Christopher Bystroff

1.3k total citations
32 papers, 1.0k citations indexed

About

Christopher Bystroff is a scholar working on Molecular Biology, Materials Chemistry and Biophysics. According to data from OpenAlex, Christopher Bystroff has authored 32 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 10 papers in Materials Chemistry and 6 papers in Biophysics. Recurrent topics in Christopher Bystroff's work include Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (10 papers) and Machine Learning in Bioinformatics (5 papers). Christopher Bystroff is often cited by papers focused on Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (10 papers) and Machine Learning in Bioinformatics (5 papers). Christopher Bystroff collaborates with scholars based in United States, Singapore and Denmark. Christopher Bystroff's co-authors include Joseph Kraut, Stuart J. Oatley, J. Kraut, Robert J. Fletterick, Yao-Ming Huang, Mong Li Lee, Wynne Hsu, David Baker, Marisa E. McGrath and Thorsten Erpel and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Christopher Bystroff

32 papers receiving 984 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Christopher Bystroff United States 15 756 301 84 81 62 32 1.0k
Conni Lauritzen Denmark 16 751 1.0× 58 0.2× 68 0.8× 75 0.9× 51 0.8× 22 1.2k
Michael S. Ackerman United States 8 594 0.8× 319 1.1× 36 0.4× 61 0.8× 22 0.4× 9 738
Marc Ribó Spain 21 1.0k 1.3× 263 0.9× 155 1.8× 70 0.9× 13 0.2× 59 1.2k
Aaron P. Yamniuk United States 18 647 0.9× 85 0.3× 67 0.8× 99 1.2× 79 1.3× 40 1.1k
Stephen J. Demarest United States 25 1.6k 2.1× 315 1.0× 127 1.5× 71 0.9× 20 0.3× 50 2.0k
Suzanne Grothé Canada 16 581 0.8× 77 0.3× 222 2.6× 69 0.9× 39 0.6× 20 842
Galina Obmolova United States 25 1.6k 2.2× 261 0.9× 203 2.4× 118 1.5× 37 0.6× 60 2.2k
Michael T. Stumpp Switzerland 18 1.7k 2.2× 132 0.4× 126 1.5× 167 2.1× 32 0.5× 26 2.3k
María Vilanova Spain 22 1.1k 1.5× 292 1.0× 154 1.8× 77 1.0× 14 0.2× 72 1.3k
Gabriel Rosenblum United States 16 537 0.7× 53 0.2× 80 1.0× 32 0.4× 53 0.9× 25 873

Countries citing papers authored by Christopher Bystroff

Since Specialization
Citations

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

Fields of papers citing papers by Christopher Bystroff

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher Bystroff

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher Bystroff. A scholar is included among the top collaborators of Christopher Bystroff 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 Christopher Bystroff. Christopher Bystroff 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.
Yuan, Xin, Dmitri V. Zagorevski, Christine L. Clarke, et al.. (2023). Bacterial production of recombinant contraceptive vaccine antigen from CatSper displayed on a human papilloma virus-like particle. Vaccine. 41(46). 6791–6801. 2 indexed citations
2.
Bystroff, Christopher. (2021). Footprints to singularity: A global population model explains late 20th century slow-down and predicts peak within ten years. PLoS ONE. 16(5). e0247214–e0247214. 7 indexed citations
3.
Hwang, Jae Yeon, Jungmin Choi, Huafeng Wang, et al.. (2021). Genetic Defects in DNAH2 Underlie Male Infertility With Multiple Morphological Abnormalities of the Sperm Flagella in Humans and Mice. Frontiers in Cell and Developmental Biology. 9. 662903–662903. 43 indexed citations
4.
Isern, Sharon, et al.. (2019). HPV VLPs as Scaffolds for Vaccine Design. Biophysical Journal. 116(3). 58a–58a. 2 indexed citations
5.
Walcott, Benjamin, et al.. (2018). Fast design of arbitrary length loops in proteins using InteractiveRosetta. BMC Bioinformatics. 19(1). 337–337. 3 indexed citations
6.
Bystroff, Christopher. (2018). Intramembranal disulfide cross-linking elucidates the super-quaternary structure of mammalian CatSpers. Reproductive Biology. 18(1). 76–82. 8 indexed citations
7.
Crone, Donna E., et al.. (2017). Mispacking and the Fitness Landscape of the Green Fluorescent Protein Chromophore Milieu. Biochemistry. 56(5). 736–747. 8 indexed citations
8.
Shirke, Abhijit N., An Su, Evan H. Baugh, et al.. (2016). Influence of surface charge, binding site residues and glycosylation on Thielavia terrestris cutinase biochemical characteristics. Applied Microbiology and Biotechnology. 100(10). 4435–4446. 29 indexed citations
9.
DiPrimio, Nina, Theodore R. Keppel, Keith Fraser, et al.. (2013). The Designability of Protein Switches by Chemical Rescue of Structure: Mechanisms of Inactivation and Reactivation. Journal of the American Chemical Society. 135(50). 18840–18849. 26 indexed citations
10.
Huang, Yao‐ming, Sasmita Nayak, & Christopher Bystroff. (2011). Quantitative in vivo solubility and reconstitution of truncated circular permutants of green fluorescent protein. Protein Science. 20(11). 1775–1780. 14 indexed citations
11.
Bystroff, Christopher & Anders Krogh. (2008). Hidden Markov Models for Prediction of Protein Features. Humana Press eBooks. 413. 173–198. 26 indexed citations
12.
Shinde, Arti V., Christopher Bystroff, Chunyu Wang, et al.. (2007). Identification of the Peptide Sequences within the EIIIA (EDA) Segment of Fibronectin That Mediate Integrin α9β1-dependent Cellular Activities. Journal of Biological Chemistry. 283(5). 2858–2870. 81 indexed citations
13.
Hsu, Wynne, et al.. (2004). Remote homolog detection using local sequence–structure correlations. Proteins Structure Function and Bioinformatics. 57(3). 518–530. 33 indexed citations
14.
Hsu, Wynne, et al.. (2003). Efficient remote homology detection using local structure. Bioinformatics. 19(17). 2294–2301. 55 indexed citations
15.
Bystroff, Christopher & David Baker. (1997). Blind predictions of local protein structure in CASP2 targets using the I‐sites library. Proteins Structure Function and Bioinformatics. 29(S1). 167–171. 24 indexed citations
16.
Bystroff, Christopher, David Baker, Robert J. Fletterick, & David A. Agard. (1993). PRISM: application to the solution of two protein structures. Acta Crystallographica Section D Biological Crystallography. 49(5). 440–448. 5 indexed citations
17.
Baker, David, Christopher Bystroff, Robert J. Fletterick, & David A. Agard. (1993). PRISM: topologically constrained phased refinement for macromolecular crystallography. Acta Crystallographica Section D Biological Crystallography. 49(5). 429–439. 18 indexed citations
18.
Goddette, Dean W., et al.. (1992). The crystal structure of the Bacillus lentus alkaline protease, subtilisin BL, at 1.4 Å resolution. Journal of Molecular Biology. 228(2). 580–595. 32 indexed citations
19.
Bystroff, Christopher & Joseph Kraut. (1991). Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry. 30(8). 2227–2239. 169 indexed citations
20.

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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