Stewart H. Lecker

18.3k total citations · 7 hit papers
63 papers, 13.4k citations indexed

About

Stewart H. Lecker is a scholar working on Molecular Biology, Epidemiology and Cell Biology. According to data from OpenAlex, Stewart H. Lecker has authored 63 papers receiving a total of 13.4k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 11 papers in Epidemiology and 11 papers in Cell Biology. Recurrent topics in Stewart H. Lecker's work include Muscle Physiology and Disorders (25 papers), Ubiquitin and proteasome pathways (15 papers) and Genetic Neurodegenerative Diseases (9 papers). Stewart H. Lecker is often cited by papers focused on Muscle Physiology and Disorders (25 papers), Ubiquitin and proteasome pathways (15 papers) and Genetic Neurodegenerative Diseases (9 papers). Stewart H. Lecker collaborates with scholars based in United States, Canada and Italy. Stewart H. Lecker's co-authors include Alfred L. Goldberg, William E. Mitch, R. Thomas Jagoe, Marco Sandri, Marcelo D. Gomes, Stefano Schiaffino, Ami Navon, Carsten Skurk, Kenneth Walsh and Elisa Calabria and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Stewart H. Lecker

61 papers receiving 13.2k citations

Hit Papers

Foxo Transcription Factors Induce the Atrophy-Related Ubi... 1999 2026 2008 2017 2004 2001 2004 2007 2006 500 1000 1.5k 2.0k
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.

  1. Foxo Transcription Factors Induce the Atrophy-Related Ubiquitin Ligase Atrogin-1 and Cause Skeletal Muscle Atrophy
    2004 2.4k citations Marco Sandri, Claudia Sandri et al. Cell profile →
  2. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    2001 1.4k citations Marcelo D. Gomes, Stewart H. Lecker et al. profile →
  3. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    2004 1.3k citations Stewart H. Lecker, R. Thomas Jagoe et al. The FASEB Journal profile →
  4. FoxO3 Coordinately Activates Protein Degradation by the Autophagic/Lysosomal and Proteasomal Pathways in Atrophying Muscle Cells
    2007 1.2k citations Jinghui Zhao, Jeffrey J. Brault et al. Cell Metabolism profile →
  5. Protein Degradation by the Ubiquitin–Proteasome Pathway in Normal and Disease States
    2006 959 citations Stewart H. Lecker, Alfred L. Goldberg et al. Journal of the American Society of Nephrology profile →
  6. PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription
    2006 802 citations Marco Sandri, Stewart H. Lecker et al. profile →
  7. Muscle Protein Breakdown and the Critical Role of the Ubiquitin-Proteasome Pathway in Normal and Disease States
    1999 592 citations Stewart H. Lecker, Vered Solomon et al. Journal of Nutrition profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Stewart H. Lecker United States 37 10.5k 4.2k 2.9k 1.8k 1.7k 63 13.4k
Scot R. Kimball United States 78 11.7k 1.1× 4.8k 1.1× 7.2k 2.5× 1.5k 0.8× 1.4k 0.9× 308 18.6k
John C. Lawrence United States 65 12.6k 1.2× 3.0k 0.7× 2.9k 1.0× 1.1k 0.6× 567 0.3× 149 16.6k
Denis C. Guttridge United States 61 10.4k 1.0× 5.2k 1.2× 1.0k 0.3× 1.0k 0.6× 1.1k 0.7× 146 16.8k
R. Sanders Williams United States 63 9.4k 0.9× 2.9k 0.7× 1.6k 0.6× 566 0.3× 821 0.5× 135 13.3k
Wenli Yang China 33 5.7k 0.5× 5.1k 1.2× 836 0.3× 2.2k 1.2× 793 0.5× 100 10.7k
Matthias Gaestel Germany 70 11.6k 1.1× 1.5k 0.3× 2.1k 0.7× 865 0.5× 356 0.2× 259 16.7k
Martin Steinhoff United States 77 3.0k 0.3× 3.6k 0.9× 1.5k 0.5× 1.4k 0.8× 742 0.4× 280 20.5k
Ormond A. MacDougald United States 70 13.2k 1.3× 6.7k 1.6× 1.3k 0.4× 4.9k 2.7× 359 0.2× 170 22.8k
Darren J. Baker United States 45 8.6k 0.8× 8.1k 1.9× 1.9k 0.7× 1.6k 0.9× 198 0.1× 81 17.9k
Silvia Corvera United States 53 5.7k 0.5× 3.6k 0.9× 2.8k 1.0× 2.2k 1.2× 213 0.1× 123 10.2k

Countries citing papers authored by Stewart H. Lecker

Since Specialization
Citations

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

Fields of papers citing papers by Stewart H. Lecker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Stewart H. Lecker. 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 Stewart H. Lecker. The network helps show where Stewart H. Lecker may publish in the future.

