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Biology and Biochemistry

D-Index
56
Citations
10456
World Ranking
14506
National Ranking
1147

Research.com Recognitions

  • 2011 - Fellow of the Royal Society of Edinburgh

Overview

Frank Sargent is affiliated with Newcastle University in the United Kingdom and has contributed extensively to research in the fields of biochemistry, genetics, molecular biology, and energy. Their work encompasses a range of subfields including molecular biology, renewable energy, sustainability and the environment, endocrinology, genetics, and ecology. The scientist's research spans diverse topics such as metalloenzymes and iron-sulfur proteins, bacterial genetics and biotechnology, glycosylation and glycoproteins research, Vibrio bacteria research studies, photosynthetic processes and mechanisms, microbial metabolism and enzyme function, and microbial metabolic engineering and bioproduction.

Their frequent coauthors include Tracy Palmer, Andrew Bell, Gavin H. Thomas, David N. Bolam, and Nathalie Juge.

Frank Sargent has published several papers recently, with detailed examples as follows:

  • A holin/peptidoglycan hydrolase-dependent protein secretion system, 2020, Molecular Microbiology
  • Formate hydrogenlyase, formic acid translocation and hydrogen production: dynamic membrane biology during fermentation, 2022, Biochimica et Biophysica Acta (BBA) - Bioenergetics
  • Harnessing Escherichia coli for Bio-Based Production of Formate under Pressurized H 2 and CO 2 Gases, 2021, Applied and Environmental Microbiology
  • Hydrogen production in the presence of oxygen by Escherichia coli K-12, 2022, Microbiology
  • A paean to the ineffable Marjory Stephenson, 2022, Microbiology

The main venues where this scientist's work has appeared include Microbiology, bioRxiv (Cold Spring Harbor Laboratory), Biochimica et Biophysica Acta (BBA) - Bioenergetics, Molecular Microbiology, and Applied and Environmental Microbiology.

Frank Sargent has been recognized with the award of Fellow of the Royal Society of Edinburgh in 2011.

Best Publications

  • The Tat protein export pathway

    Ben C. Berks;Frank Sargent;Tracy Palmer;Tracy Palmer

  • Overlapping functions of components of a bacterial Sec-independent protein export pathway.

    Frank Sargent;Frank Sargent;Erik G. Bogsch;Nicola R. Stanley;Nicola R. Stanley;Margaret Wexler;Margaret Wexler

  • AN ESSENTIAL COMPONENT OF A NOVEL BACTERIAL PROTEIN EXPORT SYSTEM WITH HOMOLOGUES IN PLASTIDS AND MITOCHONDRIA

    Erik G. Bogsch;Frank Sargent;Frank Sargent;Nicola R. Stanley;Nicola R. Stanley;Ben C. Berks

  • Sec-independent Protein Translocation in Escherichia coli: A DISTINCT AND PIVOTAL ROLE FOR THE TatB PROTEIN *

    Frank Sargent;Frank Sargent;Nicola R. Stanley;Nicola R. Stanley;Ben C. Berks;Tracy Palmer;Tracy Palmer

  • TatD Is a Cytoplasmic Protein with DNase Activity NO REQUIREMENT FOR TatD FAMILY PROTEINS IN Sec-INDEPENDENT PROTEIN EXPORT

    Margaret Wexler;Frank Sargent;Frank Sargent;Rachael L. Jack;Rachael L. Jack;Nicola R. Stanley;Nicola R. Stanley

  • The Tat protein translocation pathway and its role in microbial physiology.

    Ben C. Berks;Tracy Palmer;Frank Sargent

  • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway

    Ben C Berks;Tracy Palmer;Tracy Palmer;Frank Sargent

  • Export of complex cofactor-containing proteins by the bacterial Tat pathway.

    Tracy Palmer;Frank Sargent;Ben C. Berks

  • Bacterial formate hydrogenlyase complex

    Jennifer S. McDowall;Bonnie J. Murphy;Michael Haumann;Tracy Palmer

  • How Escherichia coli Is Equipped to Oxidize Hydrogen under Different Redox Conditions

    Michael J. Lukey;Alison Parkin;Maxie M. Roessler;Bonnie J. Murphy

  • Coordinating assembly and export of complex bacterial proteins

    Rachael L Jack;Rachael L Jack;Grant Buchanan;Alexandra Dubini;Kostas Hatzixanthis

  • Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains.

    Kevin Deplanche;Isabelle Caldelari;Iryna P. Mikheenko;Frank Sargent

  • Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure.

    Frank Sargent;Ulrich Gohlke;Erik de Leeuw;Nicola R. Stanley;Nicola R. Stanley

  • Constitutive Expression of Escherichia coli tat Genes Indicates an Important Role for the Twin-Arginine Translocase during Aerobic and Anaerobic Growth

    Rachael L. Jack;Rachael L. Jack;Frank Sargent;Frank Sargent;Ben C. Berks;Gary Sawers

  • A subset of bacterial inner membrane proteins integrated by the twin‐arginine translocase

    Kostas Hatzixanthis;Tracy Palmer;Frank Sargent

  • Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster.

    Michael J. Lukey;Maxie M. Roessler;Alison Parkin;Rhiannon M. Evans

  • Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases

    Rosa María Martinez-Espinosa;Elizabeth J. Dridge;Mari­a J. Bonete;Julea N. Butt

  • Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes

    Erik de Leeuw;Thierry Granjon;Ida Porcelli;Meriem Alami

  • The twin-arginine transport system: moving folded proteins across membranes.

    F. Sargent

  • The Tat Protein Export Pathway.

    Tracy Palmer;Frank Sargent;Ben C. Berks

Frequent Co-Authors

Tracy Palmer
Tracy Palmer Newcastle University
Ben C. Berks
Ben C. Berks University of Oxford
Fraser A. Armstrong
Fraser A. Armstrong University of Oxford
Lynne E. Macaskie
Lynne E. Macaskie University of Birmingham
David J. Richardson
David J. Richardson Microsoft (United States)
Colin Robinson
Colin Robinson University of Kent
Gary Sawers
Gary Sawers Martin Luther University Halle-Wittenberg
Geerten W. Vuister
Geerten W. Vuister University of Leicester
Susan M. Lea
Susan M. Lea University of Oxford
Simon E. V. Phillips
Simon E. V. Phillips University of Oxford

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