Mark T. Griffith

4.7k total citations · 3 hit papers
11 papers, 3.8k citations indexed

About

Mark T. Griffith is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Infectious Diseases. According to data from OpenAlex, Mark T. Griffith has authored 11 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 3 papers in Cellular and Molecular Neuroscience and 2 papers in Infectious Diseases. Recurrent topics in Mark T. Griffith's work include Receptor Mechanisms and Signaling (5 papers), Lipid Membrane Structure and Behavior (4 papers) and SARS-CoV-2 and COVID-19 Research (2 papers). Mark T. Griffith is often cited by papers focused on Receptor Mechanisms and Signaling (5 papers), Lipid Membrane Structure and Behavior (4 papers) and SARS-CoV-2 and COVID-19 Research (2 papers). Mark T. Griffith collaborates with scholars based in United States, Netherlands and Germany. Mark T. Griffith's co-authors include Raymond C. Stevens, Michael A. Hanson, Vadim Cherezov, Ellen Y. T. Chien, Veli‐Pekka Jaakola, J. Robert Lane, Adriaan P. IJzerman, C. Roth, Peter Kühn and Jeffrey Velasquez and has published in prestigious journals such as Science, Cell and Nature Communications.

In The Last Decade

Mark T. Griffith

11 papers receiving 3.7k citations

Hit Papers

The 2.6 Angstrom Crystal Structure of a Human A 2A Adenos... 2008 2026 2014 2020 2008 2008 2012 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark T. Griffith United States 11 3.3k 1.6k 500 444 359 11 3.8k
Qiang Zhao China 35 3.7k 1.1× 1.5k 1.0× 516 1.0× 361 0.8× 401 1.1× 97 4.7k
Malcolm Weir United Kingdom 27 2.9k 0.9× 1.2k 0.8× 531 1.1× 418 0.9× 373 1.0× 42 3.7k
Aaron A. Thompson United States 16 2.8k 0.8× 1.7k 1.1× 425 0.8× 208 0.5× 314 0.9× 23 3.3k
James C. Errey United Kingdom 33 3.3k 1.0× 1.2k 0.8× 621 1.2× 509 1.1× 389 1.1× 45 3.9k
C. Roth United States 8 3.0k 0.9× 1.3k 0.8× 369 0.7× 236 0.5× 274 0.8× 9 3.4k
Veli‐Pekka Jaakola Finland 18 2.9k 0.9× 1.4k 0.9× 435 0.9× 597 1.3× 373 1.0× 37 3.3k
A.S. Dore United Kingdom 26 3.2k 1.0× 1.6k 1.0× 506 1.0× 509 1.1× 447 1.2× 37 3.6k
Beili Wu China 33 3.6k 1.1× 1.5k 1.0× 811 1.6× 471 1.1× 386 1.1× 62 5.0k
Tetsuya Hori Japan 11 4.5k 1.4× 3.0k 1.9× 543 1.1× 161 0.4× 354 1.0× 15 5.2k

Countries citing papers authored by Mark T. Griffith

Since Specialization
Citations

This map shows the geographic impact of Mark T. Griffith'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 T. Griffith with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Mark T. Griffith more than expected).

Fields of papers citing papers by Mark T. Griffith

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark T. Griffith

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

All Works

11 of 11 papers shown
1.
Fenalti, Gustavo, Nicolas Villanueva, Mark T. Griffith, et al.. (2021). Structure of the human marker of self 5-transmembrane receptor CD47. Nature Communications. 12(1). 5218–5218. 35 indexed citations
2.
Chrencik, Jill, C. Roth, H. Kurata, et al.. (2015). Crystal Structure of Antagonist Bound Human Lysophosphatidic Acid Receptor 1. Cell. 161(7). 1633–1643. 147 indexed citations
3.
Hanson, Michael A., C. Roth, Euijung Jo, et al.. (2012). Crystal Structure of a Lipid G Protein–Coupled Receptor. Science. 335(6070). 851–855. 544 indexed citations breakdown →
4.
Chun, Eugene, Aaron A. Thompson, Wei Liu, et al.. (2012). Fusion Partner Toolchest for the Stabilization and Crystallization of G Protein-Coupled Receptors. Structure. 20(6). 967–976. 325 indexed citations
5.
Cherezov, Vadim, Michael A. Hanson, Mark T. Griffith, et al.. (2009). Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10 µm size X-ray synchrotron beam. Journal of The Royal Society Interface. 6(suppl_5). S587–97. 124 indexed citations
6.
Jaakola, Veli‐Pekka, Mark T. Griffith, Michael A. Hanson, et al.. (2008). The 2.6 Angstrom Crystal Structure of a Human A 2A Adenosine Receptor Bound to an Antagonist. Science. 322(5905). 1211–1217. 1475 indexed citations breakdown →
7.
Hanson, Michael A., Vadim Cherezov, Mark T. Griffith, et al.. (2008). A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor. Structure. 16(6). 897–905. 780 indexed citations breakdown →
8.
Cherezov, Vadim, Jeffrey Liu, Mark T. Griffith, Michael A. Hanson, & Raymond C. Stevens. (2008). LCP-FRAP Assay for Pre-Screening Membrane Proteins for In Meso Crystallization. Crystal Growth & Design. 8(12). 4307–4315. 57 indexed citations
9.
Hanson, Michael A., Alexei Brooun, Kent A. Baker, et al.. (2007). Profiling of membrane protein variants in a baculovirus system by coupling cell-surface detection with small-scale parallel expression. Protein Expression and Purification. 56(1). 85–92. 34 indexed citations
10.
Joseph, Jeremiah S., Kumar Singh Saikatendu, Vanitha Subramanian, et al.. (2006). Crystal Structure of Nonstructural Protein 10 from the Severe Acute Respiratory Syndrome Coronavirus Reveals a Novel Fold with Two Zinc-Binding Motifs. Journal of Virology. 80(16). 7894–7901. 94 indexed citations
11.
Saikatendu, Kumar Singh, Jeremiah S. Joseph, Vanitha Subramanian, et al.. (2005). Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3. Structure. 13(11). 1665–1675. 157 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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