Amy Grunbeck

493 total citations
10 papers, 332 citations indexed

About

Amy Grunbeck is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Oncology. According to data from OpenAlex, Amy Grunbeck has authored 10 papers receiving a total of 332 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 5 papers in Radiology, Nuclear Medicine and Imaging and 4 papers in Oncology. Recurrent topics in Amy Grunbeck's work include Receptor Mechanisms and Signaling (7 papers), Monoclonal and Polyclonal Antibodies Research (5 papers) and Chemical Synthesis and Analysis (4 papers). Amy Grunbeck is often cited by papers focused on Receptor Mechanisms and Signaling (7 papers), Monoclonal and Polyclonal Antibodies Research (5 papers) and Chemical Synthesis and Analysis (4 papers). Amy Grunbeck collaborates with scholars based in United States, Poland and Denmark. Amy Grunbeck's co-authors include Thomas P. Sakmar, Thomas Huber, Perminder S. Sachdev, Adam M. Knepp, Sourabh Banerjee, Thue W. Schwartz, Richard Looby, Daniel J.‐F. Chinnapen, Yong Ren and Thomas J. McMurry and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Amy Grunbeck

10 papers receiving 329 citations

Peers

Amy Grunbeck
Angela Wittelsberger United States
Sergey Mamaev United States
Francis W. Lau United States
Shigeru Kubo Japan
Shenglong Ling China
Lewis R. Vidler United Kingdom
Jendrik Schöppe Switzerland
Tzvetana Lazarova Spain
Rachit Shah United States
Sourabh Banerjee United States
Angela Wittelsberger United States
Amy Grunbeck
Citations per year, relative to Amy Grunbeck Amy Grunbeck (= 1×) peers Angela Wittelsberger

Countries citing papers authored by Amy Grunbeck

Since Specialization
Citations

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

Fields of papers citing papers by Amy Grunbeck

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Amy Grunbeck

This figure shows the co-authorship network connecting the top 25 collaborators of Amy Grunbeck. A scholar is included among the top collaborators of Amy Grunbeck 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 Amy Grunbeck. Amy Grunbeck is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

10 of 10 papers shown
1.
Huber, Thomas, et al.. (2014). Mapping Substance P Binding Sites on the Neurokinin-1 Receptor Using Genetic Incorporation of a Photoreactive Amino Acid. Journal of Biological Chemistry. 289(26). 18045–18054. 50 indexed citations
2.
Grunbeck, Amy, Thomas Huber, & Thomas P. Sakmar. (2013). Mapping a Ligand Binding Site Using Genetically Encoded Photoactivatable Crosslinkers. Methods in enzymology on CD-ROM/Methods in enzymology. 520. 307–322. 18 indexed citations
3.
Grunbeck, Amy, et al.. (2013). Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors. Journal of Visualized Experiments. 11 indexed citations
4.
Grunbeck, Amy & Thomas P. Sakmar. (2013). Probing G Protein-Coupled Receptor—Ligand Interactions with Targeted Photoactivatable Cross-Linkers. Biochemistry. 52(48). 8625–8632. 38 indexed citations
5.
Berro, Reem, Anila Yasmeen, Ravinder Abrol, et al.. (2013). Use of G-Protein-Coupled and -Uncoupled CCR5 Receptors by CCR5 Inhibitor-Resistant and -Sensitive Human Immunodeficiency Virus Type 1 Variants. Journal of Virology. 87(12). 6569–6581. 30 indexed citations
6.
Grunbeck, Amy, et al.. (2013). Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors. Journal of Visualized Experiments. 3 indexed citations
7.
Grunbeck, Amy, Thomas Huber, Perminder S. Sachdev, & Thomas P. Sakmar. (2011). Mapping the Ligand-Binding Site on a G Protein-Coupled Receptor (GPCR) Using Genetically Encoded Photocrosslinkers. Biochemistry. 50(17). 3411–3413. 85 indexed citations
8.
Janz, Jay M., Yong Ren, Richard Looby, et al.. (2011). Direct Interaction between an Allosteric Agonist Pepducin and the Chemokine Receptor CXCR4. Journal of the American Chemical Society. 133(40). 15878–15881. 62 indexed citations
9.
Grunbeck, Amy, Thomas Huber, Shixin Ye, Sourabh Banerjee, & Thomas P. Sakmar. (2010). Novel Technology to Study Chemokine Receptor Signaling Complexes. Biophysical Journal. 98(3). 292a–292a. 1 indexed citations
10.
Knepp, Adam M., Amy Grunbeck, Sourabh Banerjee, Thomas P. Sakmar, & Thomas Huber. (2010). Direct Measurement of Thermal Stability of Expressed CCR5 and Stabilization by Small Molecule Ligands. Biochemistry. 50(4). 502–511. 34 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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