Vincent Dive

7.0k total citations
140 papers, 5.4k citations indexed

About

Vincent Dive is a scholar working on Molecular Biology, Oncology and Cancer Research. According to data from OpenAlex, Vincent Dive has authored 140 papers receiving a total of 5.4k indexed citations (citations by other indexed papers that have themselves been cited), including 79 papers in Molecular Biology, 67 papers in Oncology and 56 papers in Cancer Research. Recurrent topics in Vincent Dive's work include Peptidase Inhibition and Analysis (67 papers), Protease and Inhibitor Mechanisms (56 papers) and Chemical Synthesis and Analysis (36 papers). Vincent Dive is often cited by papers focused on Peptidase Inhibition and Analysis (67 papers), Protease and Inhibitor Mechanisms (56 papers) and Chemical Synthesis and Analysis (36 papers). Vincent Dive collaborates with scholars based in France, Greece and United Kingdom. Vincent Dive's co-authors include Athanasios Yiotakis, Dimitris Georgiadis, Fabrice Beau, Bertrand Czarny, Laurent Devel, Magdalini Matziari, Philippe Cuniasse, Philippe Cuniasse, Jöel Cotton and Jiřı́ Jiráček and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Vincent Dive

140 papers receiving 5.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Vincent Dive France 45 3.0k 1.9k 1.4k 1.1k 488 140 5.4k
Brion W. Murray United States 33 6.2k 2.1× 2.4k 1.2× 2.3k 1.6× 1.2k 1.1× 389 0.8× 63 9.8k
Isabel Marzo Spain 48 8.5k 2.9× 2.1k 1.1× 975 0.7× 998 0.9× 719 1.5× 109 11.7k
Pramod S. Pandey United States 43 5.3k 1.8× 1.2k 0.6× 617 0.4× 673 0.6× 237 0.5× 95 7.2k
Aviv Gazit Israel 45 5.3k 1.8× 3.3k 1.7× 913 0.6× 1.1k 1.0× 449 0.9× 99 9.7k
David A. Gewirtz United States 53 4.4k 1.5× 2.2k 1.1× 1.1k 0.7× 384 0.3× 149 0.3× 192 8.1k
Adrienne D. Cox United States 62 10.4k 3.5× 3.5k 1.8× 1.4k 0.9× 432 0.4× 468 1.0× 164 13.8k
Daniel C. Chan United States 42 3.0k 1.0× 1.6k 0.8× 622 0.4× 339 0.3× 414 0.8× 82 5.3k
Marco Falasca Australia 51 5.4k 1.8× 2.1k 1.1× 1.1k 0.8× 386 0.3× 356 0.7× 183 8.7k
Peter Störz United States 47 5.8k 2.0× 2.2k 1.1× 1.5k 1.0× 383 0.3× 256 0.5× 112 9.4k
Alexander J. Bridges United States 27 4.2k 1.4× 2.1k 1.1× 641 0.4× 2.0k 1.8× 401 0.8× 62 7.1k

