Peter Oelschlaeger

1.6k total citations
45 papers, 1.3k citations indexed

About

Peter Oelschlaeger is a scholar working on Molecular Medicine, Molecular Biology and Infectious Diseases. According to data from OpenAlex, Peter Oelschlaeger has authored 45 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Medicine, 17 papers in Molecular Biology and 15 papers in Infectious Diseases. Recurrent topics in Peter Oelschlaeger's work include Antibiotic Resistance in Bacteria (33 papers), Tuberculosis Research and Epidemiology (14 papers) and Pneumocystis jirovecii pneumonia detection and treatment (10 papers). Peter Oelschlaeger is often cited by papers focused on Antibiotic Resistance in Bacteria (33 papers), Tuberculosis Research and Epidemiology (14 papers) and Pneumocystis jirovecii pneumonia detection and treatment (10 papers). Peter Oelschlaeger collaborates with scholars based in United States, China and Germany. Peter Oelschlaeger's co-authors include Ke‐Wu Yang, Juergen Pleiss, Rolf D. Schmid, Stephen L. Mayo, Arieh Warshel, Jürgen Pleiss, Kaushik Joshi, Susanna Monti, Ying Shi and Yun Kyung Shin and has published in prestigious journals such as Nucleic Acids Research, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Peter Oelschlaeger

44 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Peter Oelschlaeger United States 24 696 561 267 248 238 45 1.3k
Christian Damblon Belgium 28 849 1.2× 673 1.2× 357 1.3× 227 0.9× 339 1.4× 56 1.7k
Donatella Tondi Italy 22 500 0.7× 584 1.0× 285 1.1× 235 0.9× 247 1.0× 50 1.2k
Yanzi Zhou China 26 596 0.9× 506 0.9× 289 1.1× 95 0.4× 153 0.6× 82 1.9k
Manuela Benvenuti Italy 18 766 1.1× 393 0.7× 413 1.5× 130 0.5× 215 0.9× 37 1.3k
Michiyoshi Nukaga Japan 18 893 1.3× 398 0.7× 407 1.5× 136 0.5× 237 1.0× 38 1.2k
Filomena De Luca Italy 20 1.1k 1.6× 466 0.8× 487 1.8× 214 0.9× 311 1.3× 41 1.5k
Philip Hinchliffe United Kingdom 21 1.3k 1.9× 1.2k 2.1× 536 2.0× 304 1.2× 406 1.7× 43 2.6k
Cecilia Pozzi Italy 18 303 0.4× 536 1.0× 171 0.6× 125 0.5× 193 0.8× 55 1.2k
Kade D. Roberts Australia 26 1.1k 1.6× 1.0k 1.8× 713 2.7× 116 0.5× 327 1.4× 57 2.3k
Patricia Lassaux Belgium 15 392 0.6× 259 0.5× 160 0.6× 154 0.6× 237 1.0× 20 781

Countries citing papers authored by Peter Oelschlaeger

Since Specialization
Citations

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

Fields of papers citing papers by Peter Oelschlaeger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Peter Oelschlaeger

