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
I02-Macromolecular Crystallography	Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase Wyatt W. Yue , Victoria Hozjan , Christoph Leonarz , Wei Ge , Christopher D. O. Cooper , Kathryn L. Kavanagh , Udo Oppermann , Michael Mcdonough , Christoph Loenarz , Christopher J. Schofield Febs Letters DOI: 10.1016/j.febslet.2009.12.055 PMID: 20067792 Diamond Proposal Number(s): [442] Show Abstract ▼ Abstract: Crystallographic analysis of the catalytic domain of PHD finger protein 8 (PHF8), an N(epsilon)-methyl lysine histone demethylase associated with mental retardation and cleft lip/palate, reveals a double-stranded beta-helix fold with conserved Fe(II) and cosubstrate binding sites typical of the 2-oxoglutarate dependent oxygenases. The PHF8 active site is highly conserved with those of the FBXL10/11demethylases, which are also selective for the di-/mono-methylated lysine states, but differs from that of the JMJD2 demethylases which are selective for tri-/di-methylated states. The results rationalize the lack of activity for the clinically observed F279S PHF8 variant and they will help to identify inhibitors selective for specific N(epsilon)-methyl lysine demethylase subfamilies.	Feb 2010

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