Sherry L. Mowbray

6.6k total citations
111 papers, 5.3k citations indexed

About

Sherry L. Mowbray is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Sherry L. Mowbray has authored 111 papers receiving a total of 5.3k indexed citations (citations by other indexed papers that have themselves been cited), including 90 papers in Molecular Biology, 40 papers in Materials Chemistry and 18 papers in Genetics. Recurrent topics in Sherry L. Mowbray's work include Enzyme Structure and Function (40 papers), Protein Structure and Dynamics (27 papers) and Bacterial Genetics and Biotechnology (17 papers). Sherry L. Mowbray is often cited by papers focused on Enzyme Structure and Function (40 papers), Protein Structure and Dynamics (27 papers) and Bacterial Genetics and Biotechnology (17 papers). Sherry L. Mowbray collaborates with scholars based in Sweden, United States and India. Sherry L. Mowbray's co-authors include Maria M. Flocco, T. Alwyn Jones, Terese Bergfors, C. Evalena Andersson, L. Brent Cole, Alexander D. Cameron, Jill A. Sigrell, Daniel E. Koshland, Michael Arand and Jinyu Zou and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Sherry L. Mowbray

111 papers receiving 5.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sherry L. Mowbray Sweden 42 3.8k 1.1k 816 545 521 111 5.3k
Joseph D. Schrag Canada 40 5.8k 1.5× 760 0.7× 417 0.5× 600 1.1× 616 1.2× 71 7.4k
David L. Ollis Australia 47 5.4k 1.4× 1.2k 1.1× 938 1.1× 570 1.0× 511 1.0× 140 7.9k
Michail N. Isupov United Kingdom 34 3.7k 1.0× 1.3k 1.2× 466 0.6× 402 0.7× 445 0.9× 116 5.2k
Kor H. Kalk Netherlands 50 5.2k 1.4× 1.5k 1.4× 1.1k 1.3× 644 1.2× 844 1.6× 95 8.0k
Patricia C. Babbitt United States 52 6.3k 1.7× 2.1k 2.0× 484 0.6× 354 0.6× 770 1.5× 134 8.1k
Karen N. Allen United States 43 4.0k 1.0× 1.9k 1.7× 473 0.6× 613 1.1× 687 1.3× 137 5.8k
Rik K. Wierenga Finland 48 6.7k 1.7× 2.8k 2.6× 526 0.6× 331 0.6× 927 1.8× 158 8.8k
Caroline Kisker Germany 52 5.7k 1.5× 979 0.9× 1.0k 1.3× 939 1.7× 219 0.4× 139 8.7k
Patrick J. Baker United Kingdom 36 3.1k 0.8× 1.7k 1.6× 503 0.6× 519 1.0× 898 1.7× 126 4.7k
S.E. Ealick United States 52 6.7k 1.8× 2.0k 1.9× 562 0.7× 707 1.3× 867 1.7× 246 9.3k

