Olivier Marcillat

1.8k total citations · 1 hit paper
47 papers, 1.5k citations indexed

About

Olivier Marcillat is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Materials Chemistry. According to data from OpenAlex, Olivier Marcillat has authored 47 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 9 papers in Radiology, Nuclear Medicine and Imaging and 9 papers in Materials Chemistry. Recurrent topics in Olivier Marcillat's work include Enzyme Structure and Function (9 papers), Advanced MRI Techniques and Applications (9 papers) and Mitochondrial Function and Pathology (7 papers). Olivier Marcillat is often cited by papers focused on Enzyme Structure and Function (9 papers), Advanced MRI Techniques and Applications (9 papers) and Mitochondrial Function and Pathology (7 papers). Olivier Marcillat collaborates with scholars based in France, United States and Switzerland. Olivier Marcillat's co-authors include Kelvin J.A. Davies, Yong Zhang, Lars Ernster, Cecilia Giulivi, Christian Vial, Yong Zhang, Thierry Granjon, S W Lin, Eric Clottes and D. Eichenberger and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Biochemistry.

In The Last Decade

Olivier Marcillat

47 papers receiving 1.5k citations

Hit Papers

The oxidative inactivation of mitochondrial electron tran... 1990 2026 2002 2014 1990 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Olivier Marcillat France 16 1.1k 219 186 136 129 47 1.5k
Joanna Szczepanowska Poland 24 1.1k 1.0× 296 1.4× 221 1.2× 118 0.9× 68 0.5× 65 1.7k
Anca D. Petrescu United States 27 1.6k 1.5× 326 1.5× 304 1.6× 118 0.9× 130 1.0× 59 2.4k
Robert A. Farley United States 28 1.8k 1.7× 174 0.8× 182 1.0× 194 1.4× 62 0.5× 59 2.4k
Gary V. Richieri United States 22 1.5k 1.4× 356 1.6× 214 1.2× 83 0.6× 61 0.5× 30 2.1k
Eduardo N. Maldonado United States 26 1.5k 1.4× 205 0.9× 166 0.9× 146 1.1× 42 0.3× 55 2.2k
Michael Janes United States 14 1.0k 0.9× 292 1.3× 107 0.6× 93 0.7× 86 0.7× 21 1.8k
Elizabeth C. Ledgerwood New Zealand 24 2.0k 1.8× 399 1.8× 236 1.3× 125 0.9× 73 0.6× 50 2.9k
Thomas R. Hurd United States 22 1.7k 1.6× 385 1.8× 140 0.8× 120 0.9× 107 0.8× 31 2.4k
Shangyu Dang China 16 1.1k 1.0× 215 1.0× 131 0.7× 162 1.2× 117 0.9× 26 1.5k
Mauro Salvi Italy 31 2.3k 2.1× 257 1.2× 292 1.6× 206 1.5× 87 0.7× 94 3.1k

