Michel Juy

1.2k total citations
23 papers, 957 citations indexed

About

Michel Juy is a scholar working on Molecular Biology, Biotechnology and Materials Chemistry. According to data from OpenAlex, Michel Juy has authored 23 papers receiving a total of 957 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 10 papers in Biotechnology and 8 papers in Materials Chemistry. Recurrent topics in Michel Juy's work include Enzyme Production and Characterization (10 papers), Enzyme Structure and Function (8 papers) and Biofuel production and bioconversion (6 papers). Michel Juy is often cited by papers focused on Enzyme Production and Characterization (10 papers), Enzyme Structure and Function (8 papers) and Biofuel production and bioconversion (6 papers). Michel Juy collaborates with scholars based in France, Tunisia and Czechia. Michel Juy's co-authors include Richard Haser, Pierre Béguin, Pedro M. Alzari, Samír Béjar, N. Aghajari, Jean-Paul Aubert, Marc Claeyssens, Anja Böckmann, François Penin and Anne Galinier and has published in prestigious journals such as Nature, Nature Biotechnology and Journal of Molecular Biology.

In The Last Decade

Michel Juy

23 papers receiving 931 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Michel Juy France 17 486 361 242 217 202 23 957
Manish D. Joshi Canada 10 640 1.3× 374 1.0× 315 1.3× 38 0.2× 141 0.7× 11 874
Jan Dohnálek Czechia 20 663 1.4× 188 0.5× 68 0.3× 47 0.2× 197 1.0× 73 1.1k
Olivier Saurel France 19 615 1.3× 55 0.2× 83 0.3× 119 0.5× 54 0.3× 43 983
Serge Pérez France 15 302 0.6× 97 0.3× 37 0.2× 71 0.3× 88 0.4× 19 899
J. Krucinski United States 6 1.1k 2.3× 59 0.2× 208 0.9× 45 0.2× 69 0.3× 6 1.4k
Krisztina Fehér Hungary 19 512 1.1× 24 0.1× 83 0.3× 138 0.6× 71 0.4× 44 946
Stéphanie Ravaud France 16 522 1.1× 137 0.4× 82 0.3× 60 0.3× 122 0.6× 34 752
Leigh A. Plesniak United States 13 394 0.8× 122 0.3× 76 0.3× 52 0.2× 77 0.4× 18 501
Joan F Back Australia 8 485 1.0× 84 0.2× 84 0.3× 77 0.4× 115 0.6× 8 902
Guewha Steven Huang Taiwan 14 532 1.1× 34 0.1× 132 0.5× 77 0.4× 371 1.8× 23 990

Countries citing papers authored by Michel Juy

Since Specialization
Citations

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

Fields of papers citing papers by Michel Juy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Michel Juy

