Martin H. Weik

13.2k total citations
112 papers, 5.2k citations indexed

About

Martin H. Weik is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, Martin H. Weik has authored 112 papers receiving a total of 5.2k indexed citations (citations by other indexed papers that have themselves been cited), including 72 papers in Molecular Biology, 44 papers in Materials Chemistry and 28 papers in Pharmacology. Recurrent topics in Martin H. Weik's work include Protein Structure and Dynamics (47 papers), Enzyme Structure and Function (41 papers) and Cholinesterase and Neurodegenerative Diseases (28 papers). Martin H. Weik is often cited by papers focused on Protein Structure and Dynamics (47 papers), Enzyme Structure and Function (41 papers) and Cholinesterase and Neurodegenerative Diseases (28 papers). Martin H. Weik collaborates with scholars based in France, United Kingdom and Germany. Martin H. Weik's co-authors include Giuseppe Zaccaı̈, Jacques‐Philippe Colletier, Joel L. Sussman, Israel Silman, Elspeth F. Garman, Frank Gabel, Ursula Lehnert, Kathleen Wood, Raimond B. G. Ravelli and Douglas J. Tobias and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Physical Review Letters.

In The Last Decade

Martin H. Weik

110 papers receiving 5.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Martin H. Weik France	42	3.0k	1.8k	870	779	581	112	5.2k
Raimond B. G. Ravelli Netherlands	47	5.2k 1.7×	2.1k 1.2×	722 0.8×	189 0.2×	446 0.8×	118	9.2k
Johan Wouters Belgium	50	2.7k 0.9×	1.9k 1.1×	883 1.0×	880 1.1×	262 0.5×	405	9.7k
Jacques‐Philippe Colletier France	38	2.5k 0.8×	737 0.4×	1.3k 1.5×	191 0.2×	933 1.6×	65	4.4k
G.N. Phillips United States	67	11.3k 3.8×	3.1k 1.8×	661 0.8×	1.2k 1.5×	332 0.6×	300	16.5k
Ilme Schlichting Germany	66	9.3k 3.1×	4.0k 2.3×	599 0.7×	470 0.6×	452 0.8×	174	14.8k
Eiki Yamashita Japan	45	8.5k 2.8×	1.1k 0.6×	511 0.6×	571 0.7×	199 0.3×	140	11.5k
Giuseppe Zaccaı̈ France	48	6.7k 2.2×	2.9k 1.7×	241 0.3×	2.0k 2.6×	184 0.3×	183	9.3k
Joel Berendzen United States	26	6.5k 2.1×	2.2k 1.3×	165 0.2×	1.0k 1.3×	203 0.3×	41	8.9k
Dagmar Ringe United States	69	10.5k 3.5×	4.7k 2.7×	479 0.6×	744 1.0×	779 1.3×	230	16.2k
Xiaolin Cheng United States	42	2.7k 0.9×	516 0.3×	258 0.3×	611 0.8×	251 0.4×	175	5.1k

Countries citing papers authored by Martin H. Weik

Since Specialization

Citations

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

Fields of papers citing papers by Martin H. Weik

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin H. Weik

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

Bódis, Eszter, Miklós Nyitrai, András Kengyel, et al.. (2024). ATP-dependent conformational dynamics in a photoactivated adenylate cyclase revealed by fluorescence spectroscopy and small-angle X-ray scattering. Communications Biology. 7(1). 147–147.

Garman, Elspeth F. & Martin H. Weik. (2023). Radiation damage to biological macromolecules∗. Current Opinion in Structural Biology. 82. 102662–102662. 25 indexed citations

Weik, Martin H. & Tatiana Domratcheva. (2022). Insight into the structural dynamics of light sensitive proteins from time-resolved crystallography and quantum chemical calculations. Current Opinion in Structural Biology. 77. 102496–102496. 3 indexed citations

Coquelle, Nicolas, Thomas R. M. Barends, Elke De Zitter, et al.. (2022). Time-resolved serial femtosecond crystallography on fatty-acid photodecarboxylase: lessons learned. Acta Crystallographica Section D Structural Biology. 78(9). 1131–1142. 9 indexed citations

