Mark A. Saper

13.2k total citations · 5 hit papers
51 papers, 10.7k citations indexed

About

Mark A. Saper is a scholar working on Molecular Biology, Immunology and Materials Chemistry. According to data from OpenAlex, Mark A. Saper has authored 51 papers receiving a total of 10.7k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 13 papers in Immunology and 13 papers in Materials Chemistry. Recurrent topics in Mark A. Saper's work include Enzyme Structure and Function (12 papers), Protein Tyrosine Phosphatases (10 papers) and RNA and protein synthesis mechanisms (10 papers). Mark A. Saper is often cited by papers focused on Enzyme Structure and Function (12 papers), Protein Tyrosine Phosphatases (10 papers) and RNA and protein synthesis mechanisms (10 papers). Mark A. Saper collaborates with scholars based in United States, Israel and Germany. Mark A. Saper's co-authors include Don C. Wiley, Pamela J. Björkman, Boudjéma Samraoui, Jack L. Strominger, William S. Bennett, Eric B. Fauman, Jack E. Dixon, Jeanne A. Stuckey, John M. Denu and Theodore S. Jardetzky and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Mark A. Saper

49 papers receiving 10.4k citations

Hit Papers

5 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.

Structure of the human class I histocompatibility antigen, HLA-A2

1987 2.7k citations Pamela J. Björkman, Mark A. Saper et al. Nature profile →
The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens

1987 1.9k citations Pamela J. Björkman, Mark A. Saper et al. Nature profile →
A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules

1988 984 citations Mark A. Saper, Boudjéma Samraoui et al. Nature profile →
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution

1991 932 citations Mark A. Saper, Pamela J. Björkman et al. Journal of Molecular Biology profile →
Specificity pockets for the side chains of peptide antigens in HLA-Aw68

1989 549 citations Mark A. Saper, Pamela J. Björkman 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
Mark A. Saper United States	30	6.4k	4.7k	1.5k	1.3k	654	51	10.7k
J L Strominger United States	51	6.4k 1.0×	3.1k 0.7×	1.8k 1.2×	1.0k 0.8×	1.1k 1.6×	101	9.9k
Raymond W. Sweet United States	43	4.0k 0.6×	5.1k 1.1×	2.5k 1.6×	1.1k 0.9×	983 1.5×	89	11.2k
Kurt Drickamer United States	68	8.6k 1.3×	10.3k 2.2×	2.2k 1.4×	847 0.6×	767 1.2×	159	17.1k
Åke Engström Sweden	47	2.4k 0.4×	4.8k 1.0×	961 0.6×	729 0.6×	501 0.8×	112	8.7k
William S. Bennett Germany	12	3.6k 0.6×	2.1k 0.5×	1.0k 0.7×	507 0.4×	343 0.5×	16	5.7k
Paul N. Barlow United Kingdom	50	3.7k 0.6×	2.5k 0.5×	568 0.4×	625 0.5×	379 0.6×	147	7.3k
Yaeta Endo Japan	46	4.3k 0.7×	5.6k 1.2×	809 0.5×	640 0.5×	330 0.5×	187	9.5k
Jens Schneider‐Mergener Germany	47	1.7k 0.3×	5.2k 1.1×	1.4k 0.9×	557 0.4×	1.1k 1.7×	124	7.5k
Jun Hirabayashi Japan	61	7.3k 1.1×	9.8k 2.1×	1.6k 1.0×	411 0.3×	1.2k 1.8×	293	13.5k
Michael Potter United States	62	4.6k 0.7×	6.8k 1.4×	4.0k 2.6×	1.2k 0.9×	2.0k 3.0×	284	12.7k

Countries citing papers authored by Mark A. Saper

Since Specialization

Citations

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

Fields of papers citing papers by Mark A. Saper

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark A. Saper

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

Isupov, Michail N., et al.. (2024). Octahedral Iron in Catalytic Sites of Endonuclease IV from Staphylococcus aureus and Escherichia coli. Biochemistry. 64(1). 67–82.

