Laurence H. Pearl

28.1k total citations · 7 hit papers
217 papers, 21.3k citations indexed

About

Laurence H. Pearl is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Laurence H. Pearl has authored 217 papers receiving a total of 21.3k indexed citations (citations by other indexed papers that have themselves been cited), including 192 papers in Molecular Biology, 53 papers in Materials Chemistry and 31 papers in Oncology. Recurrent topics in Laurence H. Pearl's work include Heat shock proteins research (66 papers), Enzyme Structure and Function (52 papers) and DNA Repair Mechanisms (51 papers). Laurence H. Pearl is often cited by papers focused on Heat shock proteins research (66 papers), Enzyme Structure and Function (52 papers) and DNA Repair Mechanisms (51 papers). Laurence H. Pearl collaborates with scholars based in United Kingdom, United States and Spain. Laurence H. Pearl's co-authors include Chrisostomos Prodromou, S. Mark Roe, Peter W. Piper, Barry Panaretou, John E. Ladbury, Ronan O’Brien, Antony W. Oliver, Cara K. Vaughan, William R. Taylor and Paul Workman and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Laurence H. Pearl

213 papers receiving 20.9k citations

Hit Papers

Identification and Structural Characterization of the ATP... 1997 2026 2006 2016 1997 2006 1999 2006 2003 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Laurence H. Pearl United Kingdom 76 18.0k 2.7k 2.5k 2.2k 2.1k 217 21.3k
Len Neckers United States 85 19.4k 1.1× 1.5k 0.6× 3.1k 1.3× 3.0k 1.4× 4.0k 1.9× 248 24.9k
A. Joachimiak United States 72 14.6k 0.8× 3.5k 1.3× 1.3k 0.5× 1.7k 0.8× 2.2k 1.0× 392 22.3k
Gert Vriend Netherlands 63 15.3k 0.9× 3.7k 1.4× 1.4k 0.6× 1.0k 0.5× 1.5k 0.7× 192 21.0k
John E. Ladbury United Kingdom 56 9.1k 0.5× 1.2k 0.5× 1.4k 0.6× 1.3k 0.6× 1.5k 0.7× 175 12.3k
T. Alwyn Jones Sweden 66 21.1k 1.2× 6.0k 2.2× 2.1k 0.9× 2.5k 1.1× 2.4k 1.1× 181 29.7k
Malcolm W. MacArthur United Kingdom 18 18.7k 1.0× 5.7k 2.1× 1.7k 0.7× 1.8k 0.8× 2.0k 1.0× 20 25.5k
Johannes Büchner Germany 91 25.7k 1.4× 5.4k 2.0× 1.2k 0.5× 4.7k 2.2× 4.0k 1.9× 293 29.8k
Wolfram Bode Germany 92 15.0k 0.8× 2.3k 0.9× 5.5k 2.2× 2.2k 1.0× 2.3k 1.1× 282 28.0k
Luke Whitesell United States 59 10.3k 0.6× 780 0.3× 1.7k 0.7× 2.1k 0.9× 4.2k 2.0× 147 15.8k
Wim G. J. Hol United States 82 15.6k 0.9× 3.9k 1.5× 1.7k 0.7× 1.6k 0.7× 1.7k 0.8× 316 23.2k

Countries citing papers authored by Laurence H. Pearl

Since Specialization
Citations

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

Fields of papers citing papers by Laurence H. Pearl

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Laurence H. Pearl. 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 Laurence H. Pearl. The network helps show where Laurence H. Pearl may publish in the future.

