Mary E. Matyskiela

3.6k total citations · 1 hit paper
21 papers, 1.8k citations indexed

About

Mary E. Matyskiela is a scholar working on Molecular Biology, Cell Biology and Oncology. According to data from OpenAlex, Mary E. Matyskiela has authored 21 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 8 papers in Cell Biology and 6 papers in Oncology. Recurrent topics in Mary E. Matyskiela's work include Ubiquitin and proteasome pathways (15 papers), Protein Degradation and Inhibitors (8 papers) and Peptidase Inhibition and Analysis (6 papers). Mary E. Matyskiela is often cited by papers focused on Ubiquitin and proteasome pathways (15 papers), Protein Degradation and Inhibitors (8 papers) and Peptidase Inhibition and Analysis (6 papers). Mary E. Matyskiela collaborates with scholars based in United States, Switzerland and Russia. Mary E. Matyskiela's co-authors include Andreas Martin, Gabriel C. Lander, Charlene Bashore, Eva Nogales, Eric Estrin, David O. Morgan, Philip P. Chamberlain, David P. Toczyski, Gang Lu and Christopher W. Carroll and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Mary E. Matyskiela

21 papers receiving 1.8k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Complete subunit architecture of the proteasome regulatory particle

2012 482 citations Gabriel C. Lander, Eric Estrin et al. Nature profile →

Peers

Countries citing papers authored by Mary E. Matyskiela

Since Specialization

Citations

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

Fields of papers citing papers by Mary E. Matyskiela

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mary E. Matyskiela. 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 Mary E. Matyskiela. The network helps show where Mary E. Matyskiela may publish in the future.

