Martin Blackledge

19.4k total citations · 1 hit paper
253 papers, 14.6k citations indexed

About

Martin Blackledge is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Martin Blackledge has authored 253 papers receiving a total of 14.6k indexed citations (citations by other indexed papers that have themselves been cited), including 176 papers in Molecular Biology, 95 papers in Spectroscopy and 65 papers in Materials Chemistry. Recurrent topics in Martin Blackledge's work include Protein Structure and Dynamics (125 papers), Advanced NMR Techniques and Applications (64 papers) and Enzyme Structure and Function (62 papers). Martin Blackledge is often cited by papers focused on Protein Structure and Dynamics (125 papers), Advanced NMR Techniques and Applications (64 papers) and Enzyme Structure and Function (62 papers). Martin Blackledge collaborates with scholars based in France, Germany and United Kingdom. Martin Blackledge's co-authors include Malene Ringkjøbing Jensen, Pau Bernadó, Dominique Marion, Markus Zweckstetter, Rob W. H. Ruigrok, Dmitri I. Svergun, Efstratios Mylonas, Loïc Salmon, Phineus R. L. Markwick and Guillaume Bouvignies and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Martin Blackledge

251 papers receiving 14.5k citations

Hit Papers

Structural Characterization of Flexible Proteins Using Sm... 2007 2026 2013 2019 2007 250 500 750
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.

  1. Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering
    2007 960 citations Pau Bernadó, Martin Blackledge et al. Journal of the American Chemical Society profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Martin Blackledge France 66 10.9k 4.4k 4.0k 1.2k 1.1k 253 14.6k
Geerten W. Vuister Netherlands 46 15.8k 1.5× 3.8k 0.9× 3.0k 0.7× 2.0k 1.7× 698 0.6× 120 20.2k
Nico Tjandra United States 54 11.1k 1.0× 3.0k 0.7× 3.9k 1.0× 1.0k 0.8× 591 0.5× 172 14.1k
Peter Güntert Germany 59 14.1k 1.3× 3.8k 0.9× 2.9k 0.7× 1.4k 1.1× 612 0.6× 237 17.9k
Guang Zhu Hong Kong 32 13.7k 1.3× 3.1k 0.7× 2.3k 0.6× 1.9k 1.6× 653 0.6× 125 18.4k
Frank Delaglio United States 30 19.3k 1.8× 4.7k 1.1× 4.2k 1.1× 2.3k 1.9× 880 0.8× 61 24.8k
Julie D. Forman‐Kay Canada 77 18.7k 1.7× 4.9k 1.1× 2.8k 0.7× 2.2k 1.8× 439 0.4× 218 21.8k
Stephan Grzesiek Switzerland 66 22.5k 2.1× 6.0k 1.4× 6.0k 1.5× 2.6k 2.2× 1.0k 0.9× 171 29.5k
Hartmut Oschkinat Germany 63 7.7k 0.7× 4.1k 0.9× 6.1k 1.5× 1.3k 1.0× 296 0.3× 280 14.3k
Rolf Boelens Netherlands 64 13.2k 1.2× 2.6k 0.6× 2.3k 0.6× 883 0.7× 387 0.4× 318 17.1k
Robert Kaptein Netherlands 64 14.1k 1.3× 3.8k 0.9× 4.0k 1.0× 890 0.7× 420 0.4× 347 20.1k

Countries citing papers authored by Martin Blackledge

Since Specialization
Citations

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

Fields of papers citing papers by Martin Blackledge

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Martin Blackledge. 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 Martin Blackledge. The network helps show where Martin Blackledge may publish in the future.

