2026 David Barford: Biology and Biochemistry Researcher – H-Index, Publications & Awards

Discipline name	D-Index	World Ranking	Current World Ranking	National Ranking	Current National Ranking	Publications	Citations
Biology and Biochemistry	92	2189	1989	144	131	270	35844

Research.com Recognitions

2006 - Fellow of the Royal Society, United Kingdom
Fellow of The Academy of Medical Sciences, United Kingdom
Member of the European Molecular Biology Organization (EMBO)
Fellow of The Academy of Medical Sciences, United Kingdom
Member of the European Molecular Biology Organization (EMBO)
Fellow of The Academy of Medical Sciences, United Kingdom
Member of the European Molecular Biology Organization (EMBO)

Overview

David Barford is affiliated with the MRC Laboratory of Molecular Biology in the United Kingdom. Their research expertise lies primarily within the fields of Biochemistry, Genetics, and Molecular Biology, with a particular focus on Molecular Biology and Cell Biology.

The scientist has contributed extensively to topics including:

Microtubule and mitosis dynamics
Photosynthetic Processes and Mechanisms
Genomics and Chromatin Dynamics
Ubiquitin and proteasome pathways
Chromosomal and Genetic Variations
Enzyme Structure and Function
Cellular transport and secretion

Their significant publications feature papers such as:

Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP, 2021, Proceedings of the National Academy of Sciences
Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome, 2022, Science
Structural basis of human separase regulation by securin and CDK1-cyclin B1, 2021, Nature
Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state, 2020, Nature Communications
Cryo-EM structure of the complete inner kinetochore of the budding yeast point centromere, 2023, Science Advances

The venues where this researcher frequently publishes include:

bioRxiv (Cold Spring Harbor Laboratory)
Nature Communications
eLife
Science
Nature Structural & Molecular Biology

Frequent collaborators in their work are:

Ziguo Zhang
Jing Yang
Stanislau Yatskevich
Stephen H. McLaughlin
Tom Dendooven

David Barford has received several recognitions, including:

Fellow of the Royal Society, United Kingdom, awarded in 2006
Member of the European Molecular Biology Organization (EMBO)
Fellow of The Academy of Medical Sciences, United Kingdom

Best Publications

Mechanism of Activation of the Raf-Erk Signaling Pathway by Oncogenic Mutations of B-Raf

Paul T.C Wan;Mathew J Garnett;S.Mark Roe;Sharlene Lee

3238
Citations
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Annette Salmeen;Jannik N. Andersen;Michael P. Myers;Tzu-Ching Meng

1139
Citations
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

Amit K. Das;Patricia T.W. Cohen;David Barford

1091
Citations
Development of “substrate-trapping” mutants to identify physiological substrates of protein tyrosine phosphatases

Andrew J. Flint;Tony Tiganis;David Barford;Nicholas K. Tonks

1006
Citations
Crystal structure of human protein tyrosine phosphatase 1B.

David Barford;Andrew J. Flint;Nicholas K. Tonks

1000
Citations
THE STRUCTURE AND MECHANISM OF PROTEIN PHOSPHATASES: Insights into Catalysis and Regulation

David Barford;and Amit K. Das;Marie-Pierre Egloff

963
Citations
Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B.

Zongchao Jia;David Barford;Andrew J. Flint;Nicholas K. Tonks

786
Citations
Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1

Marie Pierre Egloff;Deborah F. Johnson;Greg Moorhead;Patricia T.W. Cohen

765
Citations
Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains

David Komander;David Komander;Francisca Reyes‐Turcu;Julien D F Licchesi;Peter Odenwaelder

681
Citations
A family with severe insulin resistance and diabetes due to a mutation in AKT2.

Stella George;Justin J Rochford;Christian Wolfrum;Sarah L Gray

680
Citations
Structural insights into mRNA recognition from a PIWI domain-siRNA guide complex.

James S. Parker;S. Mark Roe;David Barford

673
Citations
TYK2 and JAK2 Are Substrates of Protein-tyrosine Phosphatase 1B

Michael P. Myers;Jannik N. Andersen;Alan Cheng;Michel L. Tremblay

636
Citations
Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP.

Jing Yang;Peter Cron;Valerie M. Good;Vivienne Thompson

628
Citations
The Crystal Structure of Human Eukaryotic Release Factor eRF1—Mechanism of Stop Codon Recognition and Peptidyl-tRNA Hydrolysis

Haiwei Song;Haiwei Song;Pierre M. Mugnier;Amit K. Das;Helen M. Webb

592
Citations
The Structure of the Protein Phosphatase 2A PR65/A Subunit Reveals the Conformation of Its 15 Tandemly Repeated HEAT Motifs

Matthew R. Groves;Neil Hanlon;Patric Turowski;Brian A. Hemmings

586
Citations
Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate

Marie-Pierre Egloff;Patricia T.W. Cohen;Patricia T.W. Cohen;Patricia T.W. Cohen;Peter Reinemer;Peter Reinemer;Peter Reinemer;David Barford;David Barford;David Barford

586
Citations
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.

A. K. Das;N. R. Helps;P. T. W. Cohen;D. Barford

567
Citations
Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation

Jing Yang;Peter Cron;Vivienne Thompson;Valerie M. Good

557
Citations
Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B.

Annette Salmeen;Jannik N Andersen;Michael P Myers;Nicholas K Tonks

552
Citations
Molecular mechanisms of theprotein serine/threonine phosphatases

David Barford

544
Citations