Search

Your search keyword '"Logan, Karen M."' showing total 18 results
Start Over Author "Logan, Karen M."
18 results on '"Logan, Karen M."'

4. Improved glycaemia during the Covid-19 pandemic lockdown is sustained post-lockdown and during the “Eat Out to Help Out” Government Scheme, in adults with Type 1 diabetes in the United Kingdom

Author

Avari, Parizad, primary, Unsworth, Rebecca, additional, Rilstone, Siân, additional, Uduku, Chukwuma, additional, Logan, Karen M., additional, Hill, Neil E., additional, Godsland, Ian F., additional, Reddy, Monika, additional, and Oliver, Nick, additional

Published
2021
Full Text
View/download PDF

5. ATP-mediated changes in cross-subunit interactions in the RecA protein

Author

Logan, Karen M., Forget, Anthony L., Verderese, John Paul, and Knight, Kendall L.

Subjects
Proteins -- Conformation, Conformational analysis -- Research, Nucleoproteins -- Physiological aspects, Structure-activity relationships (Biochemistry) -- Analysis, Biological sciences, Chemistry
Abstract

The mutant RecA proteins with pairwise Cys substitutions exhibit changes in the efficiency of cross-subunit disulfide bond formation in the presence of ATP or ATP/DNA. Data indicate that such cross-subunit interactions are different in free RecA protein and RecA/ATP/DNA complex.

Published
2001

7. Intersubunit proximity of residues in the RecA protein as shown by engineered disulfide cross-links

Author

Skiba, Mark C., Logan, Karen M., and Knight, Kendall L.

Subjects
Adenosine triphosphate -- Research, DNA -- Research, Proteins -- Structure, Biological sciences, Chemistry
Abstract

A series of Cys substitutions within the interacting surface have been introduced together with the F217C mutation. Disulfide formation has also been tested in conditions that include both the presence or absence of adenosine triphosphate (ATP) and ssDNA. The results indicate a location for F217 in the crystal structure that is in general agreement with its observed position in the catalytically active RecA-ATP-DNA complex.

Published
1999

9. Development of Early Adiposity in Infants of Mothers With Gestational Diabetes Mellitus

Author

Logan, Karen M., primary, Emsley, Robby J., additional, Jeffries, Suzan, additional, Andrzejewska, Izabela, additional, Hyde, Matthew J., additional, Gale, Chris, additional, Chappell, Karyn, additional, Mandalia, Sundhiya, additional, Santhakumaran, Shalini, additional, Parkinson, James R.C., additional, Mills, Luke, additional, and Modi, Neena, additional

Published
2016
Full Text
View/download PDF

17. Mutations in the N-terminal region of RecA that disrupt the stability of free protein oligomers but not RecA-DNA complexes11Edited by M. F. Moody

Author

Eldin, Sherif, Forget, Anthony L, Lindenmuth, Danielle M, Logan, Karen M, and Knight, Kendall L

Abstract

We have introduced targeted mutations in two areas that make up part of the RecA subunit interface. In the RecA crystal structure, cross-subunit interactions are observed between the Lys6 and Asp139 side-chains, and between the Arg28 and Asn113 side-chains. Unexpectedly, we find that mutations at Lys6 and Arg28 impose severe defects on the oligomeric stability of free RecA protein, whereas mutations at Asn113 or Asp139 do not. However, Lys6 and Arg28 mutant proteins showed an apparent normal formation of RecA-DNA complexes. These results suggest that cross-subunit contacts in this region of the protein are different for free RecA protein filaments versusRecA-DNA nucleoprotein filaments. Mutant proteins with substitutions at either Lys6 or Arg28 show partial inhibition of DNA strand exchange activity, yet the mechanistic reasons for this inhibition appear to be distinct. Although Lys6 and Arg28 appear to be more important to the stability of free RecA protein, as opposed to the stability of the catalytically active nucleoprotein filament, our results support the idea that the cross-subunit interactions made by each residue play an important role in optimizing the catalytic organization of the active RecA oligomer.

Published
2000
Full Text
View/download PDF

18. Mutant RecA proteins which form hexamer-sized oligomers11Edited by M. F. Moody

Author

Logan, Karen M, Skiba, Mark C, Eldin, Sherif, and Knight, Kendall L

Abstract

We have analyzed the oligomeric properties of a number of mutant RecA proteins containing single amino acid substitutions within one region of the subunit interface. In contrast to wild-type RecA, which forms a heterogeneous population of different-sized oligomers, we find that many of these mutant proteins exist in a more homogeneous oligomeric form, which approximates to the size of a RecA hexamer. Some of these mutants have a significant level of activity in vivofor recombinational DNA repair and thus represent the first mutant RecA proteins identified which retain activity yet can exist in a discrete oligomeric state as free protein.

Published
1997
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results