Co-authorship network of co-authors of Mary E. Matyskiela

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

All Works

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20 of 20 papers shown

#	Work	Indexed citations
1	Molecular glue CELMoD compounds are regulators of cereblon conformation 2022 ·Science ·Edmond R. Watson, Scott J. Novick, Mary E. Matyskiela, Philip P. Chamberlain, Andres H. de la Peña, J. Zhu, Eileen Tran, Patrick R. Griffin, Ingrid E. Wertz, Gabriel C. Lander	94
2	Profiling CELMoD-Mediated Degradation of Cereblon Neosubstrates 2021 ·Methods in molecular biology ·Joel W. Thompson, Thomas Clayton, Gody Khambatta, Leslie A. Bateman, Christopher W. Carroll, Philip P. Chamberlain, Mary E. Matyskiela	4
3	Crystal structure of the SALL4–pomalidomide–cereblon–DDB1 complex 2020 ·Nature Structural & Molecular Biology ·Mary E. Matyskiela, Thomas Clayton, Xinde Zheng, Christopher G. Mayne, Eileen Tran, (unknown), Barbra Pagarigan, Joseph J. McDonald, Mark Rolfe, Lawrence G. Hamann, Gang Lu, Philip P. Chamberlain	65
4	Cereblon Modulators Target ZBTB16 and Its Oncogenic Fusion Partners for Degradation via Distinct Structural Degrons 2020 ·ACS Chemical Biology ·Mary E. Matyskiela, J. Zhu, Joshua M. Baughman, Thomas Clayton, (unknown), Hon Kit Wong, (unknown), Xinde Zheng, Mark Labow, Laurie A. LeBrun, Gang Lu, Philip P. Chamberlain, Joel W. Thompson	30
5	Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation 2019 ·eLife ·Eric R. Greene, Ellen A. Goodall, Andres H. de la Peña, Mary E. Matyskiela, Gabriel C. Lander, Andreas Martin	19
6	CC-92480 Is a Novel Cereblon E3 Ligase Modulator with Enhanced Tumoricidal and Immunomodulatory Activity Against Sensitive and Resistant Multiple Myeloma Cells 2019 ·Blood ·Antonia Lopez‐Girona, Courtney G. Havens, Gang Lu, Emily Rychak, Derek Mendy, (unknown), Christine Surka, Chin-Chun Lu, Mary E. Matyskiela, Gody Khambatta, Lilly Wong, Joshua D. Hansen, Daniel W. Pierce, Brian E. Cathers, James Carmichael	18
7	Evolution of Cereblon-Mediated Protein Degradation as a Therapeutic Modality 2019 ·ACS Medicinal Chemistry Letters ·Philip P. Chamberlain, (unknown), J. Michael Ellis, Joshua D. Hansen, Mary E. Matyskiela, Joseph J. McDonald, Jennifer R. Riggs, Lawrence G. Hamann	47
8	UBE2G1 governs the destruction of cereblon neomorphic substrates 2018 ·eLife ·Gang Lu, (unknown), Mary E. Matyskiela, Xinde Zheng, (unknown), Scott Wood, Christine Surka, (unknown), Chin-Chun Lu, Derek Mendy, In Sock Jang, Kai Wang, Mathieu Marella, Suzana S. Couto, Brian E. Cathers, James Carmichael, Philip P. Chamberlain, Mark Rolfe	56
9	A Cereblon Modulator (CC-220) with Improved Degradation of Ikaros and Aiolos 2017 ·Journal of Medicinal Chemistry ·Mary E. Matyskiela, Weihong Zhang, Hon‐Wah Man, George W. Muller, Godrej Khambatta, (unknown), Matthew Hickman, Laurie A. LeBrun, Barbra Pagarigan, Gilles Carmel, Chin-Chun Lu, Gang Lu, Mariko Riley, Yoshitaka Satoh, Peter Schäfer, Thomas O. Daniel, James Carmichael, Brian E. Cathers, Philip P. Chamberlain	203
10	Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome 2015 ·Nature Structural & Molecular Biology ·Charlene Bashore, Corey M. Dambacher, Ellen A. Goodall, Mary E. Matyskiela, Gabriel C. Lander, Andreas Martin	97
11	Conformational switching of the 26S proteasome enables substrate degradation 2013 ·Nature Structural & Molecular Biology ·Mary E. Matyskiela, Gabriel C. Lander, Andreas Martin	199
12	Complete subunit architecture of the proteasome regulatory particle breakdown → 2012 ·Nature ·Gabriel C. Lander, Eric Estrin, Mary E. Matyskiela, Charlene Bashore, Eva Nogales, Andreas Martin	482
13	Design Principles of a Universal Protein Degradation Machine 2012 ·Journal of Molecular Biology ·Mary E. Matyskiela, Andreas Martin	47
14	Functionally Distinct Isoforms of Cik1 Are Differentially Regulated by APC/C-Mediated Proteolysis 2009 ·Molecular Cell ·Jennifer A. Benanti, Mary E. Matyskiela, David O. Morgan, David P. Toczyski	26
15	Analysis of Activator-Binding Sites on the APC/C Supports a Cooperative Substrate-Binding Mechanism 2009 ·Molecular Cell ·Mary E. Matyskiela, David O. Morgan	86
16	Mechanisms of ubiquitin transfer by the anaphase-promoting complex 2009 ·Journal of Biology ·Mary E. Matyskiela, Monica C. Rodrigo-Brenni, David O. Morgan	25
17	An architectural map of the anaphase-promoting complex 2006 ·Genes & Development ·(unknown), (unknown), Mary E. Matyskiela, Christopher W. Carroll, David O. Morgan, David P. Toczyski	126
18	Targeted gene disruption of methionine aminopeptidase 2 results in an embryonic gastrulation defect and endothelial cell growth arrest 2006 ·Proceedings of the National Academy of Sciences ·Jing-Ruey Joanna Yeh, Rong Ju, Cathleen Brdlik, Wenjun Zhang, Yi Zhang, Mary E. Matyskiela, (unknown), Craig M. Crews	46
19	Identification of a New Class of Inhibitors of the Voltage-Gated Potassium Channel, K_v1.3, with Immunosuppressant Properties 2002 ·Biochemistry ·William A. Schmalhofer, Jianming Bao, Owen B. McManus, Brian Green, Mary E. Matyskiela, (unknown), Randal M. Bugianesi, John P. Felix, Markus Hanner, (unknown), (unknown), (unknown), Gloria C. Koo, Mary Jo Staruch, (unknown), William H. Parsons, Kathleen M. Rupprecht, Robert S. Slaughter, Gregory J. Kaczorowski, María L. García	54
20	Binding of Correolide to the K_v1.3 Potassium Channel: Characterization of the Binding Domain by Site-Directed Mutagenesis 2001 ·Biochemistry ·Markus Hanner, Brian Green, Ying‐Duo Gao, William A. Schmalhofer, Mary E. Matyskiela, Daniel J. Durand, John P. Felix, (unknown), Carmen Bordallo, Gregory J. Kaczorowski, Martin Köhler, María L. García	40

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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