Laszlo Gyenis

1.4k total citations
33 papers, 962 citations indexed

About

Laszlo Gyenis is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, Laszlo Gyenis has authored 33 papers receiving a total of 962 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 7 papers in Oncology and 6 papers in Cell Biology. Recurrent topics in Laszlo Gyenis's work include Protein Kinase Regulation and GTPase Signaling (10 papers), Cancer-related Molecular Pathways (5 papers) and Wheat and Barley Genetics and Pathology (4 papers). Laszlo Gyenis is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (10 papers), Cancer-related Molecular Pathways (5 papers) and Wheat and Barley Genetics and Pathology (4 papers). Laszlo Gyenis collaborates with scholars based in Canada, United States and Poland. Laszlo Gyenis's co-authors include David W. Litchfield, James S. Duncan, Brian J. Steffenson, Song Joong Yun, Kevin P. Smith, Gary J. Muehlbauer, Maria Bretner, Patrick M. Hayes, Silvia Peñuela and Iván Matus and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Journal of Clinical Oncology.

In The Last Decade

Laszlo Gyenis

31 papers receiving 951 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Laszlo Gyenis Canada 19 639 201 122 116 93 33 962
Hyeung Kim United States 15 1.1k 1.6× 131 0.7× 73 0.6× 86 0.7× 66 0.7× 19 1.3k
Gregory P. Donoho United States 17 698 1.1× 98 0.5× 236 1.9× 168 1.4× 74 0.8× 32 1000
Hans‐Dieter Pohlenz Germany 19 817 1.3× 116 0.6× 76 0.6× 112 1.0× 58 0.6× 29 1.3k
David E. Hanna United States 14 898 1.4× 127 0.6× 179 1.5× 132 1.1× 196 2.1× 22 1.1k
Cheng Du United States 18 804 1.3× 68 0.3× 170 1.4× 63 0.5× 109 1.2× 37 1000
Mirta Mittelstedt Leal de Sousa Norway 20 977 1.5× 79 0.4× 151 1.2× 104 0.9× 57 0.6× 37 1.2k
Jun Seop Jeong United States 11 734 1.1× 141 0.7× 123 1.0× 50 0.4× 110 1.2× 17 977
Ioannis Michalopoulos Greece 19 796 1.2× 229 1.1× 95 0.8× 108 0.9× 32 0.3× 52 1.2k
Jocelyn H. Wright United States 13 869 1.4× 107 0.5× 229 1.9× 64 0.6× 175 1.9× 17 1.2k
Nozomu Hibi Japan 15 526 0.8× 174 0.9× 141 1.2× 37 0.3× 66 0.7× 46 901

