Steven C. Almo

25.4k total citations · 2 hit papers
374 papers, 18.8k citations indexed

About

Steven C. Almo is a scholar working on Molecular Biology, Materials Chemistry and Immunology. According to data from OpenAlex, Steven C. Almo has authored 374 papers receiving a total of 18.8k indexed citations (citations by other indexed papers that have themselves been cited), including 223 papers in Molecular Biology, 84 papers in Materials Chemistry and 75 papers in Immunology. Recurrent topics in Steven C. Almo's work include Enzyme Structure and Function (84 papers), Biochemical and Molecular Research (52 papers) and Immune Cell Function and Interaction (37 papers). Steven C. Almo is often cited by papers focused on Enzyme Structure and Function (84 papers), Biochemical and Molecular Research (52 papers) and Immune Cell Function and Interaction (37 papers). Steven C. Almo collaborates with scholars based in United States, New Zealand and France. Steven C. Almo's co-authors include А.А. Федоров, Stanley G. Nathenson, E.V. Fedorov, U.A. Ramagopal, Vern L. Schramm, J.B. Bonanno, Nicole M. Mahoney, Wuxian Shi, V.N. Malashkevich and Y. Patskovsky and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Steven C. Almo

371 papers receiving 18.5k 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.

Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin

2009 501 citations P.G. Leiman, Marek Basler et al. Proceedings of the National Academy of Sciences profile →
A metabolic pathway for bile acid dehydroxylation by the gut microbiome

2020 384 citations Tyler L. Grove, Steven C. Almo 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
Steven C. Almo United States	76	10.9k	4.0k	2.7k	2.2k	2.1k	374	18.8k
John D. Pfeifer United States	49	12.7k 1.2×	2.3k 0.6×	2.2k 0.8×	2.3k 1.0×	1.7k 0.8×	176	20.8k
Manuel C. Peitsch Switzerland	56	14.0k 1.3×	2.7k 0.7×	1.8k 0.7×	1.6k 0.7×	1.3k 0.6×	291	23.6k
Liang Tong United States	77	13.9k 1.3×	1.9k 0.5×	1.6k 0.6×	2.4k 1.1×	2.0k 0.9×	339	20.3k
Laurence H. Pearl United Kingdom	76	18.0k 1.7×	2.1k 0.5×	2.5k 0.9×	2.7k 1.2×	2.2k 1.0×	217	21.3k
Robert M. Stroud United States	74	11.7k 1.1×	2.2k 0.6×	1.6k 0.6×	2.4k 1.1×	1.6k 0.8×	296	17.8k
Laurent C. Storoni United Kingdom	10	14.2k 1.3×	1.8k 0.5×	1.8k 0.7×	4.1k 1.8×	1.8k 0.8×	12	19.9k
Bernhard Lohkamp Sweden	15	16.0k 1.5×	1.8k 0.4×	1.9k 0.7×	4.0k 1.8×	2.0k 0.9×	26	22.3k
Giulio Superti‐Furga Austria	77	13.5k 1.2×	4.1k 1.0×	2.9k 1.1×	588 0.3×	2.1k 1.0×	247	21.7k
Charles S. Craik United States	76	10.6k 1.0×	2.2k 0.5×	3.4k 1.2×	1.0k 0.5×	1.2k 0.6×	344	19.6k
Jiansheng Jiang United States	28	14.1k 1.3×	2.1k 0.5×	1.4k 0.5×	3.9k 1.8×	1.7k 0.8×	60	18.4k

Countries citing papers authored by Steven C. Almo

Since Specialization

Citations

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

Fields of papers citing papers by Steven C. Almo

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Steven C. Almo. 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 Steven C. Almo. The network helps show where Steven C. Almo may publish in the future.

Co-authorship network of co-authors of Steven C. Almo

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

Slough, Megan M., Rong Li, Andrew S. Herbert, et al.. (2023). Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection. Nature Communications. 14(1). 4454–4454. 2 indexed citations

Kuraoka, Masayuki, Clare Burn Aschner, Ian W. Windsor, et al.. (2022). A non-neutralizing glycoprotein B monoclonal antibody protects against herpes simplex virus disease in mice. Journal of Clinical Investigation. 133(3). 18 indexed citations

Morano, Nicholas C., Ryan Schreiner, Natalia G. Herrera, et al.. (2022). Human immunomodulatory ligand B7-1 mediates synaptic remodeling via the p75 neurotrophin receptor. Journal of Clinical Investigation. 132(22). 4 indexed citations

