Marcel Waks

1.8k total citations
59 papers, 1.6k citations indexed

About

Marcel Waks is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Marcel Waks has authored 59 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 27 papers in Cell Biology and 20 papers in Organic Chemistry. Recurrent topics in Marcel Waks's work include Hemoglobin structure and function (27 papers), Surfactants and Colloidal Systems (20 papers) and Neonatal Health and Biochemistry (13 papers). Marcel Waks is often cited by papers focused on Hemoglobin structure and function (27 papers), Surfactants and Colloidal Systems (20 papers) and Neonatal Health and Biochemistry (13 papers). Marcel Waks collaborates with scholars based in France, United States and Canada. Marcel Waks's co-authors include W. Urbach, Sherman Beychok, C. Nicot, Y K Yip, M. Gindre, J.Y. Le Huérou, Annette Alfsen, Monique Vacher, Nicolas Taulier and Massimo Marchi 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

Marcel Waks

58 papers receiving 1.5k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Marcel Waks 862 512 495 266 227 59 1.6k
Jacinto Steinhardt 1.3k 1.5× 337 0.7× 722 1.5× 141 0.5× 159 0.7× 52 2.0k
Thomas C. Strekas 1.1k 1.2× 573 1.1× 594 1.2× 289 1.1× 117 0.5× 45 2.6k
Hideo Kon 579 0.7× 196 0.4× 428 0.9× 140 0.5× 70 0.3× 78 1.8k
Gurusamy Balakrishnan 784 0.9× 158 0.3× 336 0.7× 315 1.2× 70 0.3× 58 1.7k
G. Blauer 981 1.1× 231 0.5× 435 0.9× 59 0.2× 459 2.0× 63 1.7k
L. Powers 1.3k 1.6× 146 0.3× 605 1.2× 222 0.8× 56 0.2× 72 2.3k
Leslie W.‐M. Fung 712 0.8× 176 0.3× 555 1.1× 79 0.3× 179 0.8× 65 1.4k
Hidetake Imasato 942 1.1× 298 0.6× 283 0.6× 88 0.3× 55 0.2× 52 1.6k
D. H. Irvine 572 0.7× 139 0.3× 702 1.4× 90 0.3× 192 0.8× 58 1.5k
W. N. Lipscomb 832 1.0× 404 0.8× 223 0.5× 78 0.3× 90 0.4× 60 1.8k

Countries citing papers authored by Marcel Waks

Since Specialization
Citations

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

Fields of papers citing papers by Marcel Waks

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Marcel Waks

This figure shows the co-authorship network connecting the top 25 collaborators of Marcel Waks. A scholar is included among the top collaborators of Marcel Waks 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 Marcel Waks. Marcel Waks 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.
Abel, Stéphane, Marcel Waks, & Massimo Marchi. (2010). Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps. The European Physical Journal E. 32(4). 399–409. 33 indexed citations
2.
Taulier, Nicolas, et al.. (2007). Molecular Origin of Model Membrane Bending Rigidity. Physical Review Letters. 98(25). 258103–258103. 27 indexed citations
3.
Taulier, Nicolas, J.Y. Le Huérou, M. Gindre, et al.. (2006). Unfolding and Refolding of Bovine Serum Albumin at Acid pH: Ultrasound and Structural Studies. Biophysical Journal. 91(9). 3397–3404. 177 indexed citations
4.
Abel, Stéphane, Marcel Waks, W. Urbach, & Massimo Marchi. (2005). Structure, Stability, and Hydration of a Polypeptide in AOT Reverse Micelles. Journal of the American Chemical Society. 128(2). 382–383. 41 indexed citations
5.
Kanjilal, Sanjit, Nicolas Taulier, J.Y. Le Huérou, et al.. (2003). Ultrasonic Studies of Alcohol-Induced Transconformation in β-Lactoglobulin: The Intermediate State. Biophysical Journal. 85(6). 3928–3934. 14 indexed citations
6.
Huérou, J.Y. Le, et al.. (2001). Hydration and Protein Folding in Water and in Reverse Micelles: Compressibility and Volume Changes. Biophysical Journal. 80(6). 2751–2760. 44 indexed citations
7.
Taulier, Nicolas, C. Nicot, Marcel Waks, et al.. (2000). Unbinding–Binding Transition Induced by Molecular Snaps in Model Membranes. Biophysical Journal. 78(2). 857–865. 13 indexed citations
8.
Nicot, C. & Marcel Waks. (1996). Proteins as Invited Guests of Reverse Micelles: Conformational Effects, Significance, Applications. Biotechnology and Genetic Engineering Reviews. 13(1). 267–314. 25 indexed citations
9.
Nicot, C., et al.. (1993). Limited Proteolysis of Myelin Basic Protein in a System Mimetic of the Myelin Interlamellar Aqueous Space. Journal of Neurochemistry. 60(4). 1283–1291. 10 indexed citations
11.
Desfosses, Bernard, C. Nicot, & Marcel Waks. (1992). A drug release-facilitating mechanism for human serum albumin in reverse micelles: requirement of a structural switch.. PubMed. 26(2). 257–64. 5 indexed citations
12.
Desfosses, Bernard, N. Cittanova, W. Urbach, & Marcel Waks. (1991). Ligand binding at membrane mimetic interfaces. European Journal of Biochemistry. 199(1). 79–87. 22 indexed citations
13.
Kahn, Peter C., et al.. (1990). “Hydration memory” of lysozyme: A misinterpretation. Biochemical and Biophysical Research Communications. 166(2). 1039–1046. 1 indexed citations
14.
Vacher, Monique, Marcel Waks, & C. Nicot. (1989). Myelin Proteins in Reverse Micelles: Tight Lipid Association Required for Insertion of the Folch‐Pi Proteolipid into a Membrane‐Mimetic System. Journal of Neurochemistry. 52(1). 117–123. 15 indexed citations
15.
Binks, B. P., D. Chatenay, C. Nicot, W. Urbach, & Marcel Waks. (1989). Structural parameters of the myelin transmembrane proteolipid in reverse micelles. Biophysical Journal. 55(5). 949–955. 20 indexed citations
16.
Gallay, Jacques, Michel Vincent, C. Nicot, & Marcel Waks. (1987). Conformational aspects and rotational dynamics of synthetic adrenocorticotropin-(1-24) and glucagon in reverse micelles. Biochemistry. 26(18). 5738–5747. 29 indexed citations
17.
Waks, Marcel. (1986). Proteins and peptides in water‐restricted environments. Proteins Structure Function and Bioinformatics. 1(1). 4–15. 126 indexed citations
18.
Vacher, Monique, et al.. (1984). Solubilization and insertion into reverse micelles of the major myelin transmembrane proteolipid. FEBS Letters. 172(2). 343–347. 26 indexed citations
19.
Lombart, Christian, et al.. (1979). Identification of haptoglobin in chicken serum and specificity of the chicken haptoglobin-hemoglobin complex formation. Comparative Biochemistry and Physiology Part B Comparative Biochemistry. 62(3). 241–244. 7 indexed citations
20.
Engler, R, et al.. (1977). Determination immunochimique de l'hemoglobine humaine dans les liquides biologiques. Clinica Chimica Acta. 77(2). 159–165. 7 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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