Countries citing papers authored by Vincent Dive

Since Specialization
Citations

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

Fields of papers citing papers by Vincent Dive

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Vincent Dive

This figure shows the co-authorship network connecting the top 25 collaborators of Vincent Dive. A scholar is included among the top collaborators of Vincent Dive 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 Vincent Dive. Vincent Dive 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
2.
Kamińska, M., Carole Malgorn, Carole Fruchart‐Gaillard, et al.. (2021). Ligand‐Directed Modification of Active Matrix Metalloproteases: Activity‐based Probes with no Photolabile Group. Angewandte Chemie International Edition. 60(33). 18272–18279. 14 indexed citations
3.
Kamińska, M., Carole Malgorn, Carole Fruchart‐Gaillard, et al.. (2021). Ligand‐Directed Modification of Active Matrix Metalloproteases: Activity‐based Probes with no Photolabile Group. Angewandte Chemie. 133(33). 18420–18427. 1 indexed citations
4.
Malgorn, Carole, Dominique Georgin, Antoine Sallustrau, et al.. (2020). Development of a Mass Spectrometry Imaging Method for Detecting and Mapping Graphene Oxide Nanoparticles in Rodent Tissues. Journal of the American Society for Mass Spectrometry. 31(5). 1025–1036. 8 indexed citations
5.
Vera, Laura, et al.. (2014). Halogen Bonding Controls Selectivity of FRET Substrate Probes for MMP-9. Chemistry & Biology. 21(3). 408–413. 25 indexed citations
6.
Goff, Sandrine Vadon‐Le, Frédéric Delolme, Jean‐Marie Bourhis, et al.. (2012). Sizzled Is Unique among Secreted Frizzled-related Proteins for Its Ability to Specifically Inhibit Bone Morphogenetic Protein-1 (BMP-1)/Tolloid-like Proteinases. Journal of Biological Chemistry. 287(40). 33581–33593. 25 indexed citations
7.
Devel, Laurent, Bertrand Czarny, Fabrice Beau, et al.. (2010). Third generation of matrix metalloprotease inhibitors: Gain in selectivity by targeting the depth of the S1′ cavity. Biochimie. 92(11). 1501–1508. 75 indexed citations
8.
Akif, Mohd, Dimitris Georgiadis, Aman Mahajan, et al.. (2010). High-Resolution Crystal Structures of Drosophila melanogaster Angiotensin-Converting Enzyme in Complex with Novel Inhibitors and Antihypertensive Drugs. Journal of Molecular Biology. 400(3). 502–517. 68 indexed citations
9.
Troeberg, Linda, Kazunari Fushimi, Simone Dario Scilabra, et al.. (2009). The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3. Matrix Biology. 28(8). 463–469. 54 indexed citations
10.
Tremblay, Évelyne, Oualid Sbai, Lotfi Ferhat, et al.. (2009). A New Role for TIMP-1 in Modulating Neurite Outgrowth and Morphology of Cortical Neurons. PLoS ONE. 4(12). e8289–e8289. 52 indexed citations
11.
Pallafacchina, Giorgia, Stéphanie François, Béatrice Regnault, et al.. (2009). An adult tissue-specific stem cell in its niche: A gene profiling analysis of in vivo quiescent and activated muscle satellite cells. Stem Cell Research. 4(2). 77–91. 218 indexed citations
12.
Bourenkow, G., H.D. Bartunik, Henning Scholze, et al.. (2002). Crystal Structure of the Dinuclear Zinc Aminopeptidase PepV from Lactobacillus delbrueckii Unravels Its Preference for Dipeptides. Structure. 10(8). 1097–1106. 66 indexed citations
13.
Cotton, Jöel, et al.. (2001). Potency and selectivity of RXP407 on human, rat, and mouse angiotensin-converting enzyme. Biochemical Pharmacology. 61(7). 835–841. 18 indexed citations
14.
Gall, Andrew, Marc Ruff, Vincent Dive, et al.. (2000). Crystal structure of the Stromelysin-3 complexed with a phosphinic inhibitor reveals that its S1′ pocket is a deep opened cavity. Acta Crystallographica Section A Foundations of Crystallography. 56(s1). s440–s440. 1 indexed citations
15.
Vincent, Bruno, Jiřı́ Jiráček, Florence Noble, et al.. (1997). Contribution of endopeptidase 3.4.24.15 to central neurotensin inactivation. European Journal of Pharmacology. 334(1). 49–53. 32 indexed citations
16.
Checler, Frédéric, Hélène Barelli, Pascale Dauch, et al.. (1995). [36] Neurolysin: Purification and assays. Methods in enzymology on CD-ROM/Methods in enzymology. 593–614. 29 indexed citations
18.
Barelli, Hélène, J.E.T. Fox‐Threlkeld, Vincent Dive, et al.. (1994). Role of endopeptidase 3.4.24.16 in the catabolism of neurotensin,in vivo, in the vascularly perfused dog ileum. British Journal of Pharmacology. 112(1). 127–132. 42 indexed citations
19.
Yiotakis, Athanasios, Alain Lecoq, Stamatia Vassiliou, et al.. (1994). Cyclic Peptides with a Phosphinic Bond as Potent Inhibitors of a Zinc Bacterial Collagenase. Journal of Medicinal Chemistry. 37(17). 2713–2720. 21 indexed citations
20.
Dive, Vincent, Adolfo Lai, Gianni Valensin, et al.. (1991). Proton and tritium nmr relaxation studies of peptide inhibitor binding to bacterial collagenase: Conformation and dynamics. Biopolymers. 31(3). 305–317. 11 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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