B.D. Bax

6.6k total citations
70 papers, 3.9k citations indexed

About

B.D. Bax is a scholar working on Molecular Biology, Materials Chemistry and Toxicology. According to data from OpenAlex, B.D. Bax has authored 70 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 51 papers in Molecular Biology, 15 papers in Materials Chemistry and 11 papers in Toxicology. Recurrent topics in B.D. Bax's work include Cancer therapeutics and mechanisms (17 papers), Bioactive Compounds and Antitumor Agents (11 papers) and Enzyme Structure and Function (10 papers). B.D. Bax is often cited by papers focused on Cancer therapeutics and mechanisms (17 papers), Bioactive Compounds and Antitumor Agents (11 papers) and Enzyme Structure and Function (10 papers). B.D. Bax collaborates with scholars based in United Kingdom, United States and Germany. B.D. Bax's co-authors include Jörg Müssig, Peter F. Lindley, Tom L. Blundell, C. Slingsby, Pan F. Chan, H.P.C. Driessen, V. Nalini, G.L. Card, I. Zaitseva and A. Ralph and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

B.D. Bax

70 papers receiving 3.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
B.D. Bax United Kingdom 32 2.4k 421 383 372 360 70 3.9k
Junhua Wu China 38 2.2k 0.9× 309 0.7× 480 1.3× 226 0.6× 413 1.1× 171 4.9k
Mingzhen Zhang United States 35 1.8k 0.8× 116 0.3× 407 1.1× 278 0.7× 174 0.5× 84 3.3k
Xiaoying Wang China 38 2.5k 1.1× 240 0.6× 251 0.7× 141 0.4× 151 0.4× 209 5.7k
Yonglan Liu United States 29 914 0.4× 344 0.8× 367 1.0× 243 0.7× 95 0.3× 82 2.7k
Wencheng Zhu China 29 1.2k 0.5× 562 1.3× 335 0.9× 213 0.6× 113 0.3× 63 3.5k
Liyan Qiu China 36 1.5k 0.6× 443 1.1× 1.5k 4.0× 484 1.3× 110 0.3× 136 3.9k
Masayoshi Itoh Japan 39 3.2k 1.3× 430 1.0× 126 0.3× 751 2.0× 219 0.6× 188 6.1k
Jiangning Chen China 43 2.8k 1.2× 181 0.4× 871 2.3× 234 0.6× 135 0.4× 125 5.6k
Mihee Kim South Korea 21 1.9k 0.8× 185 0.4× 422 1.1× 271 0.7× 303 0.8× 75 4.0k
Hu‐Lin Jiang China 46 3.0k 1.3× 310 0.7× 1.8k 4.6× 357 1.0× 225 0.6× 195 6.7k

