David B. Williams

8.5k total citations · 2 hit papers
60 papers, 7.1k citations indexed

About

David B. Williams is a scholar working on Cell Biology, Molecular Biology and Immunology. According to data from OpenAlex, David B. Williams has authored 60 papers receiving a total of 7.1k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Cell Biology, 35 papers in Molecular Biology and 35 papers in Immunology. Recurrent topics in David B. Williams's work include Endoplasmic Reticulum Stress and Disease (38 papers), Heat shock proteins research (19 papers) and Toxin Mechanisms and Immunotoxins (16 papers). David B. Williams is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (38 papers), Heat shock proteins research (19 papers) and Toxin Mechanisms and Immunotoxins (16 papers). David B. Williams collaborates with scholars based in Canada, United States and Japan. David B. Williams's co-authors include Myrna F. Cohen-Doyle, Eleanor A Degen, Per A. Peterson, Michael R. Jackson, David Y. Thomas, Aikaterini Vassilakos, John Bergeron, S. Pind, Timothy J. Jensen and John R. Riordan and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David B. Williams

60 papers receiving 7.0k citations

Hit Papers

Multiple proteolytic systems, including the proteasome, c... 1995 2026 2005 2015 1995 2009 200 400 600

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
David B. Williams Canada 41 3.7k 3.3k 3.0k 949 633 60 7.1k
Stephen M. Robbins Canada 44 2.9k 0.8× 2.3k 0.7× 1.1k 0.4× 510 0.5× 760 1.2× 90 6.1k
Ineke Braakman Netherlands 45 5.2k 1.4× 1.5k 0.4× 3.7k 1.2× 1.4k 1.5× 327 0.5× 100 8.3k
Toshisuke Kawasaki Japan 47 5.4k 1.5× 2.9k 0.9× 1.3k 0.4× 415 0.4× 417 0.7× 179 8.0k
Václav Hořejšı́ Czechia 51 4.1k 1.1× 4.6k 1.4× 1.0k 0.3× 383 0.4× 795 1.3× 168 8.4k
Waldemar Kolanus Germany 40 3.1k 0.8× 2.3k 0.7× 1.2k 0.4× 483 0.5× 754 1.2× 87 6.1k
Bharat Joshi United States 42 2.8k 0.8× 1.6k 0.5× 847 0.3× 481 0.5× 1.1k 1.7× 109 5.5k
Xosé R. Bustelo Spain 57 7.0k 1.9× 2.8k 0.9× 1.9k 0.6× 382 0.4× 2.0k 3.2× 172 11.1k
Claudio Schneider Italy 43 4.4k 1.2× 1.4k 0.4× 826 0.3× 597 0.6× 1.2k 1.9× 79 6.4k
Espen Stang Norway 37 3.8k 1.0× 841 0.3× 2.7k 0.9× 398 0.4× 967 1.5× 80 5.8k
E. Sergio Trombetta United States 24 2.5k 0.7× 2.3k 0.7× 1.1k 0.3× 457 0.5× 613 1.0× 27 4.8k

Countries citing papers authored by David B. Williams

Since Specialization
Citations

This map shows the geographic impact of David B. Williams'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 David B. Williams with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites David B. Williams more than expected).

Fields of papers citing papers by David B. Williams

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David B. Williams. 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 David B. Williams. The network helps show where David B. Williams may publish in the future.

