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Biology and Biochemistry

D-Index
70
Citations
15641
World Ranking
7094
National Ranking
543

Overview

Raymond J. Owens is affiliated with the University of Oxford in the United Kingdom and works primarily in the fields of Medicine and Biochemistry, Genetics and Molecular Biology. Their research spans several specific subfields including Infectious Diseases, Molecular Biology, Radiology, Nuclear Medicine and Imaging, Neurology, and Ecology.

The main topics of Raymond J. Owens's work focus on SARS-CoV-2 and COVID-19 research, monoclonal and polyclonal antibodies research, COVID-19 clinical research studies, parasites and host interactions, glycosylation and glycoproteins research, bacteriophages and microbial interactions, and viral gastroenteritis research and epidemiology.

Owens has published extensively, including papers addressing mechanisms of viral neutralization and vaccine development related to SARS-CoV-2. Recent notable publications include:

  • Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2, 2020, Nature Structural & Molecular Biology
  • Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike, 2020, Cell Host & Microbe
  • Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient, 2020, Nature Structural & Molecular Biology
  • A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses, 2021, Nature Communications
  • A potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19, 2021, Nature Communications

Raymond J. Owens collaborates frequently with several researchers in related fields, including Jiandong Huo, James H. Naismith, David I. Stuart, Helen M. E. Duyvesteyn, and Tomas Malinauskas.

Owens's research has appeared in multiple publication venues, with several works published in bioRxiv (Cold Spring Harbor Laboratory), Nature Structural & Molecular Biology, Nature Communications, Science Advances, and the Journal of Biological Chemistry.

Best Publications

  • Protein production and purification.

    S Gräslund

  • Oncostatin M drives intestinal inflammation and predicts response to tumor necrosis factor-neutralizing therapy in patients with inflammatory bowel disease

    N R West;A N Hegazy;Owens Bmj.;S J Bullers

  • A versatile ligation-independent cloning method suitable for high-throughput expression screening applications

    Nick S. Berrow;David Alderton;Sarah Sainsbury;Joanne E. Nettleship

  • Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2.

    J Huo;J Huo;A Le Bas;A Le Bas;R R Ruza;Duyvesteyn Hme.

  • Structure and functionality in flavivirus NS-proteins: Perspectives for drug design

    Michela Bollati;Karin Alvarez;René Assenberg;Cécile Baronti

  • Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike.

    Jiandong Huo;Jiandong Huo;Yuguang Zhao;Jingshan Ren;Daming Zhou

  • Lysine methylation as a routine rescue strategy for protein crystallization.

    Thomas S. Walter;Christoph Meier;Rene Assenberg;Kin Fai Au

  • Glycoprotein Structural Genomics: Solving the Glycosylation Problem

    V T Chang;M Crispin;M Crispin;A R Aricescu;D J Harvey

  • Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient.

    D Zhou;Duyvesteyn Hme.;Chen C-P.;Huang C-G.;Huang C-G.

  • A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization.

    T.S. Walter;J.M. Diprose;C.J. Mayo;C. Siebold

  • The Nsp9 Replicase Protein of Sars-Coronavirus, Structure and Functional Insights

    Geoff Sutton;Elizabeth Fry;Lester Carter;Sarah Sainsbury

  • A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses.

    T K Tan;P Rijal;P Rijal;R Rahikainen;A H Keeble

  • The crystal structure of IgE Fc reveals an asymmetrically bent conformation

    Tommy Wan;Rebecca L. Beavil;Stella M. Fabiane;Andrew J. Beavil

  • Recombinant protein expression and solubility screening in Escherichia coli: a comparative study

    Nick S. Berrow;K. Büssow;B. Coutard;J. Diprose

  • Affimer proteins are versatile and renewable affinity reagents

    Christian Tiede;Robert Bedford;Sophie J Heseltine;Gina Smith

  • Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications

    Christian Tiede;Anna A. S. Tang;Sarah E. Deacon;Upasana Mandal

  • Structural and Functional Insights of RANKL–RANK Interaction and Signaling

    Changzhen Liu;Thomas S. Walter;Peng Huang;Shiqian Zhang

  • Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family.

    M. R. Crompton;R. J. Owens;N. F. Totty;S. E. Moss

  • Crystal Structure of a Novel Conformational State of the Flavivirus Ns3 Protein: Implications for Polyprotein Processing and Viral Replication.

    René Assenberg;Eloise Mastrangelo;Thomas S. Walter;Anil Verma

  • A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses

    Tiong Kit Tan;Pramila Rijal;Pramila Rijal;Rolle Rahikainen;Anthony H. Keeble

Frequent Co-Authors

David I. Stuart
David I. Stuart University of Oxford
Jingshan Ren
Jingshan Ren University of Oxford
Jonathan M. Grimes
Jonathan M. Grimes University of Oxford
Alain Townsend
Alain Townsend University of Oxford
Miles W. Carroll
Miles W. Carroll University of Oxford
Karl Harlos
Karl Harlos University of Oxford
James H. Naismith
James H. Naismith Rosalind Franklin Institute
David K. Stammers
David K. Stammers University of Oxford
Juthathip Mongkolsapaya
Juthathip Mongkolsapaya University of Oxford

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