J.L. Schlessman

2.1k total citations
29 papers, 1.7k citations indexed

About

J.L. Schlessman is a scholar working on Molecular Biology, Cell Biology and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, J.L. Schlessman has authored 29 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 6 papers in Cell Biology and 5 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in J.L. Schlessman's work include Protein Structure and Dynamics (13 papers), DNA and Nucleic Acid Chemistry (9 papers) and Photosynthetic Processes and Mechanisms (8 papers). J.L. Schlessman is often cited by papers focused on Protein Structure and Dynamics (13 papers), DNA and Nucleic Acid Chemistry (9 papers) and Photosynthetic Processes and Mechanisms (8 papers). J.L. Schlessman collaborates with scholars based in United States, Sweden and France. J.L. Schlessman's co-authors include Bertrand García‐Moreno E., Douglas C. Rees, James B. Howard, Hermann Schindelin, Caroline Kisker, Michael J. Harms, Carlos A. Castañeda, Angel E. Garcı́a, Bertrand García‐Moreno and Carolyn A. Fitch and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

J.L. Schlessman

28 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J.L. Schlessman United States 17 1.2k 410 393 189 164 29 1.7k
Boris Dzikovski United States 22 705 0.6× 437 1.1× 266 0.7× 196 1.0× 124 0.8× 49 1.5k
Françoise Guerlesquin France 31 1.6k 1.3× 315 0.8× 392 1.0× 198 1.0× 197 1.2× 97 2.3k
Ronald A. Venters United States 23 1.0k 0.9× 464 1.1× 154 0.4× 70 0.4× 100 0.6× 36 1.6k
Ishita Mukerji United States 25 1.4k 1.2× 298 0.7× 136 0.3× 309 1.6× 342 2.1× 70 1.9k
Yun Xiang China 9 954 0.8× 324 0.8× 70 0.2× 173 0.9× 115 0.7× 11 1.5k
S. Turley United States 27 1.7k 1.4× 486 1.2× 450 1.1× 30 0.2× 500 3.0× 43 2.9k
Liliya A. Yatsunyk United States 29 2.0k 1.7× 547 1.3× 99 0.3× 57 0.3× 401 2.4× 58 3.0k
Nozomi Ando United States 24 976 0.8× 536 1.3× 141 0.4× 92 0.5× 283 1.7× 62 1.6k
A.W. Roszak United Kingdom 25 1.4k 1.2× 445 1.1× 188 0.5× 370 2.0× 143 0.9× 71 2.1k
Qin Zou China 17 623 0.5× 620 1.5× 91 0.2× 130 0.7× 39 0.2× 30 1.5k

Countries citing papers authored by J.L. Schlessman

Since Specialization
Citations

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

Fields of papers citing papers by J.L. Schlessman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.L. Schlessman. 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 J.L. Schlessman. The network helps show where J.L. Schlessman may publish in the future.

