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Biology and Biochemistry

D-Index
60
Citations
12375
World Ranking
11993
National Ranking
924

Research.com Recognitions

  • 2011 - Fellow of the Royal Society of Edinburgh

Overview

Neil J. Bulleid is affiliated with the University of Glasgow in the United Kingdom. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology, with a significant focus on Medicine.

The scientist's subfields of study include Cell Biology, Molecular Biology, Physiology, Genetics, and Epidemiology. Their main research topics encompass Endoplasmic Reticulum Stress and Disease, Cellular Transport and Secretion, Autophagy in Disease and Therapy, Redox Biology and Oxidative Stress, Connective Tissue Disorders Research, Sulfur Compounds in Biology, and Adenosine and Purinergic Signaling.

Notable recent papers authored by or involving Neil J. Bulleid include:

  • Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway, 2020, Cells
  • Activation of the UPR sensor ATF6α is regulated by its redox-dependent dimerization and ER retention by ERp18, 2022, Proceedings of the National Academy of Sciences
  • The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins, 2020, Journal of Cell Science
  • Protein secondary structure determines the temporal relationship between folding and disulfide formation, 2020, Journal of Biological Chemistry
  • Dietary-derived vitamin B12 protects Caenorhabditis elegans from thiol-reducing agents, 2022, BMC Biology

Frequent co-authors in their scientific work include Marie Anne Pringle, Philip J. Robinson, Bethany Fleming, Tom Van Agtmael, and Zhenbo Cao.

The common venues where Neil J. Bulleid's work is published are the Journal of Cell Science, Cell Death Discovery, bioRxiv (Cold Spring Harbor Laboratory), Cells, and Proceedings of the National Academy of Sciences.

Neil J. Bulleid was awarded the title of Fellow of the Royal Society of Edinburgh in 2011.

Best Publications

  • Protein Folding and Modification in the Mammalian Endoplasmic Reticulum

    Ineke Braakman;Neil J. Bulleid

  • The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress.

    Seema Chakravarthi;Catherine E Jessop;Neil J Bulleid

  • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

    Jason D. Oliver;Fimme J. van der Wal;Neil J. Bulleid;Stephen High

  • Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes.

    Neil J. Bulleid;Robert B. Freedman

  • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum.

    Andrea Cabibbo;Massimiliano Pagani;Marco Fabbri;Mariano Rocchi

  • Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

    Timothy J Tavender;Jennifer J Springate;Neil J Bulleid

  • Endoplasmic Reticulum Oxidoreductin 1-Lβ (ERO1-Lβ), a Human Gene Induced in the Course of the Unfolded Protein Response

    Massimiliano Pagani;Marco Fabbri;Cristina Benedetti;Anna Fassio

  • Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen.

    Mohammed Tasab;Margaret R. Batten;Neil J. Bulleid

  • Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process

    Jan Riemer;Neil Bulleid;Johannes M. Herrmann

  • Multiple ways to make disulfides

    Neil J. Bulleid;Lars Ellgaard

  • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.

    Catherine E. Jessop;Rachel H. Watkins;Jennifer J. Simmons;Mohammed Tasab

  • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains

    Catherine E Jessop;Seema Chakravarthi;Natalio Garbi;Günter J Hämmerling

  • Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation

    Timothy J. Tavender;Neil J. Bulleid

  • Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells

    Catherine E. Jessop;Neil J. Bulleid

  • Glutathione Is Required to Regulate the Formation of Native Disulfide Bonds within Proteins Entering the Secretory Pathway

    Seema Chakravarthi;Neil J. Bulleid

  • Identification of the molecular recognition sequence which determines the type‐specific assembly of procollagen

    Janice F. Lees;Mohammed Tasab;Neil J. Bulleid

  • Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells

    Timothy J. Tavender;Alyson M. Sheppard;Neil J. Bulleid

  • Protein disulfide Isomerase Acts as a Molecular Chaperone during the Assembly of Procollagen

    Richard Wilson;Janice F. Lees;Neil J. Bulleid

  • The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells.

    R Wilson;A J Allen;J Oliver;J L Brookman

  • Real-Time Fluorescence Detection of ERAD Substrate Retrotranslocation in a Mammalian In Vitro System

    Judit Wahlman;George N. DeMartino;William R. Skach;Neil J. Bulleid

Frequent Co-Authors

Karl E. Kadler
Karl E. Kadler University of Manchester
Robert B. Freedman
Robert B. Freedman University of Warwick
Philip C. Robinson
Philip C. Robinson University of Queensland
Richard Wilson
Richard Wilson Department for Environment Food and Rural Affairs
Rhian M. Touyz
Rhian M. Touyz McGill University Health Centre
Ineke Braakman
Ineke Braakman Utrecht University
Stephen High
Stephen High University of Manchester
Roberto Sitia
Roberto Sitia Vita-Salute San Raffaele University
Gunnar von Heijne
Gunnar von Heijne Stockholm University
Martin J. Humphries
Martin J. Humphries University of Manchester

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