L L Randall
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Explore the profile of L L Randall including associated specialties, affiliations and a list of published articles.
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70
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1803
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Recent Articles
1.
Randall L, Hardy S
Cell Mol Life Sci
. 2002 Dec;
59(10):1617-23.
PMID: 12475171
SecB is only one of a plethora of cytosolic chaperones in E. coli whose common property is that they bind nonnative proteins. It plays a crucial role during protein export...
2.
Randall L, Krogh C, Welty T, Willinger M, Iyasu S
Am Indian Alsk Native Ment Health Res
. 2001 Aug;
10(1):1-20.
PMID: 11484150
Of all Indian Health Service areas, the Aberdeen Area has consistently had the highest infant mortality rate. Among some tribes in this area the rate has exceeded 30/ 1000 live...
3.
Topping T, Woodbury R, Diamond D, Hardy S, Randall L
J Biol Chem
. 2000 Dec;
276(10):7437-41.
PMID: 11110800
We have shown here that the cytosolic bacterial chaperone SecB is a structural dimer of dimers that undergoes a dynamic equilibrium between dimer and tetramer in the native state. We...
4.
5.
Woodbury R, Topping T, Diamond D, Suciu D, Kumamoto C, Hardy S, et al.
J Biol Chem
. 2000 May;
275(31):24191-8.
PMID: 10807917
During localization to the periplasmic space or to the outer membrane of Escherichia coli some proteins are dependent on binding to the cytosolic chaperone SecB, which in turn is targeted...
6.
Muren E, Suciu D, Topping T, Kumamoto C, Randall L
J Biol Chem
. 1999 Jun;
274(27):19397-402.
PMID: 10383453
Variant forms of SecB with substitutions of aminoacyl residues in the region from 74 to 80 were analyzed with respect to their ability to bind a physiological ligand, precursor galactose-binding...
7.
Randall L, Hardy S, Topping T, Smith V, Bruce J, Smith R
Protein Sci
. 1998 Nov;
7(11):2384-90.
PMID: 9828004
The chaperone protein SecB is dedicated to the facilitation of export of proteins from the cytoplasm to the periplasm and outer membrane of Escherichia coli. It functions to bind and...
8.
Randall L, Topping T, Suciu D, Hardy S
Protein Sci
. 1998 May;
7(5):1195-200.
PMID: 9605324
SecB is a chaperone in Escherichia coli dedicated to export of proteins from the cytoplasm to the periplasm and outer membrane. It functions to bind and deliver precursors of exported...
9.
Bruce J, Smith V, Liu C, Randall L, Smith R
Protein Sci
. 1998 May;
7(5):1180-5.
PMID: 9605322
Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) was applied for the study of noncovalent chaperone SecB-ligand complexes produced in solution and examined in the gas phase with the aid...
10.
Randall L, Topping T, Smith V, Diamond D, Hardy S
Methods Enzymol
. 1998 Apr;
290:444-59.
PMID: 9534181
No abstract available.