John H. Bushweller

9.1k total citations · 2 hit papers
113 papers, 6.1k citations indexed

About

John H. Bushweller is a scholar working on Molecular Biology, Hematology and Materials Chemistry. According to data from OpenAlex, John H. Bushweller has authored 113 papers receiving a total of 6.1k indexed citations (citations by other indexed papers that have themselves been cited), including 99 papers in Molecular Biology, 35 papers in Hematology and 16 papers in Materials Chemistry. Recurrent topics in John H. Bushweller's work include Acute Myeloid Leukemia Research (34 papers), Protein Degradation and Inhibitors (21 papers) and Genomics and Chromatin Dynamics (17 papers). John H. Bushweller is often cited by papers focused on Acute Myeloid Leukemia Research (34 papers), Protein Degradation and Inhibitors (21 papers) and Genomics and Chromatin Dynamics (17 papers). John H. Bushweller collaborates with scholars based in United States, United Kingdom and Sweden. John H. Bushweller's co-authors include Lukas K. Tamm, Tomasz Cierpicki, Nancy A. Speck, David S. Cafiso, Xing Han, Frits Abildgaard, Ashish Arora, Kurt Wuethrich, Stephen M. Lukasik and Marcelo J. Berardi and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

John H. Bushweller

111 papers receiving 6.1k citations

Hit Papers

2 papers align trajectories

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.

Targeting transcription factors in cancer — from undruggable to reality

2019 601 citations John H. Bushweller profile →
The CBFβ Subunit Is Essential for CBFα2 (AML1) Function In Vivo

1996 532 citations John H. Bushweller, Nancy A. Speck et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John H. Bushweller United States	44	4.9k	1.2k	657	545	503	113	6.1k
Timothy R. Dafforn United Kingdom	50	5.0k 1.0×	592 0.5×	1.0k 1.5×	612 1.1×	707 1.4×	152	7.4k
Tomasz Cierpicki United States	40	3.5k 0.7×	622 0.5×	390 0.6×	567 1.0×	202 0.4×	113	4.7k
Michael Blaber United States	42	3.7k 0.8×	1.1k 0.9×	555 0.8×	650 1.2×	228 0.5×	137	5.9k
Milton T. Stubbs Germany	41	3.4k 0.7×	964 0.8×	255 0.4×	607 1.1×	116 0.2×	117	5.6k
Jean‐Paul Mornon France	42	4.1k 0.9×	450 0.4×	550 0.8×	639 1.2×	217 0.4×	132	6.5k
Thomas E. Smithgall United States	52	4.3k 0.9×	1.1k 0.9×	859 1.3×	1.9k 3.5×	250 0.5×	175	7.7k
Sucha Sudarsanam United States	16	6.1k 1.3×	303 0.3×	1.1k 1.7×	1.4k 2.6×	634 1.3×	29	8.1k
Markus A. Seeliger United States	33	3.1k 0.6×	760 0.6×	654 1.0×	792 1.5×	142 0.3×	74	4.5k
Miguel Llinás United States	33	4.5k 0.9×	426 0.4×	573 0.9×	451 0.8×	835 1.7×	112	6.3k
Fritz K. Winkler Switzerland	35	3.2k 0.7×	523 0.4×	837 1.3×	402 0.7×	141 0.3×	60	4.9k

Countries citing papers authored by John H. Bushweller

Since Specialization

Citations

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

Fields of papers citing papers by John H. Bushweller

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John H. Bushweller

This figure shows the co-authorship network connecting the top 25 collaborators of John H. Bushweller. A scholar is included among the top collaborators of John H. Bushweller 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 John H. Bushweller. John H. Bushweller 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

Coleman, Daniel, Peter Keane, Paulynn Suyin Chin, et al.. (2024). Pharmacological inhibition of RAS overcomes FLT3 inhibitor resistance in FLT3-ITD+ AML through AP-1 and RUNX1. iScience. 27(4). 109576–109576. 7 indexed citations

Peramangalam, Philomina Sona, Shikan Zheng, Robert Burns, et al.. (2024). N-MYC regulates cell survival via eIF4G1 in inv(16) acute myeloid leukemia. Science Advances. 10(9). eadh8493–eadh8493. 1 indexed citations

Hegde, Mahesh, Roger Mulet‐Lazaro, Mayumi Sugita, et al.. (2024). The co-receptor Neuropilin-1 enhances proliferation in inv(16) acute myeloid leukemia via VEGF signaling. Leukemia. 39(2). 360–370. 2 indexed citations

