Robert B. Freedman

9.8k total citations · 1 hit paper
198 papers, 8.2k citations indexed

About

Robert B. Freedman is a scholar working on Molecular Biology, Cell Biology and Biotechnology. According to data from OpenAlex, Robert B. Freedman has authored 198 papers receiving a total of 8.2k indexed citations (citations by other indexed papers that have themselves been cited), including 125 papers in Molecular Biology, 86 papers in Cell Biology and 24 papers in Biotechnology. Recurrent topics in Robert B. Freedman's work include Endoplasmic Reticulum Stress and Disease (80 papers), Transgenic Plants and Applications (20 papers) and Protein Structure and Dynamics (19 papers). Robert B. Freedman is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (80 papers), Transgenic Plants and Applications (20 papers) and Protein Structure and Dynamics (19 papers). Robert B. Freedman collaborates with scholars based in United Kingdom, Finland and United States. Robert B. Freedman's co-authors include Hilary C. Hawkins, Lloyd W. Ruddock, Peter Klappa, Mick F. Tuite, Neil J. Bulleid, G. K. Radda, David A. Hillson, N. Lambert, Richard A. Williamson and Thomas E. Creighton and has published in prestigious journals such as Nature, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Robert B. Freedman

195 papers receiving 7.8k citations

Hit Papers

align trajectories sort by overperformance

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Protein disulphide isomerase: building bridges in protein folding

1994 614 citations Robert B. Freedman, Mick F. Tuite et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Robert B. Freedman	5.4k	3.5k	949	897	549	198	8.2k
Barbara Mulloy	4.3k 0.8×	3.6k 1.0×	746 0.8×	820 0.9×	371 0.7×	163	9.8k
Grant Fairbanks	5.9k 1.1×	1.9k 0.5×	404 0.4×	639 0.7×	490 0.9×	31	10.4k
Piero Pucci	4.6k 0.8×	921 0.3×	441 0.5×	642 0.7×	673 1.2×	297	8.3k
Lowell H. Ericsson	4.9k 0.9×	968 0.3×	457 0.5×	484 0.5×	757 1.4×	77	7.7k
Berl R. Oakley	10.2k 1.9×	5.4k 1.5×	962 1.0×	275 0.3×	466 0.8×	143	13.9k
Gilbert Ashwell	8.3k 1.5×	1.9k 0.5×	813 0.9×	1.9k 2.1×	1.4k 2.6×	124	13.3k
Harold Edelhoch	5.9k 1.1×	1.7k 0.5×	313 0.3×	400 0.4×	465 0.8×	180	9.2k
Leonard Warren	6.2k 1.1×	1.1k 0.3×	632 0.7×	1.0k 1.2×	460 0.8×	64	9.5k
Hiram Gilbert	4.4k 0.8×	2.4k 0.7×	463 0.5×	556 0.6×	229 0.4×	87	6.5k
Yasutsugu Shimonishi	5.8k 1.1×	995 0.3×	375 0.4×	1.3k 1.4×	471 0.9×	204	9.7k

Countries citing papers authored by Robert B. Freedman

Since Specialization

Citations

This map shows the geographic impact of Robert B. Freedman's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Robert B. Freedman with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Robert B. Freedman more than expected).

Fields of papers citing papers by Robert B. Freedman

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert B. Freedman. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Robert B. Freedman. The network helps show where Robert B. Freedman may publish in the future.

Co-authorship network of co-authors of Robert B. Freedman

This figure shows the co-authorship network connecting the top 25 collaborators of Robert B. Freedman. A scholar is included among the top collaborators of Robert B. Freedman based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Robert B. Freedman. Robert B. Freedman is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Beal, David M., et al.. (2019). Quantitative Analyses of the Yeast Oxidative Protein Folding Pathway In Vitro and In Vivo. Antioxidants and Redox Signaling. 31(4). 261–274. 6 indexed citations

Heal, Jack W., et al.. (2014). Effects of Ligand Binding on the Rigidity and Mobility of Proteins: An Experimental and Computational Approach. Biophysical Journal. 106(2). 658a–658a. 1 indexed citations