Larson, Matt, et al.. (2021). Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane. PLoS ONE. 16(11). e0259900–e0259900. 6 indexed citations

Shin, Jung‐Ho, Laura Álvarez, Lixin Fan, et al.. (2020). Structural basis of peptidoglycan endopeptidase regulation. Proceedings of the National Academy of Sciences. 117(21). 11692–11702. 29 indexed citations

Vijayalakshmi, J., et al.. (2019). Crystal structures of the amino-terminal domain of LpoA from Escherichia coli and Haemophilus influenzae. Acta Crystallographica Section F Structural Biology Communications. 75(5). 368–376. 4 indexed citations

Sathiyamoorthy, Karthik, J. Vijayalakshmi, Bhramara Tirupati, Lixin Fan, & Mark A. Saper. (2017). Structural analyses of the Haemophilus influenzae peptidoglycan synthase activator LpoA suggest multiple conformations in solution. Journal of Biological Chemistry. 292(43). 17626–17642. 10 indexed citations

Sathiyamoorthy, Karthik, Erez Mills, Titus M. Franzmann, Ilan Rosenshine, & Mark A. Saper. (2011). The Crystal Structure ofEscherichia coliGroup 4 Capsule Protein GfcC Reveals a Domain Organization Resembling That of Wza. Biochemistry. 50(24). 5465–5476. 23 indexed citations

Peleg, Adi, Yulia Shifrin, Ophir Ilan, et al.. (2005). Identification of an Escherichia coli Operon Required for Formation of the O-Antigen Capsule. Journal of Bacteriology. 187(15). 5259–5266. 77 indexed citations

Graumann, Johannes, Hauke Lilie, Xianli Tang, et al.. (2001). Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism. Structure. 9(5). 377–387. 114 indexed citations

Vijayalakshmi, J., et al.. (2001). The 2.2 Å Crystal Structure of Hsp33. Structure. 9(5). 367–375. 48 indexed citations

10.

Fauman, Eric B., Bart L. Staker, Fuzhong F. Zheng, et al.. (2000). RNA Methylation under Heat Shock Control. Molecular Cell. 6(2). 349–360. 201 indexed citations

11.

Staker, Bart L., Philipp Korber, James C.A. Bardwell, & Mark A. Saper. (2000). Structure of Hsp15 reveals a novel RNA-binding motif. The EMBO Journal. 19(4). 749–757. 46 indexed citations

12.

Denu, John M., Jeanne A. Stuckey, Mark A. Saper, & Jack E. Dixon. (1996). Form and Function in Protein Dephosphorylation. Cell. 87(3). 361–364. 282 indexed citations

13.

Fauman, Eric B. & Mark A. Saper. (1996). Structure and function of theprotein tyrosine phosphatases. Trends in Biochemical Sciences. 21(11). 413–417. 300 indexed citations

14.

Schubert, Heidi, Eric B. Fauman, Jeanne A. Stuckey, Jack E. Dixon, & Mark A. Saper. (1995). A ligand-induced conformational change in theyersiniaprotein tyrosine phosphatase. Protein Science. 4(9). 1904–1913. 94 indexed citations

15.

Stuckey, Jeanne A., et al.. (1994). Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate. Nature. 370(6490). 571–575. 334 indexed citations

16.

Latron, F, Laszlo Pazmany, Jo Morrison, et al.. (1992). A Critical Role for Conserved Residues in the Cleft of HLA-A2 in Presentation of a Nonapeptide to T Cells. Science. 257(5072). 964–967. 67 indexed citations

17.

Saper, Mark A., Halina Lis, Nathan Sharon, & Boaz Shaanan. (1987). Crystallization and preliminary X-ray diffraction studies of the lectin from Erythrina corallodendron. Journal of Molecular Biology. 193(4). 823–824. 5 indexed citations

18.

Björkman, Pamela J., Mark A. Saper, Boudjéma Samraoui, et al.. (1987). The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature. 329(6139). 512–518. 1894 indexed citations breakdown →

19.

Björkman, Pamela J., Mark A. Saper, Boudjéma Samraoui, et al.. (1987). Structure of the human class I histocompatibility antigen, HLA-A2. Nature. 329(6139). 506–512. 2696 indexed citations breakdown →

20.

Saper, Mark A., Hagit Eldar-Finkelman, Kiyoshi Mizuuchi, et al.. (1986). Crystallization of a DNA tridecamer d(C-G-C-A-G-A-A-T-T-C-G-C-G). Journal of Molecular Biology. 188(1). 111–113. 12 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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