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Biochimica Et Biophysica Acta
|
September 4, 1992
Conformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy
M D Bruch, D W Hoyt
The Journal of Biological Chemistry
|
August 5, 1991
A peptide corresponding to an export-defective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes
D W Hoyt, L M Gierasch
Biochemistry
|
October 22, 1991
Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function
D W Hoyt, L M Gierasch
The Journal of Biological Chemistry
|
November 15, 1991
Interaction of peptides corresponding to mitochondrial presequences with membranes
D W Hoyt, D M Cyr, L M Gierasch, et al.
JAMA
|
July 24, 1987
Drug testing in the workplace--are methods legally defensible? A survey of experts, arbitrators, and testing laboratories
D W Hoyt, R E Finnigan, T Nee, et al.
Biochimica Et Biophysica Acta
|
June 24, 1998
The use of sodium dodecyl sulfate to model the apolipoprotein environment. Evidence for peptide-SDS complexes using pulsed-field-gradient NMR spectroscopy
G W Buchko, A Rozek, D W Hoyt, et al.
Nature Structural Biology
|
September 27, 2001
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex
P S Brzovic, P Rajagopal, D W Hoyt, et al.
Biochemistry
|
December 27, 1994
Interaction of transforming growth factor alpha with the epidermal growth factor receptor: binding kinetics and differential mobility within the bound TGF-alpha
D W Hoyt, R N Harkins, M T Debanne, et al.
Journal of Biochemistry
|
December 17, 1997
Construction of transforming growth factor alpha (TGF-alpha) phage library and identification of high binders of epidermal growth factor receptor (EGFR) by phage display
X B Tang, P Dallaire, D W Hoyt, et al.
Journal of Molecular Biology
|
October 31, 2000
Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface
K Liu, H S Cho, D W Hoyt, et al.
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of 2
Search research articles
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Showing results (1-10 of 13) with videos related to
Sort By:
Page
of 2
Biochimica Et Biophysica Acta
|
September 4, 1992
Conformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy
M D Bruch, D W Hoyt
The Journal of Biological Chemistry
|
August 5, 1991
A peptide corresponding to an export-defective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes
D W Hoyt, L M Gierasch
Biochemistry
|
October 22, 1991
Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function
D W Hoyt, L M Gierasch
The Journal of Biological Chemistry
|
November 15, 1991
Interaction of peptides corresponding to mitochondrial presequences with membranes
D W Hoyt, D M Cyr, L M Gierasch, et al.
JAMA
|
July 24, 1987
Drug testing in the workplace--are methods legally defensible? A survey of experts, arbitrators, and testing laboratories
D W Hoyt, R E Finnigan, T Nee, et al.
Biochimica Et Biophysica Acta
|
June 24, 1998
The use of sodium dodecyl sulfate to model the apolipoprotein environment. Evidence for peptide-SDS complexes using pulsed-field-gradient NMR spectroscopy
G W Buchko, A Rozek, D W Hoyt, et al.
Nature Structural Biology
|
September 27, 2001
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex
P S Brzovic, P Rajagopal, D W Hoyt, et al.
Biochemistry
|
December 27, 1994
Interaction of transforming growth factor alpha with the epidermal growth factor receptor: binding kinetics and differential mobility within the bound TGF-alpha
D W Hoyt, R N Harkins, M T Debanne, et al.
Journal of Biochemistry
|
December 17, 1997
Construction of transforming growth factor alpha (TGF-alpha) phage library and identification of high binders of epidermal growth factor receptor (EGFR) by phage display
X B Tang, P Dallaire, D W Hoyt, et al.
Journal of Molecular Biology
|
October 31, 2000
Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface
K Liu, H S Cho, D W Hoyt, et al.
Page
of 2