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Chemistry

D-Index
69
Citations
16350
World Ranking
6213
National Ranking
359

Biology and Biochemistry

D-Index
69
Citations
16188
World Ranking
7433
National Ranking
577

Overview

Robert B. Freedman was a researcher affiliated with the University of Warwick in the United Kingdom. Throughout their career, they contributed to the academic community primarily through their association with this institution.

No specific information on recent papers, frequent co-authors, publication venues, main fields or subfields of study, or principal research topics has been provided for Robert B. Freedman. Similarly, there are no details available about book publications or academic awards.

Given the lack of documented publications or collaborations in the available data, it is unclear which exact domains or scientific questions belonged to their primary research scope. However, their association with a reputable university suggests involvement in scholarly activities aligned with the institution's academic standards.

The available data confirms that Robert B. Freedman is deceased, which frames their scholarly contributions as part of the historical record within their field and academic community.

Best Publications

  • Genomic Relationships, Novel Loci, and Pleiotropic Mechanisms across Eight Psychiatric Disorders

    Phil H. Lee;Verneri Anttila;Hyejung Won;Yen-Chen A. Feng

  • Protein disulphide isomerase: building bridges in protein folding

    Robert B. Freedman;Timothy R. Hirst;Mick F. Tuite

  • Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins

    Robert B. Freedman

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

    Neil J. Bulleid;Robert B. Freedman

  • 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

  • Native disulphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomerase

    Robert B. Freedman

  • Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase.

    David A. Hillson;Nigel Lambert;Robert B. Freedman

  • Metabolic control of recombinant protein N-glycan processing in NS0 and CHO cells

    Kym N. Baker;Mark H. Rendall;Mark H. Rendall;Anna E. Hills;Michael Hoare

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

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

  • Membrane studies with polarity-dependant and excimer-forming fluorescent probes

    J. R. Brocklehurst;R. B. Freedman;D. J. Hancock;G. K. Radda

  • Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds

    Thomas E. Creighton;David A. Hillson;Robert B. Freedman

  • Activity of lipase in water-in-oil microemulsions

    Paul D. I. Fletcher;Brian H. Robinson;Robert B. Freedman;Christopher Oldfield

  • Soil urease activity stability and kinetic properties

    N.M. Pettit;A.R.J. Smith;R.B. Freedman;R.G. Burns

  • Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP).

    Richard A. Williamson;Fiona A. Marston;Sarojani Angal;P. Koklitis

  • 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

  • N-glycosylation of recombinant human interferon-gamma produced in different animal expression systems.

    David C. James;Robert B. Freedman;Michael Hoare;Olotu W. Ogonah

  • The reaction of 2,4,6-trinitrobenzenesulphonic acid with amino acids, Peptides and proteins

    R. B. Freedman;G. K. Radda

  • Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure

    N Lambert;R B Freedman

  • The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase

    Hilary C. Hawkins;Robert B. Freedman

  • Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase.

    Lei Wang;Sheng-jian Li;Ateesh Sidhu;Li Zhu

  • The Enzymology of post-translational modification of proteins

    R. B. Freedman;Hilary C. Hawkins

Frequent Co-Authors

Lloyd W. Ruddock
Lloyd W. Ruddock University of Oulu
Mick F. Tuite
Mick F. Tuite University of Kent
Neil J. Bulleid
Neil J. Bulleid University of Glasgow
William Byerley
William Byerley University of California, San Francisco
David Curtis
David Curtis Queen Mary University of London
Michael Gill
Michael Gill Trinity College Dublin
Dominique Campion
Dominique Campion University of Rouen
Douglas F. Levinson
Douglas F. Levinson Stanford University
George Kirov
George Kirov Cardiff University
Naomi R. Wray
Naomi R. Wray University of Queensland

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