This figure shows the co-authorship network connecting the top 25 collaborators of Michel Juy. A scholar is included among the top collaborators of Michel Juy 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 Michel Juy. Michel Juy 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.
Mabrouk, Sameh, N. Aghajari, Mamdouh Ben Ali, et al.. (2010). Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions. Bioresource Technology. 102(2). 1740–1746. 36 indexed citations
2.
Rhimi, Moez, N. Aghajari, Michel Juy, et al.. (2009). Rational design of Bacillus stearothermophilus US100 l-arabinose isomerase: Potential applications for d-tagatose production. Biochimie. 91(5). 650–653. 46 indexed citations
3.
Khemakhem, Bassem, Mamdouh Ben Ali, N. Aghajari, et al.. (2009). The importance of an extra loop in the B-domain of an α-amylase from B. stearothermophilus US100. Biochemical and Biophysical Research Communications. 385(1). 78–83. 21 indexed citations
4.
Rhimi, Moez, N. Aghajari, Bassem Jaouadi, et al.. (2009). Exploring the acidotolerance of β-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus: an attractive enzyme for lactose bioconversion. Research in Microbiology. 160(10). 775–784. 26 indexed citations
5.
Borgi, Mohamed Ali, Moez Rhimi, N. Aghajari, et al.. (2009). Involvement of cysteine 306 and alanine 63 in the thermostability and oligomeric organization of glucose isomerase from Streptomyces sp. SK. Biologia. 64(5). 845–851. 6 indexed citations
6.
Khemakhem, Bassem, Mamdouh Ben Ali, N. Aghajari, et al.. (2008). Engineering of the α‐amylase from Geobacillus stearothermophilus US100 for detergent incorporation. Biotechnology and Bioengineering. 102(2). 380–389. 43 indexed citations
7.
Böckmann, Anja, Michel Juy, E. Bettler, et al.. (2005). Water–Protein Hydrogen Exchange in the Micro-Crystalline Protein Crh as Observed by Solid State NMR Spectroscopy. Journal of Biomolecular NMR. 32(3). 195–207. 45 indexed citations
8.
Böckmann, Anja, Adam Lange, Anne Galinier, et al.. (2003). Solid state NMR sequential resonance assignments and conformational analysis of the 2×10.4 kDa dimeric form of the Bacillus subtilis protein Crh. Journal of Biomolecular NMR. 27(4). 323–339. 147 indexed citations
9.
Juy, Michel, François Penin, Adrien Favier, et al.. (2003). Dimerization of Crh by Reversible 3D Domain Swapping Induces Structural Adjustments to its Monomeric Homologue Hpr. Journal of Molecular Biology. 332(4). 767–776. 25 indexed citations
10.
Chapon, Virginie, Mirjam Czjzek, Mohammed El Hassouni, et al.. (2001). Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase cel5 (formerly EGZ) from Erwinia chrysanthemi 1 1Edited by I. B. Holland. Journal of Molecular Biology. 310(5). 1055–1066. 50 indexed citations
11.
Reverbel-Leroy, C., Goetz Parsiegla, Vincent Moreau, et al.. (1998). Crystallization of the catalytic domain of Clostridium cellulolyticum CeIF cellulase in the presence of a newly synthesized cellulase inhibitor. Acta Crystallographica Section D Biological Crystallography. 54(1). 114–118. 19 indexed citations
12.
André, Gwénaëlle, Alain Buléon, V.H. Tran, et al.. (1998). Amylose chain behavior in an interacting context I. Influence of a nonchair ring on the maltose conformations. Biopolymers. 39(5). 737–751. 8 indexed citations
13.
Vallée, François, Anders Kadziola, Yves Bourne, et al.. (1998). Barley α-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 å resolution. Structure. 6(5). 649–659. 112 indexed citations
14.
Chitarra, V., et al.. (1995). Multiple crystal forms of endoglucanase CelD: Signal peptide residues modulate lattice formation. Journal of Molecular Biology. 248(2). 225–232. 8 indexed citations
15.
Juy, Michel, et al.. (1992). Three-dimensional structure of a thermostable bacterial cellulase. Nature. 357(6373). 89–91. 186 indexed citations
16.
Fermandjian, Serge, et al.. (1983). The key role of residue 5 in angiotensin II. Biopolymers. 22(1). 227–231. 18 indexed citations
17.
Juy, Michel, Hung Lamthanh, Karl Lintner, & Serge Fermandjian. (1983). Conformation and mobility of tyrosine side chain in tetrapeptides: Specific effects of cis‐ and trans ‐proline in Tyr‐Pro‐ and Pro‐Tyr‐segments. International journal of peptide & protein research. 22(4). 437–449. 21 indexed citations
18.
Juy, Michel, Hung Lamthanh, & Serge Fermandjian. (1982). CD and 1 H‐n.m.r. studies on the side‐chain conformation of tyrosine derivatives and tyrosine residues in di‐ and tripeptides. International journal of peptide & protein research. 20(4). 298–307. 9 indexed citations
19.
Vičar, Jaroslav, K. Bláha, François Piriou, et al.. (1982). Conformational studies of diastereoisomeric cyclo(alanyl‐phenylalanyl) with the coupling constants 1H–1H, 15N–1H, 13C–1H, and 13C–15N. Biopolymers. 21(12). 2317–2328. 9 indexed citations
20.
Lamthanh, Hung, Michel Juy, Christian Schneider, Serge Fermandjian, & P. Fromageot. (1981). Correlated circular dichroism, magnetic circular dichroism and high performance liquid chromatography studies of "palladium (II) — thioether peptides" complexes. Journal de Chimie Physique. 78. 695–701. 2 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Manish D. Joshi Breakdown of academic impact, for papers by Jan Dohnálek Breakdown of academic impact, for papers by Olivier Saurel Breakdown of academic impact, for papers by Serge Pérez Breakdown of academic impact, for papers by J. Krucinski Breakdown of academic impact, for papers by Krisztina Fehér Breakdown of academic impact, for papers by Stéphanie Ravaud Breakdown of academic impact, for papers by Leigh A. Plesniak Breakdown of academic impact, for papers by Joan F Back Breakdown of academic impact, for papers by Guewha Steven Huang
Rankless by CCL
2026