Countries citing papers authored by Laszlo Gyenis

Since Specialization
Citations

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

Fields of papers citing papers by Laszlo Gyenis

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Laszlo Gyenis

This figure shows the co-authorship network connecting the top 25 collaborators of Laszlo Gyenis. A scholar is included among the top collaborators of Laszlo Gyenis 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 Laszlo Gyenis. Laszlo Gyenis 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.
Gyenis, Laszlo, Pilar Sepúlveda, Fabrice Duprat, et al.. (2024). Casein kinase 2 phosphorylates and induces the SALL2 tumor suppressor degradation in colon cancer cells. Cell Death and Disease. 15(3). 223–223. 5 indexed citations
2.
Guerra, Bárbara, Thomas Koed Doktor, Aarif Siddiqui, et al.. (2024). Protein kinase CK2 sustains de novo fatty acid synthesis by regulating the expression of SCD-1 in human renal cancer cells. Cancer Cell International. 24(1). 432–432.
3.
Litchfield, David W., et al.. (2023). Towards the CSNK2 phosphoproteome – With lessons from the COVID-19 pandemic to revealing the secrets of CSNK2 and its promise as a therapeutic target. Biochimica et Biophysica Acta (BBA) - General Subjects. 1867(10). 130441–130441. 1 indexed citations
4.
Reinecke, Maria, P. Brear, Larsen Vornholz, et al.. (2023). Chemical proteomics reveals the target landscape of 1,000 kinase inhibitors. Nature Chemical Biology. 20(5). 577–585. 35 indexed citations
5.
Gyenis, Laszlo, Predrag Jovanović, Krzysztof J. Szkop, et al.. (2023). Comparison of CX-4945 and SGC-CK2-1 as inhibitors of CSNK2 using quantitative phosphoproteomics: Triple SILAC in combination with inhibitor-resistant CSNK2. PubMed. 3. 100041–100041. 8 indexed citations
6.
Gyenis, Laszlo, et al.. (2022). Chemical Genetic Validation of CSNK2 Substrates Using an Inhibitor-Resistant Mutant in Combination with Triple SILAC Quantitative Phosphoproteomics. Frontiers in Molecular Biosciences. 9. 909711–909711. 8 indexed citations
7.
Strum, Scott, Laszlo Gyenis, & David W. Litchfield. (2021). CSNK2 in cancer: pathophysiology and translational applications. British Journal of Cancer. 126(7). 994–1003. 29 indexed citations
8.
Wells, Carrow I., David H. Drewry, Julie E. Pickett, et al.. (2021). Development of a potent and selective chemical probe for the pleiotropic kinase CK2. Cell chemical biology. 28(4). 546–558.e10. 68 indexed citations
9.
Gandin, Valentina, Laìa Masvidal, Marie Cargnello, et al.. (2016). mTORC1 and CK2 coordinate ternary and eIF4F complex assembly. Nature Communications. 7(1). 11127–11127. 73 indexed citations
10.
Litchfield, David W., Brian H. Shilton, Christopher J. Brandl, & Laszlo Gyenis. (2015). Pin1: Intimate involvement with the regulatory protein kinase networks in the global phosphorylation landscape. Biochimica et Biophysica Acta (BBA) - General Subjects. 1850(10). 2077–2086. 19 indexed citations
11.
Innes, Brendan T., Modupeola A. Sowole, Laszlo Gyenis, et al.. (2015). Peroxide-mediated oxidation and inhibition of the peptidyl-prolyl isomerase Pin1. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1852(5). 905–912. 19 indexed citations
12.
Tse, Wai Hei, Laszlo Gyenis, David W. Litchfield, & Jin Zhang. (2014). Engineering large gelatin nanospheres coated with quantum dots for targeted delivery of human osteosarcoma with enhanced cellular internalization. 672–677. 3 indexed citations
13.
Gyenis, Laszlo, Jacob P. Turowec, Maria Bretner, & David W. Litchfield. (2013). Chemical proteomics and functional proteomics strategies for protein kinase inhibitor validation and protein kinase substrate identification: Applications to protein kinase CK2. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(7). 1352–1358. 11 indexed citations
14.
15.
Peñuela, Silvia, Laszlo Gyenis, Amber Ablack, et al.. (2012). Loss of Pannexin 1 Attenuates Melanoma Progression by Reversion to a Melanocytic Phenotype. Journal of Biological Chemistry. 287(34). 29184–29193. 88 indexed citations
16.
Turowec, Jacob P., James S. Duncan, Laszlo Gyenis, et al.. (2010). Protein Kinase CK2 is a Constitutively Active Enzyme that Promotes Cell Survival: Strategies to Identify CK2 Substrates and Manipulate its Activity in Mammalian Cells. Methods in enzymology on CD-ROM/Methods in enzymology. 484. 471–493. 55 indexed citations
17.
Duncan, James S., Laszlo Gyenis, John Lenehan, et al.. (2008). An Unbiased Evaluation of CK2 Inhibitors by Chemoproteomics. Molecular & Cellular Proteomics. 7(6). 1077–1088. 71 indexed citations
18.
Gyenis, Laszlo & David W. Litchfield. (2008). The emerging CK2 interactome: insights into the regulation and functions of CK2. Molecular and Cellular Biochemistry. 316(1-2). 5–14. 22 indexed citations
19.
Zhu, Hong, et al.. (2006). Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves. Transgenic Research. 16(2). 239–249. 78 indexed citations
20.
Yun, Song Joong, Laszlo Gyenis, Eligio Bossolini, et al.. (2006). Validation of Quantitative Trait Loci for Multiple Disease Resistance in Barley Using Advanced Backcross Lines Developed with a Wild Barley. Crop Science. 46(3). 1179–1186. 42 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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