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Malcolm D. Walkinshaw

Malcolm D. Walkinshaw

D-Index & Metrics

Chemistry

D-Index
67
Citations
14130
World Ranking
7014
National Ranking
403

Biology and Biochemistry

D-Index
67
Citations
14028
World Ranking
8314
National Ranking
643

Research.com Recognitions

  • 2003 - Fellow of the Royal Society of Edinburgh

Overview

Malcolm D. Walkinshaw is affiliated with the University of Edinburgh in the United Kingdom. Their research primarily covers the fields of Medicine and Biochemistry, Genetics and Molecular Biology. Within these areas, their work often focuses on Molecular Biology, Epidemiology, Radiology, Nuclear Medicine and Imaging, Public Health, Environmental and Occupational Health, and Oncology.

The scientist's research topics include the study of Trypanosoma species and their implications, biochemical and molecular research, investigations into Leishmaniasis, signaling pathways in disease, protein structure and dynamics, drug transport and resistance mechanisms, and aspects of corneal surgery and disorders.

Frequent publication venues for their work include eLife, Biochemical Journal, Nature Communications, Chemical Science, and Biochemical and Biophysical Research Communications.

Notable recent papers authored or co-authored by Walkinshaw include:

  • Biochemical and transcript level differences between the three human phosphofructokinases show optimisation of each isoform for specific metabolic niches, 2020, Biochemical Journal
  • Fast acting allosteric phosphofructokinase inhibitors block trypanosome glycolysis and cure acute African trypanosomiasis in mice, 2021, Nature Communications
  • Dynamic design: manipulation of millisecond timescale motions on the energy landscape of cyclophilin A, 2020, Chemical Science
  • Pyruvate kinase from Plasmodium falciparum: Structural and kinetic insights into the allosteric mechanism, 2020, Biochemical and Biophysical Research Communications
  • Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase, 2020, Molecular and Biochemical Parasitology

Walkinshaw has collaborated frequently with several co-authors, including Paul A.M. Michels, Meng Yuan, Joar Esteban Pinto Torres, Wim Versées, and Guy Caljon.

In 2003, Walkinshaw was recognized as a Fellow of the Royal Society of Edinburgh.

Best Publications

  • Insights into antifolate resistance from malarial DHFR-TS structures.

    Jirundon Yuvaniyama;Penchit Chitnumsub;Sumalee Kamchonwongpaisan;Jarunee Vanichtanankul

  • Order-disorder transition for a bacterial polysaccharide in solution. A role for polysaccharide conformation in recognition between Xanthomonas pathogen and its plant host

    E.R. Morris;D.A. Rees;G. Young;M.D. Walkinshaw

  • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy

    Jörg Kallen;Claus Spitzfaden;Mauro G. M. Zurini;Gerhard Wider

  • MeCP2 Binding to DNA Depends upon Hydration at Methyl-CpG

    Kok Lian Ho;Iain W. McNae;Lars Schmiedeberg;Robert J. Klose

  • Conformations and interactions of pectins. II. Models for junction zones in pectinic acid and calcium pectate gels.

    M.D. Walkinshaw;Struther Arnott

  • Three-dimensional structure of the "long" neurotoxin from cobra venom.

    Malcolm D. Walkinshaw;Wolfram Saenger;Alfred Maelicke

  • Consensus Docking: Improving the Reliability of Docking in a Virtual Screening Context

    Douglas R. Houston;Malcolm D. Walkinshaw

  • X-ray structure of a decameric cyclophilin-cyclosporin crystal complex

    Gaston Pflügl;Jörg Kallen;Tilman Schirmer;Johan N. Jansonius

  • X-Ray Structure of a Monomeric Cyclophilin A-Cyclosporin a Crystal Complex at 2.1 A Resolution.

    Vincent Mikol;Jörg Kallen;Gaston Pflügl;Malcolm D. Walkinshaw

  • The ribosome binding sites recognized by E. coli ribosomes have regions with signal character in both the leader and protein coding segments

    Günther F.E. Scherer;Malcolm D. Walkinshaw;Struther Arnott;D.James Morré

  • Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA.

    Malcolm Walkinshaw;Paul Taylor;S S Sturrock;C Atanasiu

  • Crystal environments and geometries of leucine, isoleucine, valine and phenylalanine provide estimates of minimum nonbonded contact and preferred van der Waals interaction distances

    Robert O. Gould;Alexandra M. Gray;Paul Taylor;Malcolm D. Walkinshaw

  • Metals in protein structures: a review of their principal features

    Marjorie M. Harding;Matthew W. Nowicki;Malcolm D. Walkinshaw

  • 2-Anilino-4-(thiazol-5-yl)pyrimidine CDK Inhibitors: Synthesis, SAR Analysis, X-ray Crystallography, and Biological Activity

    Shudong Wang;Christopher Meades;Gavin Wood;Andrew Osnowski

  • M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation.

    Hugh P. Morgan;Francis J. O’Reilly;Martin A. Wear;J. Robert O’Neill

  • Conformations and interactions of pectins: I. X-ray diffraction analyses of sodium pectate in neutral and acidified forms

    M.D. Walkinshaw;Struther Arnott

  • Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 Å reveals novel features of cytochrome P450

    David G Leys;Christopher G. Mowat;Kirsty J McLean;Alison Richmond

  • Structural and mechanistic mapping of a unique fumarate reductase.

    Paul Taylor;Sara L. Pealing;Graeme A. Reid;Stephen K. Chapman

  • Two Structures of Cyclophilin 40: Folding and Fidelity in the TPR Domains

    Paul Taylor;Jacqueline Dornan;Amerigo Carrello;Amerigo Carrello;Rodney F Minchin

  • The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A

    Joerg Kallen;Malcolm D. Walkinshaw

Frequent Co-Authors

Paul A. M. Michels
Paul A. M. Michels University of Edinburgh
Stephen K Chapman
Stephen K Chapman University of Edinburgh
Anton Simeonov
Anton Simeonov National Institutes of Health
Peter M. Fischer
Peter M. Fischer University of Nottingham
Nicholas J. Turner
Nicholas J. Turner University of Manchester
Ted R. Hupp
Ted R. Hupp University of Edinburgh
Paul N. Barlow
Paul N. Barlow University of Edinburgh
Peter J. Sadler
Peter J. Sadler University of Warwick
David Leys
David Leys University of Manchester

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