User profiles for David Barford

David Barford

MRC Laboratory of Molecular Biology
Verified email at mrc-lmb.cam.ac.uk
Cited by 34686

[HTML][HTML] Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF

…, CM Jones, CJ Marshall, CJ Springer, D Barford… - Cell, 2004 - cell.com
Over 30 mutations of the B-RAF gene associated with human cancers have been identified,
the majority of which are located within the kinase domain. Here we show that of 22 B-RAF …

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

…, MP Myers, TC Meng, JA Hinks, NK Tonks, D Barford - Nature, 2003 - nature.com
The second messenger hydrogen peroxide is required for optimal activation of numerous
signal transduction pathways, particularly those mediated by protein tyrosine kinases 1 , 2 , 3 , …

[HTML][HTML] The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR‐mediated protein–protein interactions

AK Das, PTW Cohen, D Barford - The EMBO journal, 1998 - embopress.org
The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence identified in a
wide variety of proteins, present in tandem arrays of 3–16 motifs, which form scaffolds to …

Crystal structure of human protein tyrosine phosphatase 1B

D Barford, AJ Flint, NK Tonks - Science, 1994 - science.org
Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic
signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues …

The structure and mechanism of protein phosphatases: insights into catalysis and regulation

D Barford, AK Das, MP Egloff - Annual review of biophysics and …, 1998 - annualreviews.org
▪ Abstract Eukaryotic protein phosphatases are structurally and functionally diverse enzymes
that are represented by three distinct gene families. Two of these, the PPP and PPM families…

Development of “substrate-trapping” mutants to identify physiological substrates of protein tyrosine phosphatases

AJ Flint, T Tiganis, D Barford… - Proceedings of the …, 1997 - National Acad Sciences
The identification of substrates of protein tyrosine phosphatases (PTPs) is an essential step
toward a complete understanding of the physiological function of members of this enzyme …

A Family with Severe Insulin Resistance and Diabetes Due to a Mutation in AKT2

…, RM Williams, CL Acerini, DB Dunger, D Barford… - Science, 2004 - science.org
Inherited defects in signaling pathways downstream of the insulin receptor have long been
suggested to contribute to human type 2 diabetes mellitus. Here we describe a mutation in …

Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains

…, P Odenwaelder, KD Wilkinson, D Barford - EMBO …, 2009 - embopress.org
At least eight types of ubiquitin chain exist, and individual linkages affect distinct cellular
processes. The only distinguishing feature of differently linked ubiquitin chains is their structure, …

[HTML][HTML] Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1

…, G Moorhead, PTW Cohen, P Cohen, D Barford - The EMBO …, 1997 - embopress.org
The diverse forms of protein phosphatase 1 in vivo result from the association of its catalytic
subunit (PP1c) with different regulatory subunits, one of which is the G‐subunit (GM) that …

Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

Z Jia, D Barford, AJ Flint, NK Tonks - Science, 1995 - science.org
The crystal structures of a cysteine-215→serine mutant of protein tyrosine phosphatase 1B
complexed with high-affinity peptide substrates corresponding to an autophosphorylation site …