Co-authorship network of co-authors of David B. Williams

This figure shows the co-authorship network connecting the top 25 collaborators of David B. Williams. A scholar is included among the top collaborators of David B. Williams 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 David B. Williams. David B. Williams is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Pocanschi, Cosmin L., et al.. (2011). Structural and Functional Relationships between the Lectin and Arm Domains of Calreticulin. Journal of Biological Chemistry. 286(31). 27266–27277. 42 indexed citations
2.
Cohen-Doyle, Myrna F., et al.. (2010). Functional Relationship between Protein Disulfide Isomerase Family Members during the Oxidative Folding of Human Secretory Proteins. Molecular Biology of the Cell. 21(18). 3093–3105. 75 indexed citations
3.
Kozlov, Guennadi, Cosmin L. Pocanschi, Angelika Rosenauer, et al.. (2010). Structural Basis of Carbohydrate Recognition by Calreticulin. Journal of Biological Chemistry. 285(49). 38612–38620. 122 indexed citations
4.
Williams, David B., et al.. (2010). ER quality control in the biogenesis of MHC class I molecules. Seminars in Cell and Developmental Biology. 21(5). 512–519. 43 indexed citations
5.
Zhang, Yi-Nan, Guennadi Kozlov, Cosmin L. Pocanschi, et al.. (2009). ERp57 Does Not Require Interactions with Calnexin and Calreticulin to Promote Assembly of Class I Histocompatibility Molecules, and It Enhances Peptide Loading Independently of Its Redox Activity. Journal of Biological Chemistry. 284(15). 10160–10173. 44 indexed citations
6.
Li, Jing, et al.. (2009). Loss of Specific Chaperones Involved in Membrane Glycoprotein Biosynthesis during the Maturation of Human Erythroid Progenitor Cells. Journal of Biological Chemistry. 284(21). 14547–14557. 25 indexed citations
7.
Brockmeier, Ulf, et al.. (2008). Distinct Contributions of the Lectin and Arm Domains of Calnexin to Its Molecular Chaperone Function. Journal of Biological Chemistry. 284(6). 3433–3444. 24 indexed citations
8.
Williams, David B., et al.. (2006). In Vitro Assays of the Functions of Calnexin and Calreticulin, Lectin Chaperones of the Endoplasmic Reticulum. Humana Press eBooks. 347. 331–342. 7 indexed citations
9.
Zhang, Yi-Nan, Ehtesham Baig, & David B. Williams. (2006). Functions of ERp57 in the Folding and Assembly of Major Histocompatibility Complex Class I Molecules. Journal of Biological Chemistry. 281(21). 14622–14631. 61 indexed citations
10.
Paquet, Marie-Ève, Myrna F. Cohen-Doyle, Gordon C. Shore, & David B. Williams. (2004). Bap29/31 Influences the Intracellular Traffic of MHC Class I Molecules. The Journal of Immunology. 172(12). 7548–7555. 79 indexed citations
11.
Leach, Michael R. & David B. Williams. (2004). Lectin-deficient Calnexin Is Capable of Binding Class I Histocompatibility Molecules in Vivo and Preventing Their Degradation. Journal of Biological Chemistry. 279(10). 9072–9079. 54 indexed citations
12.
Williams, David B., et al.. (2002). Mutant MHC class I molecules define interactions between components of the peptide‐loading complex. International Immunology. 14(4). 347–358. 29 indexed citations
13.
Danilczyk, Ursula, Myrna F. Cohen-Doyle, & David B. Williams. (2000). Functional Relationship between Calreticulin, Calnexin, and the Endoplasmic Reticulum Luminal Domain of Calnexin. Journal of Biological Chemistry. 275(17). 13089–13097. 85 indexed citations
14.
Suh, Woong‐Kyung, Michael A. Derby, Myrna F. Cohen-Doyle, et al.. (1999). Interaction of Murine MHC Class I Molecules with Tapasin and TAP Enhances Peptide Loading and Involves the Heavy Chain α3 Domain. The Journal of Immunology. 162(3). 1530–1540. 69 indexed citations
15.
Ihara, Yoshito, Myrna F. Cohen-Doyle, Yoshiro Saito, & David B. Williams. (1999). Calnexin Discriminates between Protein Conformational States and Functions as a Molecular Chaperone In Vitro. Molecular Cell. 4(3). 331–341. 135 indexed citations
16.
Vassilakos, Aikaterini, et al.. (1995). The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins. Journal of Biological Chemistry. 270(9). 4697–4704. 356 indexed citations
17.
Williams, David B.. (1995). Calnexin: a molecular chaperone with a taste for carbohydrate. Biochemistry and Cell Biology. 73(3-4). 123–132. 57 indexed citations
18.
Bergeron, John, Michael B. Brenner, David Y. Thomas, & David B. Williams. (1994). Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends in Biochemical Sciences. 19(3). 124–128. 459 indexed citations
19.
Degen, Eleanor A, Myrna F. Cohen-Doyle, & David B. Williams. (1992). Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide.. The Journal of Experimental Medicine. 175(6). 1653–1661. 163 indexed citations
20.
Luscher, Mark A., et al.. (1991). Peptide binding to class I MHC on living cells and quantitation of complexes required for CTL lysis. Nature. 352(6330). 67–70. 294 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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