Structure of the Isolated Dimerization Domain,
PA Del Rizzo, Y Bi, SD Dunn, BH Shilton
Biochemistry 41 (21), 6875-6884, 2002
Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS
KA Vassall, HR Stubbs, HA Primmer, MS Tong, SM Sullivan, R Sobering, ...
Proceedings of the National Academy of Sciences 108 (6), 2210-2215, 2011
Determination of the 1-ethyl-3-[(3-dimethylamino) propyl]-carbodiimide-induced cross-link between the beta and epsilon subunits of Escherichia coli F1-ATPase.
HG Dallmann, TG Flynn, SD Dunn
Journal of Biological Chemistry 267 (26), 18953-18960, 1992
Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk
A Wächter, Y Bi, SD Dunn, BD Cain, H Sielaff, F Wintermann, ...
Proceedings of the National Academy of Sciences 108 (10), 3924-3929, 2011
Characterization of a b2δ Complex fromEscherichia coli ATP Synthase
SD Dunn, J Chandler
Journal of Biological Chemistry 273 (15), 8646-8651, 1998
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