World's Best Scientists 2026 revealed!

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Biology and Biochemistry

D-Index
51
Citations
11307
World Ranking
17047
National Ranking
482

Overview

Michael C. Lawrence is affiliated with the Walter and Eliza Hall Institute of Medical Research in Australia. Their research has focused primarily on biochemistry, genetics, and molecular biology, with significant contributions also in the field of medicine.

The scientist's main subfields of study include molecular biology, endocrinology, diabetes and metabolism, cancer research, genetics, and oncology. Their work covers a variety of topics, such as metabolism, diabetes and cancer, protein structure and dynamics, growth hormone and insulin-like growth factors, receptor mechanisms and signaling, nicotinic acetylcholine receptors study, protein kinase regulation and GTPase signaling, as well as cancer, hypoxia, and metabolism.

Michael C. Lawrence has published numerous papers, some of the recent ones include:

  • Understanding insulin and its receptor from their three-dimensional structures (2021, Molecular Metabolism)
  • A structurally minimized yet fully active insulin based on cone-snail venom insulin principles (2020, Nature Structural & Molecular Biology)
  • How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor (2020, Structure)
  • How insulin-like growth factor I binds to a hybrid insulin receptor type 1 insulin-like growth factor receptor (2022, Structure)
  • Symmetric and asymmetric receptor conformation continuum induced by a new insulin (2022, Nature Chemical Biology)

The frequent co-authors associated with Michael C. Lawrence include John G. Menting, Carlie Delaine, Briony E. Forbes, Xiaochun Xiong, and Rahul Agrawal.

Their work has been frequently published in venues such as Nature Structural & Molecular Biology, Structure, Nature Communications, Molecular Metabolism, and Nature Chemical Biology.

Best Publications

  • Shape Complementarity at Protein/Protein Interfaces

    Michael C. Lawrence;Peter M. Colman

  • The structural biology of type I viral membrane fusion.

    Peter M. Colman;Michael C. Lawrence

  • How insulin engages its primary binding site on the insulin receptor

    John G. Menting;Jonathan Whittaker;Mai B. Margetts;Linda J. Whittaker

  • A Molecular Mechanism for Bacterial Susceptibility to Zinc.

    Christopher A. McDevitt;Abiodun D. Ogunniyi;Eugene Valkov;Michael C. Lawrence

  • Structure of the insulin receptor ectodomain reveals a folded-over conformation

    Neil M. McKern;Michael C. Lawrence;Victor A. Streltsov;Mei-Zhen Lou

  • Insulin Receptor Isoforms in Physiology and Disease: An Updated View.

    Antonino Belfiore;Roberta Malaguarnera;Veronica Vella;Michael C Lawrence;Michael C Lawrence

  • Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase.

    P M Colman;P A Hoyne;M C Lawrence

  • Structure of Phaseolin at 2·2 Å Resolution: Implications for a Common Vicilin/Legumin Structure and the Genetic Engineering of Seed Storage Proteins

    M.C. Lawrence;T. Izard;M. Beuchat;R.J. Blagrove

  • A designed ankyrin repeat protein evolved to picomolar affinity to Her2

    Christian Zahnd;Emanuel Wyler;Jochen M. Schwenk;Daniel Steiner

  • The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion.

    Lin Chen;Jeffrey J Gorman;Jenny McKimm-Breschkin;Lynne J Lawrence

  • The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein

    Michael C Lawrence;Patricia A Pilling;V Chandana Epa;Anne M Berry

  • Structure of the Haemagglutinin-neuraminidase from Human Parainfluenza Virus Type III

    Michael C. Lawrence;Natalie A. Borg;Victor A. Streltsov;Patricia A. Pilling

  • Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex.

    Alexander A. Kortt;Robyn L. Malby;J. Bruce Caldwell;L. Clem Gruen

  • A method for monitoring the collapse of plastic sections as a function of electron dose.

    P.K. Luther;M.C. Lawrence;R.A. Crowther

  • Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor.

    Colin W. Ward;Michael C. Lawrence

  • The insulin and EGF receptor structures : new insights into ligand-induced receptor activation

    Colin W. Ward;Michael C. Lawrence;Victor A. Streltsov;Timothy E. Adams

  • The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution.

    M.C. Lawrence;E. Suzuki;J.N. Varghese;P.C. Davis

  • Insulin receptor structure and its implications for the IGF-1 receptor.

    Michael C Lawrence;Neil M McKern;Colin W Ward

  • CLIX: a search algorithm for finding novel ligands capable of binding proteins of known three-dimensional structure.

    Michael C. Lawrence;Paul C. Davis

  • Protective hinge in insulin opens to enable its receptor engagement.

    John G. Menting;Yanwu Yang;Shu Jin Chan;Nelson B. Phillips

Frequent Co-Authors

Brian J. Smith
Brian J. Smith QIMR Berghofer Medical Research Institute
Colin W. Ward
Colin W. Ward Walter and Eliza Hall Institute of Medical Research
Peter M. Colman
Peter M. Colman Walter and Eliza Hall Institute of Medical Research
Michael A. Weiss
Michael A. Weiss Case Western Reserve University
Alan F. Cowman
Alan F. Cowman Walter and Eliza Hall Institute of Medical Research
Faramarz Ismail-Beigi
Faramarz Ismail-Beigi Case Western Reserve University
Raymond S. Norton
Raymond S. Norton Monash University
Shu Jin Chan
Shu Jin Chan Howard Hughes Medical Institute
James C. Paton
James C. Paton University of Adelaide
Peter J. Hudson
Peter J. Hudson Pennsylvania State University

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