Vanzulli, Silvia I., Sebastián Giulianelli, Eunice Spengler, et al.. (2024). FGFR2‐RUNX2 activation: An unexplored therapeutic pathway in luminal breast cancer related to tumor progression. International Journal of Cancer. 156(10). 2024–2038. 1 indexed citations

Schmidt, Charles, Nicholas J. Achille, Aravinda Kuntimaddi, et al.. (2020). BCOR Binding to MLL-AF9 Is Essential for Leukemia via Altered EYA1, SIX, and MYC Activity. Blood Cancer Discovery. 1(2). 162–177. 18 indexed citations

Whitmore, Hannah, Dhanesh Amarnani, Michael O’Hare, et al.. (2020). TNF‐α signaling regulates RUNX1 function in endothelial cells. The FASEB Journal. 35(2). e21155–e21155. 29 indexed citations

Boulton, Adam, Kelley E. McQueeney, John H. Bushweller, et al.. (2020). Structure of the Complex of an Iminopyridinedione Protein Tyrosine Phosphatase 4A3 Phosphatase Inhibitor with Human Serum Albumin. Molecular Pharmacology. 98(6). 648–657. 10 indexed citations

Illendula, Anuradha, John Anto Pulikkan, Justine E. Roderick, et al.. (2017). RUNX1 is required for oncogenic Myb and Myc enhancer activity in T-cell acute lymphoblastic leukemia. Blood. 130(15). 1722–1733. 65 indexed citations

Castilla, Lucio H. & John H. Bushweller. (2017). Molecular Basis and Targeted Inhibition of CBFβ-SMMHC Acute Myeloid Leukemia. Advances in experimental medicine and biology. 962. 229–244. 3 indexed citations

10.

Singh, Arpita, et al.. (2017). Bacillus anthracis Peptidoglycan Integrity Is Disrupted by the Chemokine CXCL10 through the FtsE/X Complex. Frontiers in Microbiology. 8. 740–740. 10 indexed citations

11.

Chen, Huiling, Victor Olman, Charles K. Mobley, et al.. (2011). Optimal Mutation Sites for PRE Data Collection and Membrane Protein Structure Prediction. Structure. 19(4). 484–495. 20 indexed citations

12.

Roudaia, Liya, Matthew D. Cheney, Wei Chen, et al.. (2009). CBFβ is critical for AML1-ETO and TEL-AML1 activity. Blood. 113(13). 3070–3079. 40 indexed citations

13.

Park, Sang‐Ho, Wei Chen, Tomasz Cierpicki, et al.. (2009). Structure of the AML1-ETO eTAFH domain–HEB peptide complex and its contribution to AML1-ETO activity. Blood. 113(15). 3558–3567. 28 indexed citations

14.

Cierpicki, Tomasz, Jolanta Grembecka, Stephen M. Lukasik, et al.. (2009). Structure of the MLL CXXC domain–DNA complex and its functional role in MLL-AF9 leukemia. Nature Structural & Molecular Biology. 17(1). 62–68. 144 indexed citations

15.

Grembecka, Jolanta, Tomasz Cierpicki, Y. Devedjiev, et al.. (2006). The Binding of the PDZ Tandem of Syntenin to Target Proteins^,. Biochemistry. 45(11). 3674–3683. 72 indexed citations

16.

Cierpicki, Tomasz, Binyong Liang, Lukas K. Tamm, & John H. Bushweller. (2006). Increasing the Accuracy of Solution NMR Structures of Membrane Proteins by Application of Residual Dipolar Couplings. High-Resolution Structure of Outer Membrane Protein A. Journal of the American Chemical Society. 128(21). 6947–6951. 63 indexed citations

17.

Kim, Myung Hee, Tomasz Cierpicki, Urszula Derewenda, et al.. (2003). The DCX-domain tandems of doublecortin and doublecortin-like kinase. Nature Structural & Molecular Biology. 10(5). 324–333. 108 indexed citations

18.

Berardi, Marcelo J., Chaohong Sun, Frits Abildgaard, et al.. (1999). The Ig fold of the core binding factor α Runt domain is a member of a family of structurally and functionally related Ig-fold DNA-binding domains. Structure. 7(10). 1247–1256. 70 indexed citations

19.

Kelley, John J., et al.. (1997). Comparison of Backbone Dynamics of Reduced and Oxidized Escherichia coli Glutaredoxin-1 Using ¹⁵N NMR Relaxation Measurements. Biochemistry. 36(16). 5029–5044. 33 indexed citations

20.

Crute, Barbara E., et al.. (1996). Biochemical and Biophysical Properties of the Core-binding Factor α2 (AML1) DNA-binding Domain. Journal of Biological Chemistry. 271(42). 26251–26260. 56 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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