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Lloyd W. Ruddock

Lloyd W. Ruddock

D-Index & Metrics

Biology and Biochemistry

D-Index
50
Citations
9848
World Ranking
17572
National Ranking
125

Overview

Lloyd W. Ruddock is affiliated with the University of Oulu in Finland. Their research contributions span key areas within biochemistry, genetics, and molecular biology, with a total of 61 publications in these fields. Medicine is another area of focus, accounting for 20 publications.

The scientist's work includes extensive investigation within molecular biology and cell biology, which are reflected in 26 and 16 publications respectively. Additional subfields include radiology, nuclear medicine and imaging, genetics, and ecology.

The research topics addressed cover:

  • Endoplasmic Reticulum Stress and Disease
  • Monoclonal and Polyclonal Antibodies Research
  • Viral Infectious Diseases and Gene Expression in Insects
  • Bacteriophages and microbial interactions
  • Protein purification and stability
  • Transgenic Plants and Applications
  • Autophagy in Disease and Therapy

Frequent publication venues include:

  • Journal of Biological Chemistry
  • Scientific Reports
  • Trends in biotechnology
  • International Journal of Molecular Sciences
  • Protein Expression and Purification

Notable recent publications by Lloyd W. Ruddock are:

  • "Microbial protein cell factories fight back?" (2021) in Trends in biotechnology
  • "A point mutation decouples the lipid transfer activities of microsomal triglyceride transfer protein" (2020) in PLoS Genetics
  • "Mutation in protein disulfide isomerase A3 causes neurodevelopmental defects by disturbing endoplasmic reticulum proteostasis" (2021) in The EMBO Journal
  • "So you want to express your protein in Escherichia coli?" (2021) in Essays in Biochemistry
  • "Production of Extracellular Matrix Proteins in the Cytoplasm of E. coli: Making Giants in Tiny Factories" (2020) in International Journal of Molecular Sciences

The scientist collaborates frequently with peers, including:

  • Mirva J. Saaranen
  • Aatir A. Tungekar
  • Rosario Recacha
  • Angel Castillo-Corujo
  • Anil A. Sohail

Best Publications

  • The human protein disulphide isomerase family: substrate interactions and functional properties

    Lars Ellgaard;Lloyd W. Ruddock

  • Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.

    Feras Hatahet;Lloyd W. Ruddock

  • The b′ domain provides the principal peptide‐binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

    Peter Klappa;Lloyd W. Ruddock;Nigel J. Darby;Nigel J. Darby;Robert B. Freedman

  • Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation

    Christoph Reinhardt;Marie Luise Von Brühl;Davit Manukyan;Lenka Grahl

  • N-glycan processing in ER quality control.

    Lloyd W. Ruddock;Maurizio Molinari

  • Two Endoplasmic Reticulum PDI Peroxidases Increase the Efficiency of the Use of Peroxide during Disulfide Bond Formation

    Van Dat Nguyen;Mirva J. Saaranen;Anna-Riikka Karala;Anna-Kaisa Lappi

  • A molecular specificity code for the three mammalian KDEL receptors

    Irina Raykhel;Heli Alanen;Kirsi Salo;Jaana Jurvansuu

  • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.

    Robert B. Freedman;Peter Klappa;Lloyd W. Ruddock

  • Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli

    Van Dat Nguyen;Feras Hatahet;Kirsi E H Salo;Eveliina Enlund

  • Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae.

    Simon S. Eaglestone;Lloyd W. Ruddock;Brian S. Cox;Mick F. Tuite

  • EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation.

    Silvia Olivari;Tito Cali;Kirsi E.H. Salo;Paolo Paganetti

  • A Major Fraction of Endoplasmic Reticulum-located Glutathione Is Present as Mixed Disulfides with Protein

    Rosemary Bass;Lloyd W. Ruddock;Peter Klappa;Robert B. Freedman

  • A Novel Stress-induced EDEM Variant Regulating Endoplasmic Reticulum-associated Glycoprotein Degradation

    Silvia Olivari;Carmela Galli;Heli Alanen;Lloyd Ruddock

  • Substrate recognition by the protein disulfide isomerases

    Feras Hatahet;Lloyd W. Ruddock

  • Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase.

    Annamari Pirneskoski;Peter Klappa;Mario Lobell;Richard A. Williamson

  • A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases.

    Anna Kaisa A.K. Lappi;Marc Lensink;Heli H.I. Alanen;Kirsi E H K.E.H. Salo

  • Insights into Deglutathionylation Reactions DIFFERENT INTERMEDIATES IN THE GLUTAREDOXIN AND PROTEIN DISULFIDE ISOMERASE CATALYZED REACTIONS ARE DEFINED BY THE γ-LINKAGE PRESENT IN GLUTATHIONE

    Mirva J. Peltoniemi;Anna-Riikka Karala;Jaana K. Jurvansuu;Vuokko L. Kinnula

  • Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain.

    Van Dat Nguyen;Katrine Wallis;Mark J. Howard;Antti M. Haapalainen

  • Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli.

    Feras Hatahet;Van Dat Nguyen;Kirsi E H Salo;Lloyd W Ruddock

  • pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate

    Lloyd W. Ruddock;Timothy R. Hirst;Robert B. Freedman

Frequent Co-Authors

Robert B. Freedman
Robert B. Freedman University of Warwick
Timothy R. Hirst
Timothy R. Hirst University of Adelaide
Maurizio Molinari
Maurizio Molinari Universita della Svizzera Italiana
Vuokko L. Kinnula
Vuokko L. Kinnula University of Helsinki
Kari I. Kivirikko
Kari I. Kivirikko University of Oulu
Ylermi Soini
Ylermi Soini University of Eastern Finland
Thomas Kietzmann
Thomas Kietzmann University of Oulu
Claudio Hetz
Claudio Hetz University of Chile
Johanna Myllyharju
Johanna Myllyharju University of Oulu
Mika Rämet
Mika Rämet Oulu University Hospital

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