Co-authorship network of co-authors of J.L. Schlessman

This figure shows the co-authorship network connecting the top 25 collaborators of J.L. Schlessman. A scholar is included among the top collaborators of J.L. Schlessman 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 J.L. Schlessman. J.L. Schlessman 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.
Schlessman, J.L., et al.. (2025). Extremophilic hemoglobins: The structure of Shewanella benthica truncated hemoglobin N. Journal of Biological Chemistry. 301(3). 108223–108223. 2 indexed citations
2.
Schlessman, J.L., et al.. (2024). Heme d formation in a Shewanella benthica hemoglobin. Journal of Inorganic Biochemistry. 259. 112654–112654. 2 indexed citations
3.
Schlessman, J.L., et al.. (2021). Control of distal lysine coordination in a monomeric hemoglobin: A role for heme peripheral interactions. Journal of Inorganic Biochemistry. 219. 111437–111437. 8 indexed citations
4.
Johnson, Eric A., et al.. (2018). Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii. Biochimica et Biophysica Acta (BBA) - General Subjects. 1862(12). 2660–2673. 14 indexed citations
5.
Robinson, A.C., et al.. (2015). Interactions between Pairs of Charges Buried in the Hydrophobic Interior of a Protein are Unexpectedly Weak. Biophysical Journal. 108(2). 517a–517a. 1 indexed citations
6.
Robinson, A.C., Carlos A. Castañeda, J.L. Schlessman, & Bertrand García‐Moreno E.. (2014). Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein. Proceedings of the National Academy of Sciences. 111(32). 11685–11690. 36 indexed citations
7.
Chimenti, Michael S., V.S. Khangulov, A.C. Robinson, et al.. (2012). Structural Reorganization Triggered by Charging of Lys Residues in the Hydrophobic Interior of a Protein. Structure. 20(6). 1071–1085. 40 indexed citations
8.
Harms, Michael J., et al.. (2011). Arginine residues at internal positions in a protein are always charged. Proceedings of the National Academy of Sciences. 108(47). 18954–18959. 146 indexed citations
9.
Robinson, A.C., Carlos A. Castañeda, J.L. Schlessman, & Bertrand García‐Moreno. (2011). Ion Pairs in the Hydrophobic Interior of a Protein: How Do Proteins Dissolve Salt in Oil?. Biophysical Journal. 100(3). 213a–213a.
10.
Tooley, James, V.S. Khangulov, J.L. Schlessman, et al.. (2011). The 1.75 Å resolution structure of fission protein Fis1 fromSaccharomyces cerevisiaereveals elusive interactions of the autoinhibitory domain. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(11). 1310–1315. 6 indexed citations
11.
Chimenti, Michael S., V.S. Khangulov, A.C. Robinson, et al.. (2009). Structural Consequences of the Ionization of Internal Lys Residues in a Protein. Biophysical Journal. 96(3). 587a–587a. 1 indexed citations
12.
Castañeda, Carlos A., Carolyn A. Fitch, Ananya Majumdar, et al.. (2009). Molecular determinants of the pKa values of Asp and Glu residues in staphylococcal nuclease. Proteins Structure Function and Bioinformatics. 77(3). 570–588. 143 indexed citations
13.
Harms, Michael J., Carlos A. Castañeda, J.L. Schlessman, et al.. (2009). The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors. Journal of Molecular Biology. 389(1). 34–47. 120 indexed citations
14.
Schlessman, J.L., et al.. (2008). Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable Groups. Biophysical Journal. 94(8). 3208–3216. 29 indexed citations
15.
Chimenti, Michael S., et al.. (2008). Electrostatic Effects in a Network of Polar and Ionizable Groups in Staphylococcal Nuclease. Journal of Molecular Biology. 379(5). 1045–1062. 47 indexed citations
16.
Damjanović, A., J.L. Schlessman, Carolyn A. Fitch, Angel E. Garcı́a, & Bertrand García‐Moreno E.. (2007). Role of Flexibility and Polarity as Determinants of the Hydration of Internal Cavities and Pockets in Proteins. Biophysical Journal. 93(8). 2791–2804. 33 indexed citations
17.
Denisov, Vladimir P., J.L. Schlessman, Bertrand García‐Moreno E., & Bertil Halle. (2004). Stabilization of Internal Charges in a Protein: Water Penetration or Conformational Change?. Biophysical Journal. 87(6). 3982–3994. 50 indexed citations
18.
Stewart, Phoebe L., Charles Y. Chiu, Dana A. Haley, Lawrence B. Kong, & J.L. Schlessman. (1999). Review: Resolution Issues in Single-Particle Reconstruction. Journal of Structural Biology. 128(1). 58–64. 10 indexed citations
19.
Schlessman, J.L., et al.. (1998). Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum. Journal of Molecular Biology. 280(4). 669–685. 118 indexed citations
20.
Schindelin, Hermann, Caroline Kisker, J.L. Schlessman, James B. Howard, & Douglas C. Rees. (1997). Structure of ADP·AIF4–-stabilized nitrogenase complex and its implications for signal transduction. Nature. 387(6631). 370–376. 396 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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