Alanen, Heli I., M. Lourdes Velez‐Suberbie, Cristina F.R.O. Matos, et al.. (2014). Efficient export of human growth hormone, interferon α2b and antibody fragments to the periplasm by the Escherichia coli Tat pathway in the absence of prior disulfide bond formation. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853(3). 756–763. 35 indexed citations

Wallis, A. Katrine & Robert B. Freedman. (2011). Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?. Topics in current chemistry. 328. 1–34. 17 indexed citations

Wang, Lei, Ateesh Sidhu, Li Zhu, et al.. (2008). Reconstitution of Human Ero1-Lα/Protein-Disulfide Isomerase Oxidative Folding Pathway in Vitro. Journal of Biological Chemistry. 284(1). 199–206. 128 indexed citations

Klappa, Peter, Mario Lobell, Richard A. Williamson, et al.. (2004). Molecular Characterization of the Principal Substrate Binding Site of the Ubiquitous Folding Catalyst Protein Disulfide Isomerase. Journal of Biological Chemistry. 279(11). 10374–10381. 137 indexed citations

Freedman, Robert B., Peter Klappa, & Lloyd W. Ruddock. (2002). [34] Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase. Methods in enzymology on CD-ROM/Methods in enzymology. 348. 342–354. 16 indexed citations

Hills, Anna, et al.. (2001). Metabolic control of recombinant protein N‐glycan processing in NS0 and CHO cells. Biotechnology and Bioengineering. 73(3). 188–202. 131 indexed citations

Ruddock, Lloyd W., et al.. (2001). Domains b′ and a′ of Protein Disulfide Isomerase Fulfill the Minimum Requirement for Function as a Subunit of Prolyl 4-Hydroxylase. Journal of Biological Chemistry. 276(14). 11287–11293. 49 indexed citations

10.

Freedman, Robert B., et al.. (1998). Protein folding: A missing redox link in the endoplasmic reticulum. Current Biology. 8(13). R468–R470. 28 indexed citations

11.

Ison, A. P., et al.. (1997). Real-time monitoring of recombinant protein concentration in animal cell cultures using an optical biosensor. Kent Academic Repository (University of Kent). 7 indexed citations

12.

Ali, Bassam R., Liqing Zhou, Robert B. Freedman, et al.. (1995). Cellulases and hemicellulases of the anaerobic fungusPiromycesconstitute a multiprotein cellulose-binding complex and are encoded by multigene families. FEMS Microbiology Letters. 125(1). 15–22. 63 indexed citations

13.

Ruddock, Lloyd W., et al.. (1995). Kinetics of Acid-mediated Disassembly of the B Subunit Pentamer of Escherichia coli Heat-labile Enterotoxin. Journal of Biological Chemistry. 270(50). 29953–29958. 44 indexed citations

14.

Tuite, Mick F. & Robert B. Freedman. (1994). Improving secretion of recombinant proteins from yeast and mammalian cells: Rational or empirical design?. Trends in biotechnology. 12(11). 432–434. 12 indexed citations

15.

Creighton, Thomas E. & Robert B. Freedman. (1993). Protein-structure - a model catalyst of protein disulfide bond formation. Kent Academic Repository (University of Kent). 1 indexed citations

16.

Rowling, Pamela J. E. & Robert B. Freedman. (1993). Folding, Assembly, and Posttranslational Modification of Proteins within the Lumen of the Endoplasmic Reticulum. Sub-cellular biochemistry. 21. 41–80. 32 indexed citations

17.

Freedman, Robert B., et al.. (1993). Factor affecting enzyme characteristics of bilirubin oxidase suspensions in organic solvents. Biotechnology and Bioengineering. 41(9). 887–893. 14 indexed citations

18.

Freedman, Robert B., et al.. (1989). Induction of expression of protein disulphide‐isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide. FEBS Letters. 242(2). 357–362. 14 indexed citations

19.

Hillson, David A., Nigel Lambert, & Robert B. Freedman. (1984). Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase. Methods in enzymology on CD-ROM/Methods in enzymology. 107. 281–294. 193 indexed citations

20.

Freedman, Robert B. & Hilary C. Hawkins. (1980). The Enzymology of post-translational modification of proteins. Academic Press eBooks. 193 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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