Search Results

You searched for all publications:

with publication states 'Published (Approved)'

Search Again...

Author Name

Author Affiliation

Author ORCID

Title of Publication

DOI

Data DOI

Type of Publication (check all that apply) select all

Book Chapter

Conference Paper

Diamond Annual Review Highlight

Editors' Note

Journal Paper

Magazine Article

Poster

Report

Thesis

Title of Journal

Title of Conference

Peer Reviewed:

Yes No Either

Title of Magazine

Abstract

Keywords

Tags

Funding

Diamond Proposal Number

ISBN

BookChapter

Open Access:

Yes No Either

Published In or After Help

Published In or Before Help

Added In or After Help

Added In or Before Help

These results only include publications that have been reviewed and processed by Diamond Light Source. To also view papers that have not yet been processed click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

One item found (0 items not approved).1

Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS	A mechanism for cancer-associated inactivation of NQO1 due to P187S and its reactivation by the consensus mutation H80R Ines G. Munoz , Bertrand Morel , Encarnación Medina-Carmona , Angel L. Pey Febs Letters DOI: 10.1002/1873-3468.12772 Diamond Proposal Number(s): [12571] Show Abstract ▼ Abstract: The cancer-associated P187S polymorphism in the NAD(P)H:quinone oxidoreductase 1 (NQO1) abolishes enzyme activity by strongly reducing FAD binding affinity. A single mammalian consensus mutation (H80R) protects P187S from inactivation. To provide mechanistic insight into these effects, we report here a detailed structural and thermodynamic characterization of FAD binding to these NQO1 variants. Our results show that H80R causes a population shift in the conformational ensemble of apo-P187S, remodeling the structure and dynamics of the FAD binding site and reducing the energetic penalization arising from the equilibrium between apo- and holo-states. Our analyses illustrate how single amino acid changes can profoundly affect structural and mechanistic features of protein functional traits, with implications for our understanding of protein evolution and human disease.	Aug 2017

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User