Robert L. Matts

5.2k total citations
95 papers, 4.3k citations indexed

About

Robert L. Matts is a scholar working on Molecular Biology, Cell Biology and Computational Theory and Mathematics. According to data from OpenAlex, Robert L. Matts has authored 95 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 89 papers in Molecular Biology, 19 papers in Cell Biology and 13 papers in Computational Theory and Mathematics. Recurrent topics in Robert L. Matts's work include Heat shock proteins research (64 papers), Endoplasmic Reticulum Stress and Disease (16 papers) and Protein Structure and Dynamics (15 papers). Robert L. Matts is often cited by papers focused on Heat shock proteins research (64 papers), Endoplasmic Reticulum Stress and Disease (16 papers) and Protein Structure and Dynamics (15 papers). Robert L. Matts collaborates with scholars based in United States, United Kingdom and Australia. Robert L. Matts's co-authors include Steven D. Hartson, Bo-Geon Yun, Brian S. J. Blagg, R. P. Hurst, Thomas L. Prince, Jieya Shao, Sheri Uma, Vanitha Thulasiraman, Nicholas A. Kotov and Wenjun Huang and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Advanced Materials.

In The Last Decade

Robert L. Matts

94 papers receiving 4.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert L. Matts United States 45 3.5k 750 563 484 469 95 4.3k
Holger Sondermann United States 41 4.8k 1.4× 1.0k 1.3× 588 1.0× 647 1.3× 137 0.3× 84 6.1k
Ichio Shimada Japan 45 4.8k 1.4× 548 0.7× 655 1.2× 585 1.2× 214 0.5× 253 6.5k
Franz Hagn Germany 24 2.5k 0.7× 203 0.3× 283 0.5× 207 0.4× 114 0.2× 50 3.0k
Palma Rocchi France 40 3.0k 0.9× 367 0.5× 212 0.4× 507 1.0× 83 0.2× 85 4.5k
Atanas V. Koulov United States 24 2.7k 0.8× 479 0.6× 407 0.7× 314 0.6× 72 0.2× 36 3.8k
Achim Brinker United States 20 3.0k 0.9× 359 0.5× 419 0.7× 303 0.6× 282 0.6× 31 3.6k
Enríque Pérez‐Payá Spain 41 3.3k 0.9× 309 0.4× 616 1.1× 330 0.7× 45 0.1× 151 5.3k
O. Gileadi United Kingdom 44 4.3k 1.2× 346 0.5× 272 0.5× 264 0.5× 143 0.3× 108 5.5k
Jesper Nylandsted Denmark 35 3.6k 1.0× 1.3k 1.8× 158 0.3× 530 1.1× 71 0.2× 72 5.0k
Carlos H.I. Ramos Brazil 32 2.6k 0.7× 411 0.5× 397 0.7× 179 0.4× 148 0.3× 145 3.5k

