Philip P. Chamberlain

5.2k total citations · 2 hit papers
27 papers, 2.1k citations indexed

About

Philip P. Chamberlain is a scholar working on Molecular Biology, Hematology and Infectious Diseases. According to data from OpenAlex, Philip P. Chamberlain has authored 27 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 10 papers in Hematology and 6 papers in Infectious Diseases. Recurrent topics in Philip P. Chamberlain's work include Protein Degradation and Inhibitors (13 papers), Multiple Myeloma Research and Treatments (9 papers) and Ubiquitin and proteasome pathways (9 papers). Philip P. Chamberlain is often cited by papers focused on Protein Degradation and Inhibitors (13 papers), Multiple Myeloma Research and Treatments (9 papers) and Ubiquitin and proteasome pathways (9 papers). Philip P. Chamberlain collaborates with scholars based in United States, United Kingdom and Switzerland. Philip P. Chamberlain's co-authors include Lawrence G. Hamann, Brian E. Cathers, Jingshan Ren, D.K. Stammers, David I. Stuart, Louise E. Bird, Barbra Pagarigan, Mary E. Matyskiela, Kurt Weaver and Thomas O. Daniel and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Philip P. Chamberlain

26 papers receiving 2.0k citations

Hit Papers

Structure of the human Cereblon–DDB1–lenalidomide complex... 2014 2026 2018 2022 2014 2019 100 200 300

Peers

Philip P. Chamberlain
L Tuel-Ahlgren United States
I. Felletar United Kingdom
C. Tallant United Kingdom
Cheng‐Ming Chiang United States
Radosław P. Nowak United States
Joseph W. Leone United States
Michael A. Milhollen United States
Christophe Dhalluin United States
David G. Sanford United States
L Tuel-Ahlgren United States
Philip P. Chamberlain
Citations per year, relative to Philip P. Chamberlain Philip P. Chamberlain (= 1×) peers L Tuel-Ahlgren

Countries citing papers authored by Philip P. Chamberlain

Since Specialization
Citations

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

Fields of papers citing papers by Philip P. Chamberlain

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Philip P. Chamberlain. 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 Philip P. Chamberlain. The network helps show where Philip P. Chamberlain may publish in the future.

Co-authorship network of co-authors of Philip P. Chamberlain

This figure shows the co-authorship network connecting the top 25 collaborators of Philip P. Chamberlain. A scholar is included among the top collaborators of Philip P. Chamberlain 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 Philip P. Chamberlain. Philip P. Chamberlain 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.
Watson, Edmond R., Scott J. Novick, Mary E. Matyskiela, et al.. (2022). Molecular glue CELMoD compounds are regulators of cereblon conformation. Science. 378(6619). 549–553. 94 indexed citations
2.
Fenalti, Gustavo, Nicolas Villanueva, Mark T. Griffith, et al.. (2021). Structure of the human marker of self 5-transmembrane receptor CD47. Nature Communications. 12(1). 5218–5218. 35 indexed citations
3.
Thompson, Joel W., Thomas Clayton, Gody Khambatta, et al.. (2021). Profiling CELMoD-Mediated Degradation of Cereblon Neosubstrates. Methods in molecular biology. 2365. 283–300. 4 indexed citations
4.
Matyskiela, Mary E., Thomas Clayton, Xinde Zheng, et al.. (2020). Crystal structure of the SALL4–pomalidomide–cereblon–DDB1 complex. Nature Structural & Molecular Biology. 27(4). 319–322. 65 indexed citations
5.
Gooding, Sarah, Naser Ansari‐Pour, Fadi Towfic, et al.. (2020). Multiple cereblon genetic changes are associated with acquired resistance to lenalidomide or pomalidomide in multiple myeloma. Blood. 137(2). 232–237. 107 indexed citations
6.
Chamberlain, Philip P. & Brian E. Cathers. (2019). Cereblon modulators: Low molecular weight inducers of protein degradation. Drug Discovery Today Technologies. 31. 29–34. 79 indexed citations
7.
Chamberlain, Philip P. & Lawrence G. Hamann. (2019). Development of targeted protein degradation therapeutics. Nature Chemical Biology. 15(10). 937–944. 344 indexed citations breakdown →
8.
Chamberlain, Philip P.. (2018). Linkers for protein degradation. Nature Chemical Biology. 14(7). 639–640. 5 indexed citations
9.
Chamberlain, Philip P., S.L. Delker, Barbra Pagarigan, et al.. (2014). Crystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes. PLoS ONE. 9(8). e103638–e103638. 11 indexed citations
10.
Chamberlain, Philip P., Antonia Lopez‐Girona, Karen Miller, et al.. (2014). Structure of the human Cereblon–DDB1–lenalidomide complex reveals basis for responsiveness to thalidomide analogs. Nature Structural & Molecular Biology. 21(9). 803–809. 371 indexed citations breakdown →
11.
Miller, Andrew T., Philip P. Chamberlain, & M. Cooke. (2008). Beyond IP3: Roles for higher order inositol phosphates in immune cell signaling. Cell Cycle. 7(4). 463–467. 30 indexed citations
12.
Ren, Jingshan, Philip P. Chamberlain, Anna Stamp, et al.. (2008). Structural Basis for the Improved Drug Resistance Profile of New Generation Benzophenone Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors. Journal of Medicinal Chemistry. 51(16). 5000–5008. 64 indexed citations
13.
Chamberlain, Philip P., Xun Qian, Amanda R. Stiles, et al.. (2007). Integration of Inositol Phosphate Signaling Pathways via Human ITPK1. Journal of Biological Chemistry. 282(38). 28117–28125. 38 indexed citations
14.
Ren, Jingshan, Charles E. Nichols, Philip P. Chamberlain, et al.. (2007). Relationship of Potency and Resilience to Drug Resistant Mutations for GW420867X Revealed by Crystal Structures of Inhibitor Complexes for Wild-Type, Leu100Ile, Lys101Glu, and Tyr188Cys Mutant HIV-1 Reverse Transcriptases. Journal of Medicinal Chemistry. 50(10). 2301–2309. 55 indexed citations
15.
Chamberlain, Philip P., Heath E. Klock, Daniel McMullan, et al.. (2006). Advances in High-throughput Methodologies for Crystallizing Proteins. Biotechnology and Genetic Engineering Reviews. 23(1). 1–20. 1 indexed citations
16.
Bird, Louise E., Philip P. Chamberlain, Guillaume B. E. Stewart-Jones, et al.. (2002). Cloning, expression, purification, and crystallisation of HIV-2 reverse transcriptase. Protein Expression and Purification. 27(1). 12–18. 9 indexed citations
17.
Chamberlain, Philip P., Jingshan Ren, C.E. Nichols, et al.. (2002). Crystal Structures of Zidovudine- or Lamivudine-Resistant Human Immunodeficiency Virus Type 1 Reverse Transcriptases Containing Mutations at Codons 41, 184, and 215. Journal of Virology. 76(19). 10015–10019. 49 indexed citations
18.
19.
Ryan, T W, et al.. (1990). Characterization of a large linear ion source. Journal of Vacuum Science & Technology A Vacuum Surfaces and Films. 8(4). 3284–3288. 2 indexed citations
20.
Chamberlain, Philip P. & Gordon H. Whitham. (1970). The oxymercuration of conformationally biassed cyclohex-2-enols. Journal of the Chemical Society B Physical Organic. 1382–1382. 4 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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