Co-authorship network of co-authors of Martin Blackledge

This figure shows the co-authorship network connecting the top 25 collaborators of Martin Blackledge. A scholar is included among the top collaborators of Martin Blackledge 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 Martin Blackledge. Martin Blackledge 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.
Li, Xiaohan, C. Yu, Natalia Gómez‐Navarro, et al.. (2023). Dynamic conformational changes of a tardigrade group-3 late embryogenesis abundant protein modulate membrane biophysical properties. PNAS Nexus. 3(1). pgae006–pgae006. 3 indexed citations
2.
Bottaro, Sandro, Robbin Schnieders, Hendrik R. A. Jonker, et al.. (2023). Integrated NMR/Molecular Dynamics Determination of the Ensemble Conformation of a Thermodynamically Stable CUUG RNA Tetraloop. Journal of the American Chemical Society. 145(30). 16557–16572. 16 indexed citations
3.
Camacho‐Zarco, Aldo R., Damien Maurin, Guillaume Bouvignies, et al.. (2023). Multivalent Dynamic Colocalization of Avian Influenza Polymerase and Nucleoprotein by Intrinsically Disordered ANP32A Reveals the Molecular Basis of Human Adaptation. Journal of the American Chemical Society. 145(38). 20985–21001. 6 indexed citations
4.
Gari, Raghavendar Reddy Sanganna, Ruth A. Pumroy, Yining Jiang, et al.. (2023). Intrinsically disordered regions in TRPV2 mediate protein-protein interactions. Communications Biology. 6(1). 966–966. 4 indexed citations
5.
Abyzov, Anton, Martin Blackledge, & Markus Zweckstetter. (2022). Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry. Chemical Reviews. 122(6). 6719–6748. 108 indexed citations
6.
Ibrahim, Ziad, Tao Wang, Olivier Destaing, et al.. (2022). Structural insights into p300 regulation and acetylation-dependent genome organisation. Nature Communications. 13(1). 7759–7759. 34 indexed citations
7.
Bessa, Luiza M., Serafima Guseva, Aldo R. Camacho‐Zarco, et al.. (2022). The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a. Science Advances. 8(3). eabm4034–eabm4034. 59 indexed citations
8.
9.
Salvi, Nicola, Luiza M. Bessa, Serafima Guseva, et al.. (2021). 1H, 13C and 15N backbone chemical shift assignments of SARS-CoV-2 nsp3a. Biomolecular NMR Assignments. 15(1). 173–176. 4 indexed citations
10.
Guseva, Serafima, Sigrid Milles, Malene Ringkjøbing Jensen, et al.. (2020). Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. Science Advances. 6(14). eaaz7095–eaaz7095. 135 indexed citations
11.
Rasmussen, Kim Krighaar, Andrés Palencia, Elisabetta Boeri Erba, et al.. (2020). Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage. Proceedings of the National Academy of Sciences. 117(34). 20576–20585. 7 indexed citations
12.
Camacho‐Zarco, Aldo R., Sissy Kalayil, Damien Maurin, et al.. (2020). Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A. Nature Communications. 11(1). 40 indexed citations
13.
Salvi, Nicola, Anton Abyzov, & Martin Blackledge. (2019). Solvent-dependent segmental dynamics in intrinsically disordered proteins. Science Advances. 5(6). eaax2348–eaax2348. 43 indexed citations
14.
Yarava, Jayasubba Reddy, Albert Hofstetter, Nicola Salvi, et al.. (2018). Probing Protein Dynamics Using Multifield Variable Temperature NMR Relaxation and Molecular Dynamics Simulation. The Journal of Physical Chemistry B. 122(42). 9697–9702. 16 indexed citations
15.
Delaforge, Elise, Jaka Kragelj, Andrés Palencia, et al.. (2017). Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy. Journal of the American Chemical Society. 140(3). 1148–1158. 60 indexed citations
16.
Salvi, Nicola, Loïc Salmon, & Martin Blackledge. (2017). Dynamic Descriptions of Highly Flexible Molecules from NMR Dipolar Couplings: Physical Basis and Limitations. Journal of the American Chemical Society. 139(14). 5011–5014. 9 indexed citations
17.
Lewandowski, Józef R., Meghan E. Halse, Martin Blackledge, & Lyndon Emsley. (2015). Direct observation of hierarchical protein dynamics. Science. 348(6234). 578–581. 215 indexed citations
18.
Schneider, Robert C., Jie‐rong Huang, Mingxi Yao, et al.. (2011). Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy. Molecular BioSystems. 8(1). 58–68. 88 indexed citations
19.
Bernadó, Pau, Laurence Blanchard, Peter Timmins, et al.. (2005). A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. Proceedings of the National Academy of Sciences. 102(47). 17002–17007. 354 indexed citations
20.
Bouvignies, Guillaume, Pau Bernadó, Sebastián Meier, et al.. (2005). Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings. Proceedings of the National Academy of Sciences. 102(39). 13885–13890. 202 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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