Schirò, Giorgio, Yann Fichou, Alex P. S. Brogan, et al.. (2021). Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid. Physical Review Letters. 126(8). 88102–88102. 7 indexed citations

Mora, E. De la, Nicolas Coquelle, Charles S. Bury, et al.. (2020). Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures. Proceedings of the National Academy of Sciences. 117(8). 4142–4151. 88 indexed citations

Arcovito, Alessandro, S. Della Longa, Peter van der Linden, et al.. (2019). Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments. IUCrJ. 6(5). 832–842. 8 indexed citations

Schirò, Giorgio & Martin H. Weik. (2019). Role of hydration water in the onset of protein structural dynamics. Journal of Physics Condensed Matter. 31(46). 463002–463002. 40 indexed citations

Santoni, Gianluca, E. De la Mora, José Dias, et al.. (2018). Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited by Organophosphorus Nerve Agents. Journal of Medicinal Chemistry. 61(17). 7630–7639. 46 indexed citations

10.

Heyes, Derren J., Samantha J. O. Hardman, Martin Nors Pedersen, et al.. (2018). Light-induced structural changes in a full-length cyanobacterial phytochrome probed by time-resolved X-ray scattering. Communications Biology. 2(1). 1–1. 104 indexed citations

11.

Heyes, Derren J., Samantha J. O. Hardman, Michiyo Sakuma, et al.. (2018). Photochemical Mechanism of an Atypical Algal Phytochrome. ChemBioChem. 19(10). 1036–1043. 11 indexed citations

12.

Santoni, Gianluca, Delphine Karila, Cédric Lecoutey, et al.. (2018). Novel multitarget-directed ligands targeting acetylcholinesterase and σ1 receptors as lead compounds for treatment of Alzheimer's disease: Synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase. European Journal of Medicinal Chemistry. 162. 234–248. 39 indexed citations

13.

Zorbaz, Tamara, Julien Renou, Nikolina Maček Hrvat, et al.. (2018). Potent 3‐Hydroxy‐2‐Pyridine Aldoxime Reactivators of Organophosphate‐Inhibited Cholinesterases with Predicted Blood–Brain Barrier Penetration. Chemistry - A European Journal. 24(38). 9675–9691. 56 indexed citations

14.

Fichou, Yann, Giorgio Schirò, François‐Xavier Gallat, et al.. (2015). Hydration water mobility is enhanced around tau amyloid fibers. Proceedings of the National Academy of Sciences. 112(20). 6365–6370. 85 indexed citations

15.

Wood, Kathleen, François‐Xavier Gallat, Renee Otten, et al.. (2012). Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation. Angewandte Chemie International Edition. 52(2). 665–668. 29 indexed citations

16.

Xu, Yechun, Jacques‐Philippe Colletier, Martin H. Weik, et al.. (2010). Long Route or Shortcut? A Molecular Dynamics Study of Traffic of Thiocholine within the Active-Site Gorge of Acetylcholinesterase. Biophysical Journal. 99(12). 4003–4011. 33 indexed citations

17.

McGeehan, J.E., Raimond B. G. Ravelli, James W. Murray, et al.. (2009). Colouring cryo-cooled crystals: online microspectrophotometry. Journal of Synchrotron Radiation. 16(2). 163–172. 65 indexed citations

18.

Dekker, Carien, Bogos Agianian, Martin H. Weik, et al.. (2001). Biophysical Characterization of the Influence of Salt on Tetrameric SecB. Biophysical Journal. 81(1). 455–462. 2 indexed citations

19.

Weik, Martin H., Gitay Kryger, A.M.M. Schreurs, et al.. (2001). Solvent behaviour in flash-cooled protein crystals at cryogenic temperatures. Acta Crystallographica Section D Biological Crystallography. 57(4). 566–573. 46 indexed citations

20.

Lehnert, Ursula, Valérie Réat, Martin H. Weik, Giuseppe Zaccaı̈, & Claude Pfister. (1998). Thermal Motions in Bacteriorhodopsin at Different Hydration Levels Studied by Neutron Scattering: Correlation with Kinetics and Light-Induced Conformational Changes. Biophysical Journal. 75(4). 1945–1952. 130 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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