This figure shows the co-authorship network connecting the top 25 collaborators of Peter Oelschlaeger. A scholar is included among the top collaborators of Peter Oelschlaeger 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 Peter Oelschlaeger. Peter Oelschlaeger 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.
Oelschlaeger, Peter. (2024). Molecular Mechanisms and the Significance of Synonymous Mutations. Biomolecules. 14(1). 132–132. 11 indexed citations
2.
Chen, Cheng, Peter Oelschlaeger, Jürgen Brem, et al.. (2023). A dual covalent binder for labelling and inhibiting serine and metallo-carbapenemases. Chemical Communications. 59(60). 9227–9230. 2 indexed citations
3.
Oelschlaeger, Peter, et al.. (2023). Strategies to Name Metallo-β-Lactamases and Number Their Amino Acid Residues. Antibiotics. 12(12). 1746–1746. 6 indexed citations
4.
Chen, Cheng, Peter Oelschlaeger, Dongmei Wang, et al.. (2022). Structure and Mechanism-Guided Design of Dual Serine/Metallo-Carbapenemase Inhibitors. Journal of Medicinal Chemistry. 65(8). 5954–5974. 13 indexed citations
5.
Nielsen, Travis B., Jun Yan, Rachel Li, et al.. (2021). Monoclonal Antibody Therapy against Acinetobacter baumannii. Infection and Immunity. 89(10). e0016221–e0016221. 28 indexed citations
6.
Faheem, Mohammad, et al.. (2021). Role of Synonymous Mutations in the Evolution of TEM β-Lactamase Genes. Antimicrobial Agents and Chemotherapy. 65(6). 6 indexed citations
7.
Zhang, Charles J., et al.. (2019). Mutation S115T in IMP-Type Metallo-β-Lactamases Compensates for Decreased Expression Levels Caused by Mutation S119G. Biomolecules. 9(11). 724–724. 3 indexed citations
8.
Kim, Jean, et al.. (2016). Functionalizing the γ-position of α-diazo-β-ketoesters. Tetrahedron Letters. 57(30). 3330–3333. 1 indexed citations
9.
Liu, Xiaolong, Ke‐Wu Yang, Yuejuan Zhang, et al.. (2016). Optimization of amino acid thioesters as inhibitors of metallo-β-lactamase L1. Bioorganic & Medicinal Chemistry Letters. 26(19). 4698–4701. 16 indexed citations
10.
Zhai, Le, et al.. (2016). Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) Inhibitors. ACS Medicinal Chemistry Letters. 7(4). 413–417. 55 indexed citations
11.
Oelschlaeger, Peter, et al.. (2015). Uncovering Molecular Bases Underlying Bone Morphogenetic Protein Receptor Inhibitor Selectivity. PLoS ONE. 10(7). e0132221–e0132221. 11 indexed citations
12.
Cook, Katie, et al.. (2015). Triethysilyl enol ethers in the synthesis of carbapenem precursors. Tetrahedron Letters. 56(23). 3385–3389. 4 indexed citations
13.
Yang, Ke‐Wu, et al.. (2014). Diaryl‐Substituted Azolylthioacetamides: Inhibitor Discovery of New Delhi Metallo‐β‐Lactamase‐1 (NDM‐1). ChemMedChem. 9(11). 2445–2448. 58 indexed citations
14.
Monti, Susanna, Peter Fristrup, Kaushik Joshi, et al.. (2013). Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field. Physical Chemistry Chemical Physics. 15(36). 15062–15062. 130 indexed citations
15.
Rucker, Robert B., Peter Oelschlaeger, & Arieh Warshel. (2009). A binding free energy decomposition approach for accurate calculations of the fidelity of DNA polymerases. Proteins Structure Function and Bioinformatics. 78(3). 671–680. 23 indexed citations
16.
Oelschlaeger, Peter. (2008). Outsmarting metallo-β-lactamases by mimicking their natural evolution. Journal of Inorganic Biochemistry. 102(12). 2043–2051. 20 indexed citations
17.
Oelschlaeger, Peter & Juergen Pleiss. (2006). Hydroxyl Groups in the ββ Sandwich of Metallo-β-lactamases Favor Enzyme Activity: Tyr218 and Ser262 Pull Down the Lid. Journal of Molecular Biology. 366(1). 316–329. 17 indexed citations
18.
Oelschlaeger, Peter, et al.. (2003). Identification of factors impeding the production of a single-chain antibody fragment in Escherichia coli by comparing in vivo and in vitro expression. Applied Microbiology and Biotechnology. 61(2). 123–132. 18 indexed citations
19.
Oelschlaeger, Peter, Rolf D. Schmid, & Jürgen Pleiss. (2003). Insight into the mechanism of the IMP-1 metallo- -lactamase by molecular dynamics simulations. Protein Engineering Design and Selection. 16(5). 341–350. 50 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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