A. Podjarny

6.1k total citations · 2 hit papers
132 papers, 5.1k citations indexed

About

A. Podjarny is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, A. Podjarny has authored 132 papers receiving a total of 5.1k indexed citations (citations by other indexed papers that have themselves been cited), including 86 papers in Molecular Biology, 49 papers in Materials Chemistry and 45 papers in Cell Biology. Recurrent topics in A. Podjarny's work include Enzyme Structure and Function (46 papers), Aldose Reductase and Taurine (45 papers) and Protein Structure and Dynamics (29 papers). A. Podjarny is often cited by papers focused on Enzyme Structure and Function (46 papers), Aldose Reductase and Taurine (45 papers) and Protein Structure and Dynamics (29 papers). A. Podjarny collaborates with scholars based in France, United States and Argentina. A. Podjarny's co-authors include A. Mitschler, Dino Moras, A. Cousido-Siah, Patrick Barth, Eduardo Howard, Matthew P. Blakeley, Francesc X. Ruiz, Isabelle Hazemann, B. Rees and Arnaud Poterszman and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

A. Podjarny

129 papers receiving 4.9k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Class II Aminoacyl Transfer Rna Synthetases: Crystal Structure of Yeast Aspartyl-trna Synthetase Complexed with tRNA ^Asp

1991 548 citations Arnaud Poterszman, A. Mitschler et al. profile →
Structure of the E6/E6AP/p53 complex required for HPV-mediated degradation of p53

2016 361 citations Francesc X. Ruiz, Juline Poirson et al. Nature profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
A. Podjarny France	35	3.2k	1.3k	1.2k	697	397	132	5.1k
A. Mitschler France	44	3.3k 1.0×	1.1k 0.9×	1.1k 0.9×	2.1k 3.1×	250 0.6×	120	7.3k
Joel Berendzen United States	26	6.5k 2.0×	2.3k 1.8×	2.2k 1.8×	308 0.4×	266 0.7×	41	8.9k
Yoshimasa Kyōgoku Japan	39	3.9k 1.2×	793 0.6×	793 0.6×	652 0.9×	149 0.4×	229	5.8k
Michael J. Sutcliffe United Kingdom	52	5.5k 1.7×	962 0.7×	1.3k 1.1×	705 1.0×	79 0.2×	169	8.3k
J. Kraut United States	44	6.3k 2.0×	1.4k 1.1×	2.2k 1.8×	809 1.2×	135 0.3×	82	9.2k
Maurice R. Eftink United States	33	5.3k 1.7×	851 0.7×	1.6k 1.3×	1.1k 1.6×	104 0.3×	99	7.5k
Dominique Bourgeois France	39	3.1k 1.0×	965 0.7×	1.6k 1.3×	202 0.3×	121 0.3×	116	5.1k
H.C. Watson United Kingdom	35	3.8k 1.2×	1.2k 1.0×	1.9k 1.5×	232 0.3×	229 0.6×	68	5.4k
Nei‐Li Chan United States	41	4.1k 1.3×	526 0.4×	563 0.5×	837 1.2×	64 0.2×	127	5.6k
Camillo A. Ghiron United States	21	3.4k 1.1×	629 0.5×	978 0.8×	652 0.9×	76 0.2×	64	4.7k

Countries citing papers authored by A. Podjarny

Since Specialization

Citations

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

Fields of papers citing papers by A. Podjarny

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A. Podjarny

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

Poirson, Juline, Marie‐Laure Straub, A. Cousido-Siah, et al.. (2022). High-Risk Mucosal Human Papillomavirus 16 (HPV16) E6 Protein and Cutaneous HPV5 and HPV8 E6 Proteins Employ Distinct Strategies To Interfere with Interferon Regulatory Factor 3-Mediated Beta Interferon Expression. Journal of Virology. 96(10). e0187521–e0187521. 18 indexed citations

Blakeley, Matthew P. & A. Podjarny. (2018). Neutron macromolecular crystallography. Emerging Topics in Life Sciences. 2(1). 39–55. 17 indexed citations

Noguera, Martín E., Ernesto A. Román, A. Cousido-Siah, et al.. (2015). Structural characterization of metal binding to a cold-adapted frataxin. JBIC Journal of Biological Inorganic Chemistry. 20(4). 653–664. 9 indexed citations