Co-authorship network of co-authors of Laurence H. Pearl

This figure shows the co-authorship network connecting the top 25 collaborators of Laurence H. Pearl. A scholar is included among the top collaborators of Laurence H. Pearl 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 Laurence H. Pearl. Laurence H. Pearl 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.
Day, M.W., Yuichiro Saito, Masato T. Kanemaki, et al.. (2025). The human RIF1-Long isoform interacts with BRCA1 to promote recombinational fork repair under DNA replication stress. Nature Communications. 16(1). 5820–5820.
2.
Nieminuszczy, Jadwiga, Jörg Mansfeld, Laurence H. Pearl, et al.. (2025). The CIP2A-TOPBP1 axis facilitates mitotic DNA repair via MiDAS and MMEJ. Nature Communications. 16(1). 10623–10623.
3.
Day, M.W., Markus Räschle, Farnusch Kaschani, et al.. (2024). TopBP1 utilises a bipartite GINS binding mode to support genome replication. Nature Communications. 15(1). 1797–1797. 4 indexed citations
4.
Day, M.W., Antony W. Oliver, & Laurence H. Pearl. (2022). Structure of the human RAD17–RFC clamp loader and 9–1–1 checkpoint clamp bound to a dsDNA–ssDNA junction. Nucleic Acids Research. 50(14). 8279–8289. 19 indexed citations
5.
Day, M.W., Antony W. Oliver, & Laurence H. Pearl. (2021). Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1. DNA repair. 108. 103232–103232. 21 indexed citations
6.
Vidler, Lewis R., P. J. Simpson, Bissan Al‐Lazikani, et al.. (2020). Solution structure of the Hop TPR2A domain and investigation of target druggability by NMR, biochemical and in silico approaches. Scientific Reports. 10(1). 16000–16000. 11 indexed citations
7.
Bigot, Nicolas, M.W. Day, Robert A. Baldock, et al.. (2019). Phosphorylation-mediated interactions with TOPBP1 couple 53BP1 and 9-1-1 to control the G1 DNA damage checkpoint. eLife. 8. 40 indexed citations
8.
Martino, Fabrizio, Mohinder Pal, Hugo Muñoz-Hernández, et al.. (2018). RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nature Communications. 9(1). 1501–1501. 53 indexed citations
10.
Smith, Jeffrey R., Emmanuel de Billy, Steve Hobbs, et al.. (2013). Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins. Oncogene. 34(1). 15–26. 34 indexed citations
11.
Dekker, Carien, S. Mark Roe, Elizabeth A. McCormack, et al.. (2011). The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. The EMBO Journal. 30(15). 3078–3090. 80 indexed citations
12.
Anderson, Victoria E., Michael I. Walton, Paul D. Eve, et al.. (2011). CCT241533 Is a Potent and Selective Inhibitor of CHK2 that Potentiates the Cytotoxicity of PARP Inhibitors. Cancer Research. 71(2). 463–472. 79 indexed citations
13.
Kumar, Sanjeev, John A. Hinks, Joseph D Maman, et al.. (2011). p185, an Immunodominant Epitope, Is an Autoantigen Mimotope. Journal of Biological Chemistry. 286(29). 26220–26227. 4 indexed citations
14.
Bunney, Tom D., S. Mark Roe, Petra Vatter, et al.. (2009). Structural Insights into Formation of an Active Signaling Complex between Rac and Phospholipase C Gamma 2. Molecular Cell. 34(2). 223–233. 54 indexed citations
15.
Bunney, Tom D., Richard Harris, Michelle B. Josephs, et al.. (2006). Structural and Mechanistic Insights into Ras Association Domains of Phospholipase C Epsilon. Molecular Cell. 21(4). 495–507. 111 indexed citations
16.
Sharp, Swee Y., Alison Maloney, Paul A. Clarke, et al.. (2004). Mechanism of action of a novel series of inhibitors of the Hsp90 molecular chaperone. Cancer Research. 64. 922–923. 1 indexed citations
17.
Prodromou, Chrisostomos, S. Mark Roe, Ronan O’Brien, et al.. (1997). Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone. Cell. 90(1). 65–75. 1058 indexed citations breakdown →
18.
Koulis, Athanasios, Don A. Cowan, Laurence H. Pearl, & Renos Savva. (1996). Uracil-DNA glycosylase activities in hyperthermophilic micro-organisms. FEMS Microbiology Letters. 143(2-3). 267–271. 34 indexed citations
19.
Pearl, Laurence H. & Renos Savva. (1995). DNA repair in three dimensions. Trends in Biochemical Sciences. 20(10). 421–426. 13 indexed citations
20.
Moelling, Karin, et al.. (1990). In vitro inhibition of HIV‐1 proteinase by cerulenin. FEBS Letters. 261(2). 373–377. 24 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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