Liu, Weifeng, Sarah C. Garrett-Thomson, Goo‐Young Seo, et al.. (2021). HVEM structures and mutants reveal distinct functions of binding to LIGHT and BTLA/CD160. The Journal of Experimental Medicine. 218(12). 20 indexed citations

Garforth, S., Hang Su, R. Brad Jones, et al.. (2021). T cell receptor–targeted immunotherapeutics drive selective in vivo HIV- and CMV-specific T cell expansion in humanized mice. Journal of Clinical Investigation. 131(23). 18 indexed citations

Esakova, Olga, Tyler L. Grove, Neela H. Yennawar, et al.. (2021). Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB. Nature. 597(7877). 566–570. 39 indexed citations

Pierce, Carl A., Paula Preston‐Hurlburt, Yile Dai, et al.. (2020). Immune responses to SARS-CoV-2 infection in hospitalized pediatric and adult patients. Science Translational Medicine. 12(564). 213 indexed citations

Aschner, Clare Burn, Benjamin Galen, Rohit K. Jangra, et al.. (2020). HVEM signaling promotes protective antibody-dependent cellular cytotoxicity (ADCC) vaccine responses to herpes simplex viruses. Science Immunology. 5(50). 14 indexed citations

Wang, Hua, А.А. Федоров, E.V. Fedorov, et al.. (2019). An essential bifunctional enzyme in Mycobacterium tuberculosis for itaconate dissimilation and leucine catabolism. Proceedings of the National Academy of Sciences. 116(32). 15907–15913. 47 indexed citations

10.

Kenney, Grace E., Laura M. K. Dassama, Maria‐Eirini Pandelia, et al.. (2018). The biosynthesis of methanobactin. Science. 359(6382). 1411–1416. 104 indexed citations

11.

Calhoun, Sara, Magdalena Korczynska, Brian San Francisco, et al.. (2018). Prediction of enzymatic pathways by integrative pathway mapping. eLife. 7. 30 indexed citations

12.

Ramagopal, U.A., R. Toro, Mingzhao Zhu, et al.. (2018). Comparison of Alicyclobacillus acidocaldarius o-Succinylbenzoate Synthase to Its Promiscuous N-Succinylamino Acid Racemase/o-Succinylbenzoate Synthase Relatives. Biochemistry. 57(26). 3676–3689. 8 indexed citations

13.

Janakiram, Murali, Jordan M. Chinai, Susan Fineberg, et al.. (2014). Expression, Clinical Significance, and Receptor Identification of the Newest B7 Family Member HHLA2 Protein. Clinical Cancer Research. 21(10). 2359–2366. 131 indexed citations

14.

Lukk, Tiit, A. Sakai, Chakrapani Kalyanaraman, et al.. (2012). Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily. Proceedings of the National Academy of Sciences. 109(11). 4122–4127. 45 indexed citations

15.

Samanta, Dibyendu, Gayatri Mukherjee, U.A. Ramagopal, et al.. (2011). Structural and functional characterization of a single-chain peptide–MHC molecule that modulates both naive and activated CD8 ⁺ T cells. Proceedings of the National Academy of Sciences. 108(33). 13682–13687. 18 indexed citations

16.

Ho, Meng-Chiao, Wuxian Shi, Agnes Rinaldo-Matthis, et al.. (2010). Four generations of transition-state analogues for human purine nucleoside phosphorylase. Proceedings of the National Academy of Sciences. 107(11). 4805–4812. 68 indexed citations

17.

Seffernick, Jennifer L., А.А. Федоров, E.V. Fedorov, et al.. (2010). X-ray Structure and Mutational Analysis of the Atrazine Chlorohydrolase TrzN. Journal of Biological Chemistry. 285(40). 30606–30614. 27 indexed citations

18.

Leiman, P.G., Marek Basler, U.A. Ramagopal, et al.. (2009). Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proceedings of the National Academy of Sciences. 106(11). 4154–4159. 501 indexed citations breakdown →

19.

Rinaldo-Matthis, Agnes, Andrew S. Murkin, U.A. Ramagopal, et al.. (2007). l -Enantiomers of Transition State Analogue Inhibitors Bound to Human Purine Nucleoside Phosphorylase. Journal of the American Chemical Society. 130(3). 842–844. 19 indexed citations

20.

Vorobiev, S.M., B.V. Strokopytov, David G. Drubin, et al.. (2003). The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism. Proceedings of the National Academy of Sciences. 100(10). 5760–5765. 132 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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