Giménez-Dejoz, Joan, Michal H. Kolář, Francesc X. Ruiz, et al.. (2015). Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase. PLoS ONE. 10(7). e0134506–e0134506. 23 indexed citations

Cousido-Siah, A., Francesc X. Ruiz, A. Mitschler, et al.. (2014). Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design. Acta Crystallographica Section D Biological Crystallography. 70(3). 889–903. 30 indexed citations

Cousido-Siah, A., Francesc X. Ruiz, Isidro Crespo, et al.. (2014). Structural analysis of sulindac as an inhibitor of aldose reductase and AKR1B10. Chemico-Biological Interactions. 234. 290–296. 22 indexed citations

Petrova, T., Vladimir Y. Lunin, Stephan L. Ginell, et al.. (2012). X-ray-induced overall structural changes in a protein molecule at cryogenic temperatures. Acta Crystallographica Section A Foundations of Crystallography. 68(a1). s266–s266. 2 indexed citations

Podjarny, A., Annick Dejaegere, & Bruno Kieffer. (2011). Biophysical approaches determining ligand binding to biomolecular targets : detection, measurement and modelling. 24 indexed citations

Petrova, T., Stephan L. Ginell, A. Mitschler, et al.. (2010). X-ray-induced deterioration of disulfide bridges at atomic resolution. Acta Crystallographica Section D Biological Crystallography. 66(10). 1075–1091. 18 indexed citations

10.

Guillot, Benoı̂t, Christian Jelsch, A. Podjarny, & Claude Lecomte. (2008). Charge-density analysis of a protein structure at subatomic resolution: the human aldose reductase case. Acta Crystallographica Section D Biological Crystallography. 64(5). 567–588. 50 indexed citations

11.

Hazemann, Isabelle, A. Cousido-Siah, A. Joachimiak, et al.. (2007). The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. Acta Crystallographica Section D Biological Crystallography. 63(6). 665–672. 12 indexed citations

12.

Hazemann, Isabelle, Marie-Thérèse Dauvergne, Matthew P. Blakeley, et al.. (2005). High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase. Acta Crystallographica Section D Biological Crystallography. 61(10). 1413–1417. 52 indexed citations

13.

Joachimiak, A., A. Podjarny, Raúl E. Cachau, T. Schneider, & M. Van Zandt. (2004). Subatomic and atomic crystallographic studies of aldose reductase: implications for inhibitor binding. Cellular and Molecular Life Sciences. 61(7-8). 763–773. 38 indexed citations

14.

Darmanin, Connie, Guillaume Chevreux, Noëlle Potier, et al.. (2004). Probing the ultra-high resolution structure of aldose reductase with molecular modelling and noncovalent mass spectrometry. Bioorganic & Medicinal Chemistry. 12(14). 3797–3806. 15 indexed citations

15.

Lunin, Vladimir Y., et al.. (2000). Low-resolution ab initio phasing: problems and advances. Acta Crystallographica Section D Biological Crystallography. 56(10). 1223–1232. 9 indexed citations

16.

Calderone, V., Bernard Chevrier, M. Van Zandt, et al.. (2000). The structure of human aldose reductase bound to the inhibitor IDD384. Acta Crystallographica Section D Biological Crystallography. 56(5). 536–540. 33 indexed citations

17.

Urzhumtsev, Alexandre, et al.. (2000). Density constraints and low-resolution phasing. Acta Crystallographica Section D Biological Crystallography. 56(10). 1233–1244. 3 indexed citations

18.

Lunin, Vladimir Y., et al.. (1995). On theab initiosolution of the phase problem for macromolecules at very low resolution: the few atoms model method. Acta Crystallographica Section D Biological Crystallography. 51(6). 896–903. 13 indexed citations

19.

Cura, Vincent, et al.. (1992). Heavy-atom refinement against solvent-flattened phases. Acta Crystallographica Section A Foundations of Crystallography. 48(5). 756–764. 11 indexed citations

20.

Dock‐Brégeon, Anne‐Catherine, Bernard Chevrier, A. Podjarny, et al.. (1988). High resolution structure of the RNA duplex [U(U-A)6A]2. Nature. 335(6188). 375–378. 69 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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