Michael S. Chapman

7.1k total citations · 1 hit paper
117 papers, 5.6k citations indexed

About

Michael S. Chapman is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, Michael S. Chapman has authored 117 papers receiving a total of 5.6k indexed citations (citations by other indexed papers that have themselves been cited), including 77 papers in Molecular Biology, 40 papers in Genetics and 31 papers in Materials Chemistry. Recurrent topics in Michael S. Chapman's work include Virus-based gene therapy research (40 papers), Enzyme Structure and Function (31 papers) and Protein Structure and Dynamics (23 papers). Michael S. Chapman is often cited by papers focused on Virus-based gene therapy research (40 papers), Enzyme Structure and Function (31 papers) and Protein Structure and Dynamics (23 papers). Michael S. Chapman collaborates with scholars based in United States, United Kingdom and Switzerland. Michael S. Chapman's co-authors include Qing Xie, Thayumanasamy Somasundaram, Michael G. Rossmann, Nancy Meyer, Felcy Fabiola, Thomas F. Lerch, Joan Hare, W. Ross Ellington, Arezki Azzi and Omar Davulcu and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Michael S. Chapman

117 papers receiving 5.5k citations

Hit Papers

An essential receptor for adeno-associated virus infection 2016 2026 2019 2022 2016 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Michael S. Chapman United States 39 3.5k 2.5k 1.1k 796 746 117 5.6k
Phoebe L. Stewart United States 53 5.3k 1.5× 2.5k 1.0× 1.2k 1.1× 412 0.5× 271 0.4× 125 8.2k
Roger M. Burnett United States 39 2.9k 0.8× 2.2k 0.9× 1.3k 1.2× 228 0.3× 268 0.4× 78 5.4k
José L. Carrascosa Spain 59 4.9k 1.4× 1.6k 0.6× 1.1k 1.0× 415 0.5× 381 0.5× 217 9.6k
Guy Schoehn France 53 5.5k 1.6× 1.6k 0.6× 1.8k 1.7× 275 0.3× 286 0.4× 184 9.3k
Jonathan M. Grimes United Kingdom 54 3.9k 1.1× 1.1k 0.4× 2.9k 2.7× 700 0.9× 564 0.8× 158 9.4k
Sarah J. Butcher Finland 44 2.6k 0.8× 789 0.3× 1.5k 1.4× 570 0.7× 326 0.4× 129 5.7k
Mark Yeager United States 48 4.2k 1.2× 681 0.3× 1.9k 1.8× 488 0.6× 355 0.5× 115 7.8k
R. Holland Cheng United States 40 2.1k 0.6× 529 0.2× 1.8k 1.6× 661 0.8× 294 0.4× 119 5.8k
Charles C. Richardson United States 57 8.7k 2.5× 3.8k 1.5× 1.1k 1.0× 413 0.5× 349 0.5× 187 10.5k
Naiqian Cheng United States 46 2.7k 0.8× 884 0.4× 925 0.9× 532 0.7× 237 0.3× 86 5.7k

Countries citing papers authored by Michael S. Chapman

Since Specialization
Citations

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

Fields of papers citing papers by Michael S. Chapman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Michael S. Chapman. 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 Michael S. Chapman. The network helps show where Michael S. Chapman may publish in the future.