Countries citing papers authored by Robert L. Matts

Since Specialization
Citations

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

Fields of papers citing papers by Robert L. Matts

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert L. Matts

This figure shows the co-authorship network connecting the top 25 collaborators of Robert L. Matts. A scholar is included among the top collaborators of Robert L. Matts 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 Robert L. Matts. Robert L. Matts 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.
Lyu, Wentao, Zhuo Deng, Lakshmi T. Sunkara, et al.. (2018). High Throughput Screening for Natural Host Defense Peptide-Inducing Compounds as Novel Alternatives to Antibiotics. Frontiers in Cellular and Infection Microbiology. 8. 191–191. 28 indexed citations
2.
Khandelwal, Anuj, Shuxia Peng, Sanket J. Mishra, et al.. (2018). Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor. Nature Communications. 9(1). 425–425. 90 indexed citations
3.
Sun, Liang, Steven D. Hartson, & Robert L. Matts. (2015). Identification of proteins associated with Aha1 in HeLa cells by quantitative proteomics. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(5). 365–380. 8 indexed citations
4.
Brown, Douglas, Huiping Zhao, Bhaskar Reddy Kusuma, et al.. (2013). Development of a High-Throughput Screening Cancer Cell-Based Luciferase Refolding Assay for Identifying Hsp90 Inhibitors. Assay and Drug Development Technologies. 11(8). 478–488. 12 indexed citations
5.
Xu, Wanping, Mehdi Mollapour, Chrisostomos Prodromou, et al.. (2012). Dynamic Tyrosine Phosphorylation Modulates Cycling of the HSP90-P50CDC37-AHA1 Chaperone Machine. Molecular Cell. 47(3). 434–443. 102 indexed citations
6.
Sun, Liang, et al.. (2012). Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823(6). 1092–1101. 30 indexed citations
7.
Hartson, Steven D. & Robert L. Matts. (2011). Approaches for defining the Hsp90-dependent proteome. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823(3). 656–667. 46 indexed citations
8.
Matts, Robert L., Gary Brandt, Yuanming Lu, et al.. (2010). A systematic protocol for the characterization of Hsp90 modulators. Bioorganic & Medicinal Chemistry. 19(1). 684–692. 72 indexed citations
9.
Matthews, Shawna B., George Vielhauer, Robert L. Matts, et al.. (2009). Characterization of a novel novobiocin analogue as a putative C‐terminal inhibitor of heat shock protein 90 in prostate cancer cells. The Prostate. 70(1). 27–36. 40 indexed citations
10.
Matts, Robert L., et al.. (2009). Assays for Identification of Hsp90 Inhibitors and Biochemical Methods for Discriminating their Mechanism of Action. Current Topics in Medicinal Chemistry. 9(15). 1462–1478. 18 indexed citations
11.
Hadden, M. Kyle, et al.. (2008). Synthesis and evaluation of Hsp90 inhibitors that contain the 1,4-naphthoquinone scaffold. Bioorganic & Medicinal Chemistry. 17(2). 634–640. 61 indexed citations
12.
Galam, Lakshmi, M. Kyle Hadden, Zeqiang Ma, et al.. (2007). High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase. Bioorganic & Medicinal Chemistry. 15(5). 1939–1946. 69 indexed citations
13.
Prince, Thomas L. & Robert L. Matts. (2005). Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37. Biochemical and Biophysical Research Communications. 338(3). 1447–1454. 17 indexed citations
14.
Yun, Bo-Geon, Jessica Matts, & Robert L. Matts. (2005). Interdomain interactions regulate the activation of the heme-regulated eIF2α kinase. Biochimica et Biophysica Acta (BBA) - General Subjects. 1725(2). 174–181. 13 indexed citations
15.
Prince, Thomas L., Jieya Shao, Robert L. Matts, & Steven D. Hartson. (2005). Evidence for chaperone heterocomplexes containing both Hsp90 and VCP. Biochemical and Biophysical Research Communications. 331(4). 1331–1337. 15 indexed citations
16.
Yorgin, Peter D., Steven D. Hartson, Bradley T. Scroggins, et al.. (2000). Effects of Geldanamycin, a Heat-Shock Protein 90-Binding Agent, on T Cell Function and T Cell Nonreceptor Protein Tyrosine Kinases. The Journal of Immunology. 164(6). 2915–2923. 44 indexed citations
17.
Lele, Zsolt, Steven D. Hartson, Christian Martin, et al.. (1999). Disruption of Zebrafish Somite Development by Pharmacologic Inhibition of Hsp90. Developmental Biology. 210(1). 56–70. 66 indexed citations
18.
Thulasiraman, Vanitha, et al.. (1998). Evidence that Hsc70 negatively modulates the activation of the heme‐regulated eIF‐2α kinase in rabbit reticulocyte lysate. European Journal of Biochemistry. 255(3). 552–562. 30 indexed citations
19.
Thomas, N. Shaun B., Lu Yu, Jane-Jane Chen, et al.. (1996). Cloning and characterization of cDNAs encoding the ϵ-subunit of eukaryotic initiation factor-2B from rabbit and human. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1307(3). 309–317. 2 indexed citations
20.
Matts, Robert L., et al.. (1996). Cloning and characterization of complementary and genomic DNAs encoding the ϵ-subunit of rat translation initiation factor-2B. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1307(3). 318–324. 12 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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