Countries citing papers authored by Sherry L. Mowbray

Since Specialization
Citations

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

Fields of papers citing papers by Sherry L. Mowbray

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sherry L. Mowbray

This figure shows the co-authorship network connecting the top 25 collaborators of Sherry L. Mowbray. A scholar is included among the top collaborators of Sherry L. Mowbray 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 Sherry L. Mowbray. Sherry L. Mowbray 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.
Cao, Sha, Bo Lundgren, Katharina Klöditz, et al.. (2024). Design, synthesis, and in vitro biological evaluation of meta-sulfonamidobenzamide-based antibacterial LpxH inhibitors. European Journal of Medicinal Chemistry. 278. 116790–116790. 1 indexed citations
2.
Karlén, Anders, et al.. (2022). Bacterial type I signal peptidase inhibitors - Optimized hits from nature. European Journal of Medicinal Chemistry. 238. 114490–114490. 14 indexed citations
3.
Amrein, Beat Anton, Paul Bauer, Fernanda Duarte, et al.. (2015). Expanding the Catalytic Triad in Epoxide Hydrolases and Related Enzymes. ACS Catalysis. 5(10). 5702–5713. 38 indexed citations
4.
Covarrubias, Adrian Suárez, et al.. (2011). Expression and β-glucan binding properties of Scots pine (Pinus sylvestris L.) antimicrobial protein (Sp-AMP). Plant Molecular Biology. 77(1-2). 33–45. 19 indexed citations
5.
6.
7.
8.
Krajewski, Wojciech, R. Collins, L. Holmberg-Schiavone, et al.. (2007). Crystal Structures of Mammalian Glutamine Synthetases Illustrate Substrate-Induced Conformational Changes and Provide Opportunities for Drug and Herbicide Design. Journal of Molecular Biology. 375(1). 217–228. 103 indexed citations
9.
Chye, Mee‐Len, et al.. (2004). Functional analyses of the chitin-binding domains and the catalytic domain of Brassica juncea chitinase BjCHI1. Plant Molecular Biology. 56(2). 285–298. 31 indexed citations
10.
Harhangi, Harry R., Wimal Ubhayasekera, Maarten van Dinther, et al.. (2003). Cel6A, a major exoglucanase from the cellulosome of the anaerobic fungi Piromyces sp. E2 and Piromyces equi. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1628(1). 30–39. 25 indexed citations
11.
Persson, C., Ulla Engström, Sherry L. Mowbray, & Arne Östman. (2002). Primary sequence determinants responsible for site‐selective dephosphorylation of the PDGF β‐receptor by the receptor‐like protein tyrosine phosphatase DEP‐1. FEBS Letters. 517(1-3). 27–31. 18 indexed citations
12.
Muñoz, Inés G., Wimal Ubhayasekera, Hongbin Henriksson, et al.. (2001). Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 Å resolution and homology models of the isozymes. Journal of Molecular Biology. 314(5). 1097–1111. 82 indexed citations
13.
Mowbray, Sherry L., Charlotte Helgstrand, Jill A. Sigrell, Alexander D. Cameron, & T. Alwyn Jones. (1999). Errors and reproducibility in electron-density map interpretation. Acta Crystallographica Section D Biological Crystallography. 55(7). 1309–1319. 14 indexed citations
14.
Mowbray, Sherry L., et al.. (1998). Multiple open forms of ribose-binding protein trace the path of its conformational change. Journal of Molecular Biology. 279(3). 651–664. 143 indexed citations
15.
Sigrell, Jill A., Alexander D. Cameron, T. Alwyn Jones, & Sherry L. Mowbray. (1998). Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 å resolution: insights into a new family of kinase structures. Structure. 6(2). 183–193. 164 indexed citations
16.
Mowbray, Sherry L. & Mats Sandgren. (1998). Chemotaxis Receptors: A Progress Report on Structure and Function. Journal of Structural Biology. 124(2-3). 257–275. 55 indexed citations
17.
Dunten, Pete & Sherry L. Mowbray. (1995). Modeling of the structure of the Haemophilus influenzae heme‐binding protein suggests a mode of heme interaction. Protein Science. 4(11). 2335–2340. 10 indexed citations
18.
Flocco, Maria M. & Sherry L. Mowbray. (1995). Cα‐based torsion angles: A simple tool to analyze protein conformational changes. Protein Science. 4(10). 2118–2122. 34 indexed citations
19.
Dunten, Pete, et al.. (1993). Crystallization and Preliminary X-ray Analysis of the Periplasmic Dipeptide Binding Protein from Escherichia coli. Journal of Molecular Biology. 231(1). 145–147. 8 indexed citations
20.
Mowbray, Sherry L.. (1990). STRUCTURE OF THE PERIPLASMIC GLUCOSE/GALACTOSE RECEPTOR OF SALMONELLA TYPHIMURIUM. PubMed. 1(1-2). 41–53. 29 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Joseph D. Schrag Breakdown of academic impact, for papers by David L. Ollis Breakdown of academic impact, for papers by Michail N. Isupov Breakdown of academic impact, for papers by Kor H. Kalk Breakdown of academic impact, for papers by Patricia C. Babbitt Breakdown of academic impact, for papers by Karen N. Allen Breakdown of academic impact, for papers by Rik K. Wierenga Breakdown of academic impact, for papers by Caroline Kisker Breakdown of academic impact, for papers by Patrick J. Baker Breakdown of academic impact, for papers by S.E. Ealick
Rankless by CCL
2026