Countries citing papers authored by B.D. Bax

Since Specialization
Citations

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

Fields of papers citing papers by B.D. Bax

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of B.D. Bax

This figure shows the co-authorship network connecting the top 25 collaborators of B.D. Bax. A scholar is included among the top collaborators of B.D. Bax 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 B.D. Bax. B.D. Bax 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.
Wilkinson, H. Scott, et al.. (2025). Gene editing for collagen disorders: current advances and future perspectives. Gene Therapy. 32(6). 676–689. 1 indexed citations
2.
Nicholls, Robert A., Anna J. Warren, Simon E. Ward, et al.. (2024). How Do Gepotidacin and Zoliflodacin Stabilize DNA Cleavage Complexes with Bacterial Type IIA Topoisomerases? 1. Experimental Definition of Metal Binding Sites. International Journal of Molecular Sciences. 25(21). 11688–11688. 1 indexed citations
3.
Nicholls, Robert A., et al.. (2024). How Do Gepotidacin and Zoliflodacin Stabilize DNA-Cleavage Complexes with Bacterial Type IIA Topoisomerases? 2. A Single Moving Metal Mechanism. International Journal of Molecular Sciences. 26(1). 33–33. 1 indexed citations
4.
Elvers, Karen T, S. Mark Roe, Simon E. Ward, et al.. (2022). Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase. Communications Biology. 5(1). 346–346. 5 indexed citations
5.
Bax, B.D., et al.. (2020). Conformational flexibility within the small domain of human serine racemase. Acta Crystallographica Section F Structural Biology Communications. 76(2). 65–73. 4 indexed citations
6.
Bax, B.D., Garib N. Murshudov, Anthony Maxwell, & Thomas Germe. (2019). DNA Topoisomerase Inhibitors: Trapping a DNA-Cleaving Machine in Motion. Journal of Molecular Biology. 431(18). 3427–3449. 83 indexed citations
7.
Velupillai, Srikannathasan, Alexandre Wohlkönig, Anthony Shillings, et al.. (2015). Crystallization and initial crystallographic analysis of covalent DNA-cleavage complexes of Staphyloccocus aureus DNA gyrase with QPT-1, moxifloxacin and etoposide. Acta Crystallographica Section F Structural Biology Communications. 71(10). 1242–1246. 16 indexed citations
8.
Agrawal, Alka, Mélanie Roué, Claus Spitzfaden, et al.. (2013). Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion. Biochemical Journal. 456(2). 263–273. 40 indexed citations
9.
Gentile, Gabriella, Alfonso Pozzan, Giovanni Bernasconi, et al.. (2012). 5-Aryl-4-carboxamide-1,3-oxazoles: Potent and selective GSK-3 inhibitors. Bioorganic & Medicinal Chemistry Letters. 22(5). 1989–1994. 39 indexed citations
10.
Smith, Kathrine J., Paul S. Carter, Angela Bridges, et al.. (2004). The Structure of MSK1 Reveals a Novel Autoinhibitory Conformation for a Dual Kinase Protein. Structure. 12(6). 1067–1077. 41 indexed citations
11.
Bax, B.D., Paul S. Carter, Ceri Lewis, et al.. (2001). The Structure of Phosphorylated GSK-3β Complexed with a Peptide, FRATtide, that Inhibits β-Catenin Phosphorylation. Structure. 9(12). 1143–1152. 172 indexed citations
12.
Culbert, Ainsley A., Murray J. B. Brown, Sheelagh Frame, et al.. (2001). GSK‐3 inhibition by adenoviral FRAT1 overexpression is neuroprotective and induces Tau dephosphorylation and β‐catenin stabilisation without elevation of glycogen synthase activity. FEBS Letters. 507(3). 288–294. 80 indexed citations
13.
Tisi, Dominic, B.D. Bax, & Andreas Loew. (2001). The three-dimensional structure of cytosolic bovine retinal creatine kinase. Acta Crystallographica Section D Biological Crystallography. 57(2). 187–193. 23 indexed citations
14.
Loew, Andreas & B.D. Bax. (1998). Purification, crystallization and preliminary crystallographic analysis of bovine cytosolic brain-type creatine kinase. Acta Crystallographica Section D Biological Crystallography. 54(5). 989–990. 1 indexed citations
15.
Srinivasan, Narayanaswamy, et al.. (1996). Structural aspects of the functional modules in human protein kinase-Cα deduced from comparative analyses. Proteins Structure Function and Bioinformatics. 26(2). 217–235. 30 indexed citations
16.
Greasley, S.E., Harren Jhoti, Carmel G. Teahan, et al.. (1995). The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nature Structural & Molecular Biology. 2(9). 797–806. 89 indexed citations
17.
Bax, B.D. & Harren Jhoti. (1995). Protein–Protein Interactions: Putting the pieces together. Current Biology. 5(10). 1119–1121. 6 indexed citations
18.
Nalini, V., B.D. Bax, H.P.C. Driessen, et al.. (1994). Close packing of an oligomeric eye lens β-crystallin induces loss of symmetry and ordering of sequence extensions. Journal of Molecular Biology. 236(4). 1250–1258. 46 indexed citations
19.
Lapatto, Risto, V. Nalini, B.D. Bax, et al.. (1991). High resolution structure of an oligomeric eye lens β-crystallin. Journal of Molecular Biology. 222(4). 1067–1083. 80 indexed citations
20.
Slingsby, C., H.P.C. Driessen, Daruka Mahadevan, B.D. Bax, & Tom L. Blundell. (1988). Evolutionary and functional relationships between the basic and acidic β-crystallins. Experimental Eye Research. 46(3). 375–403. 43 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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