Co-authorship network of co-authors of Stewart H. Lecker

This figure shows the co-authorship network connecting the top 25 collaborators of Stewart H. Lecker. A scholar is included among the top collaborators of Stewart H. Lecker 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 Stewart H. Lecker. Stewart H. Lecker 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.
Lecker, Stewart H., et al.. (2025). Metabolic Acidosis. PubMed. 32(1). 61–68. 1 indexed citations
2.
Lecker, Stewart H., et al.. (2023). Acid Base Disorders in Cirrhosis. PubMed. 30(4). 336–342. 2 indexed citations
3.
Hoenig, Melanie P., et al.. (2022). More than meets the I(ris): Use of manual urine microscopy to complement automated findings in acute kidney injury. Practical Laboratory Medicine. 29. e00267–e00267.
4.
Zhuo, Min, et al.. (2019). Brugada phenocopy induced by hyperkalemia. Kidney International. 95(2). 471–471. 3 indexed citations
5.
Forman, Daniel E., Karla M. Daniels, Lawrence P. Cahalin, et al.. (2014). Analysis of Skeletal Muscle Gene Expression Patterns and the Impact of Functional Capacity in Patients With Systolic Heart Failure. Journal of Cardiac Failure. 20(6). 422–430. 20 indexed citations
6.
Lecker, Stewart H. & William E. Mitch. (2011). Proteolysis by the Ubiquitin-Proteasome System and Kidney Disease. Journal of the American Society of Nephrology. 22(5). 821–824. 19 indexed citations
7.
Phillips, Paul S, M. Anthony Verity, Reijo Laaksonen, et al.. (2010). Survey of muscle characteristics after statin-induced rhabdomyolysis. Clinical Lipidology. 5(1). 17–27. 3 indexed citations
8.
Smith, Ira J., Stewart H. Lecker, & Per-Olof Hasselgren. (2008). Calpain activity and muscle wasting in sepsis. American Journal of Physiology-Endocrinology and Metabolism. 295(4). E762–E771. 102 indexed citations
9.
Zhao, Jinghui, Jeffrey J. Brault, Andreas Schild, et al.. (2007). FoxO3 Coordinately Activates Protein Degradation by the Autophagic/Lysosomal and Proteasomal Pathways in Atrophying Muscle Cells. Cell Metabolism. 6(6). 472–483. 1206 indexed citations breakdown →
10.
Hanai, Jun‐ichi, Peirang Cao, Shintaro Imamura, et al.. (2007). The muscle-specific ubiquitin ligase atrogin-1/MAFbx mediates statin-induced muscle toxicity. Journal of Clinical Investigation. 117(12). 3940–51. 230 indexed citations
11.
Bdolah, Yuval, et al.. (2006). Atrophy-related ubiquitin ligases atrogin-1 and MuRF-1 are associated with uterine smooth muscle involution in the postpartum period. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 292(2). R971–R976. 24 indexed citations
12.
Sandri, Marco, Claudia Sandri, Carsten Skurk, et al.. (2004). Foxo Transcription Factors Induce the Atrophy-Related Ubiquitin Ligase Atrogin-1 and Cause Skeletal Muscle Atrophy. Cell. 117(3). 399–412. 2354 indexed citations breakdown →
13.
Lecker, Stewart H.. (2003). Ubiquitin-protein ligases in muscle wasting: multiple parallel pathways?. Current Opinion in Clinical Nutrition & Metabolic Care. 6(3). 271–275. 56 indexed citations
14.
Jagoe, R. Thomas, Stewart H. Lecker, Marcelo D. Gomes, & Alfred L. Goldberg. (2002). Patterns of gene expression in atrophying skeletal muscles: response to food deprivation. The FASEB Journal. 16(13). 1697–1712. 274 indexed citations
15.
Gao, Youhe, Stewart H. Lecker, Mark J. Post, et al.. (2000). Inhibition of ubiquitin-proteasome pathway–mediated IκBα degradation by a naturally occurring antibacterial peptide. Journal of Clinical Investigation. 106(3). 439–448. 139 indexed citations
16.
Lecker, Stewart H., Vered Solomon, William E. Mitch, & Alfred L. Goldberg. (1999). Muscle Protein Breakdown and the Critical Role of the Ubiquitin-Proteasome Pathway in Normal and Disease States. Journal of Nutrition. 129(1). 227S–237S. 592 indexed citations breakdown →
17.
Solomon, Vered, Stewart H. Lecker, & Alfred L. Goldberg. (1998). The N-end Rule Pathway Catalyzes a Major Fraction of the Protein Degradation in Skeletal Muscle. Journal of Biological Chemistry. 273(39). 25216–25222. 117 indexed citations
18.
Hartl, F. Ulrich, et al.. (1990). The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane. Cell. 63(2). 269–279. 477 indexed citations
19.
Lecker, Stewart H., David I. Meyer, & William Wickner. (1989). Export of Prepro-α-factor from Escherichia coli. Journal of Biological Chemistry. 264(3). 1882–1886. 3 indexed citations
20.
Crooke, Elliott, Brenda Guthrie, Stewart H. Lecker, Roland Lill, & William Wickner. (1988). ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle. Cell. 54(7). 1003–1011. 170 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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