User profiles for David Barford
David BarfordMRC 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 …
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 , …
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
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 …
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 …
signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues …
The structure and mechanism of protein phosphatases: insights into catalysis and regulation
▪ 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…
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
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 …
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
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 …
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, …
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
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 …
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
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 …
complexed with high-affinity peptide substrates corresponding to an autophosphorylation site …