Co-authorship network of co-authors of Michael S. Chapman

This figure shows the co-authorship network connecting the top 25 collaborators of Michael S. Chapman. A scholar is included among the top collaborators of Michael S. Chapman 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 Michael S. Chapman. Michael S. Chapman 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.
Large, Edward & Michael S. Chapman. (2023). Adeno-associated virus receptor complexes and implications for adeno-associated virus immune neutralization. Frontiers in Microbiology. 14. 1116896–1116896. 10 indexed citations
2.
Xie, Qing, Alex J. Noble, Duncan Sousa, et al.. (2017). The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide. Molecular Therapy — Methods & Clinical Development. 5. 1–12. 31 indexed citations
3.
Davulcu, Omar, et al.. (2015). Parsimony in Protein Conformational Change. Structure. 23(7). 1190–1198. 7 indexed citations
4.
Lerch, Thomas F. & Michael S. Chapman. (2011). Identification of the heparin binding site on adeno-associated virus serotype 3B (AAV-3B). Virology. 423(1). 6–13. 43 indexed citations
5.
Lerch, Thomas F., Qing Xie, & Michael S. Chapman. (2010). The structure of adeno-associated virus serotype 3B (AAV-3B): Insights into receptor binding and immune evasion. Virology. 403(1). 26–36. 84 indexed citations
6.
Whittaker, Mei M., et al.. (2010). Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase. Archives of Biochemistry and Biophysics. 505(2). 213–225. 14 indexed citations
7.
Fabiola, Felcy, А.A. Коростелев, & Michael S. Chapman. (2006). Bias in cross-validated freeRfactors: mitigation of the effects of non-crystallographic symmetry. Acta Crystallographica Section D Biological Crystallography. 62(3). 227–238. 28 indexed citations
8.
Azzi, Arezki, Mohammad S. Yousef, J L Gattis, et al.. (2003). The Putative Catalytic Bases Have, at Most, an Accessory Role in the Mechanism of Arginine Kinase. Journal of Biological Chemistry. 278(29). 26952–26957. 47 indexed citations
9.
Bubb, M, L. Govindasamy, Elena G. Yarmola, et al.. (2002). Polylysine Induces an Antiparallel Actin Dimer That Nucleates Filament Assembly. Journal of Biological Chemistry. 277(23). 20999–21006. 67 indexed citations
10.
Fabiola, Felcy, Richard Bertram, А.A. Коростелев, & Michael S. Chapman. (2002). An improved hydrogen bond potential: Impact on medium resolution protein structures. Protein Science. 11(6). 1415–1423. 99 indexed citations
11.
Chapman, Michael S., et al.. (2001). Conformational Disorder of Proteins Assessed by Real-Space Molecular Dynamics Refinement. Biophysical Journal. 80(3). 1466–1472. 12 indexed citations
12.
Bertram, Richard, J. R. Quine, Michael S. Chapman, & Timothy A. Cross. (2000). Atomic Refinement Using Orientational Restraints from Solid-State NMR. Journal of Magnetic Resonance. 147(1). 9–16. 26 indexed citations
13.
Zhou, Genfa, W. Ross Ellington, & Michael S. Chapman. (2000). Induced Fit in Arginine Kinase. Biophysical Journal. 78(3). 1541–1550. 35 indexed citations
14.
Zhou, Genfa, Junfeng Wang, Eric Blanc, & Michael S. Chapman. (1998). Determination of the Relative Precision of Atoms in a Macromolecular Structure. Acta Crystallographica Section D Biological Crystallography. 54(3). 391–399. 10 indexed citations
15.
Chapman, Michael S.. (1998). Watching One’s P’s and Q’s: Promiscuity, Plasticity, and Quasiequivalence in a T=1 Virus. Biophysical Journal. 74(1). 639–644. 3 indexed citations
16.
Chapman, Michael S. & Eric Blanc. (1997). Potential use of real-space refinement in protein structure determination. Acta Crystallographica Section D Biological Crystallography. 53(2). 203–206. 7 indexed citations
17.
Xie, Qing & Michael S. Chapman. (1996). Canine Parvovirus Capsid Structure, Analyzed at 2.9 Å Resolution. Journal of Molecular Biology. 264(3). 497–520. 111 indexed citations
18.
Chapman, Michael S. & Michael G. Rossmann. (1996). Structural refinement of the DNA-containing capsid of canine parvovirus using RSRef, a resolution-dependent stereochemically restrained real-space refinement method. Acta Crystallographica Section D Biological Crystallography. 52(1). 129–142. 13 indexed citations
19.
Chapman, Michael S. & M.G. Rossmann. (1993). Structure, Sequence, and Function Correlations among Parvoviruses. Virology. 194(2). 491–508. 163 indexed citations
20.
Kim, Sangsoo, Thomas J. Smith, Michael S. Chapman, et al.. (1989). Crystal structure of human rhinovirus serotype 1A (HRV1A). Journal of Molecular Biology. 210(1). 91–111. 161 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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