Countries citing papers authored by Olivier Marcillat

Since Specialization
Citations

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

Fields of papers citing papers by Olivier Marcillat

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Olivier Marcillat

This figure shows the co-authorship network connecting the top 25 collaborators of Olivier Marcillat. A scholar is included among the top collaborators of Olivier Marcillat 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 Olivier Marcillat. Olivier Marcillat 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.
Gadet, Rudy, Olivier Lohez, Ivan Mikaélian, et al.. (2024). The endoplasmic reticulum pool of Bcl-xL prevents cell death through IP3R-dependent calcium release. Cell Death Discovery. 10(1). 346–346. 5 indexed citations
2.
Dương, Minh Quang, Rudy Gadet, Isabelle Treilleux, et al.. (2023). Nrh L11R single nucleotide polymorphism, a new prediction biomarker in breast cancer, impacts endoplasmic reticulum-dependent Ca2+ traffic and response to neoadjuvant chemotherapy. Cell Death and Disease. 14(6). 392–392. 5 indexed citations
3.
Popgeorgiev, Nikolay, Loay Kassem, Soleilmane Omarjee, et al.. (2018). Breast Cancer Targeting through Inhibition of the Endoplasmic Reticulum-Based Apoptosis Regulator Nrh/BCL2L10. Cancer Research. 78(6). 1404–1417. 34 indexed citations
4.
Merceron, Romain, et al.. (2015). The Substrate-free and -bound Crystal Structures of the Duplicated Taurocyamine Kinase from the Human Parasite Schistosoma mansoni. Journal of Biological Chemistry. 290(20). 12951–12963. 8 indexed citations
5.
Maniti, Ofélia, Yi Jia, Jie Zhao, et al.. (2014). Carrier-inside-carrier: polyelectrolyte microcapsules as reservoir for drug-loaded liposomes. Journal of Liposome Research. 25(2). 122–130. 6 indexed citations
6.
Hologne, Maggy, et al.. (2012). Dynamical properties of the loop 320s of substrate‐free and substrate‐bound muscle creatine kinase by NMR. FEBS Journal. 279(16). 2863–2875. 2 indexed citations
7.
Maniti, Ofélia, M.F. Lecompte, Olivier Marcillat, et al.. (2011). Acyl chain composition determines cardiolipin clustering induced by mitochondrial creatine kinase binding to monolayers. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1808(4). 1129–1139. 12 indexed citations
8.
Barelier, Sarah, et al.. (2010). Fragment-Based Deconstruction of Bcl-x L Inhibitors. Journal of Medicinal Chemistry. 53(6). 2577–2588. 54 indexed citations
9.
Bandorowicz‐Pikuła, Joanna, René Buchet, F. Javier Cañada, et al.. (2010). Characterization of caged compounds binding to proteins by NMR spectroscopy. Biochemical and Biophysical Research Communications. 400(3). 447–451. 2 indexed citations
10.
Vernoux, Nathalie, Ofélia Maniti, Olivier Marcillat, Christian Vial, & Thierry Granjon. (2009). Mitochondrial creatine kinase interaction with heterogeneous monolayers: Effect on lipid lateral organization. Biochimie. 91(6). 752–764. 6 indexed citations
11.
Dissous, Colette, et al.. (2008). Crystallization and X-ray analysis of theSchistosoma mansoniguanidino kinase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(9). 854–857. 10 indexed citations
12.
Vernoux, Nathalie, Ofélia Maniti, Françoise Besson, et al.. (2007). Mitochondrial creatine kinase adsorption to biomimetic membranes: A Langmuir monolayer study. Journal of Colloid and Interface Science. 310(2). 436–445. 15 indexed citations
13.
Mazon, Hortense, et al.. (2006). Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer. Archives of Biochemistry and Biophysics. 458(2). 158–166. 7 indexed citations
14.
Mazon, Hortense, Olivier Marcillat, Éric Forest, & Christian Vial. (2005). Local dynamics measured by hydrogen/deuterium exchange and mass spectrometry of creatine kinase digested by two proteases. Biochimie. 87(12). 1101–1110. 13 indexed citations
15.
Mazon, Hortense, Olivier Marcillat, Éric Forest, & Christian Vial. (2005). Denaturant sensitive regions in creatine kinase identified by hydrogen/deuterium exchange. Rapid Communications in Mass Spectrometry. 19(11). 1461–1468. 4 indexed citations
16.
Mazon, Hortense, Olivier Marcillat, Éric Forest, & Christian Vial. (2004). Hydrogen/deuterium exchange studies of native rabbit MM‐CK dynamics. Protein Science. 13(2). 476–486. 4 indexed citations
17.
Marcillat, Olivier, et al.. (1999). Cloning, Escherichia coli Expression, and Phase-Transition Chromatography-Based Purification of Recombinant Rabbit Heart Mitochondrial Creatine Kinase. Protein Expression and Purification. 17(1). 163–168. 11 indexed citations
18.
Andersen, Jens, Éric Forest, Olivier Marcillat, et al.. (1997). Proteinase K Processing of Rabbit Muscle Creatine Kinase. Journal of Protein Chemistry. 16(1). 67–74. 11 indexed citations
19.
Clottes, Eric, et al.. (1997). Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: evidence for a multiple-step process. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1338(1). 37–46. 25 indexed citations
20.
Quéméneur, Éric, Olivier Marcillat, D. Eichenberger, & Christian Vial. (1989). Isoelectric point heterogeneity of the two oligomeric forms of heart mitochondrial creatine kinase.. PubMed. 18(2). 365–71. 3 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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