John E. Bylander

712 total citations
23 papers, 545 citations indexed

About

John E. Bylander is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Health, Toxicology and Mutagenesis. According to data from OpenAlex, John E. Bylander has authored 23 papers receiving a total of 545 indexed citations (citations by other indexed papers that have themselves been cited), including 5 papers in Molecular Biology, 4 papers in Cellular and Molecular Neuroscience and 4 papers in Health, Toxicology and Mutagenesis. Recurrent topics in John E. Bylander's work include Protease and Inhibitor Mechanisms (4 papers), Heavy Metal Exposure and Toxicity (4 papers) and Trace Elements in Health (3 papers). John E. Bylander is often cited by papers focused on Protease and Inhibitor Mechanisms (4 papers), Heavy Metal Exposure and Toxicity (4 papers) and Trace Elements in Health (3 papers). John E. Bylander collaborates with scholars based in United States and United Kingdom. John E. Bylander's co-authors include Judith Bond, Greg P. Bertenshaw, Gary A. Clawson, Nuray Erin, Wei Zhao, Gary A. Chase, Donald A. Sens, Simon J. Hubbard, William Reeves and Gail L. Matters and has published in prestigious journals such as Journal of Biological Chemistry, Diabetes and Biochemical and Biophysical Research Communications.

In The Last Decade

John E. Bylander

23 papers receiving 538 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John E. Bylander United States 13 183 97 79 67 59 23 545
Gin‐Fu Chen United States 13 205 1.1× 30 0.3× 80 1.0× 49 0.7× 164 2.8× 21 610
Masayo Yamagata Japan 15 376 2.1× 126 1.3× 50 0.6× 29 0.4× 71 1.2× 28 758
Priya Raman United States 16 309 1.7× 75 0.8× 59 0.7× 38 0.6× 38 0.6× 21 603
SS Shasby United States 6 283 1.5× 48 0.5× 20 0.3× 77 1.1× 54 0.9× 7 640
Masako Nakanishi Japan 14 325 1.8× 127 1.3× 117 1.5× 73 1.1× 36 0.6× 34 699
Emilio Chiosi Italy 17 452 2.5× 81 0.8× 171 2.2× 95 1.4× 31 0.5× 35 802
E Kökoğlu Türkiye 12 154 0.8× 65 0.7× 31 0.4× 32 0.5× 39 0.7× 22 347
María Magdalena Vilchis‐Landeros Mexico 13 465 2.5× 79 0.8× 102 1.3× 38 0.6× 29 0.5× 20 791
Vijayalakshmi Thamilselvan United States 18 518 2.8× 106 1.1× 187 2.4× 149 2.2× 34 0.6× 31 995
Lixiang Yang China 16 322 1.8× 89 0.9× 45 0.6× 43 0.6× 38 0.6× 34 633

Countries citing papers authored by John E. Bylander

Since Specialization
Citations

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

Fields of papers citing papers by John E. Bylander

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John E. Bylander

This figure shows the co-authorship network connecting the top 25 collaborators of John E. Bylander. A scholar is included among the top collaborators of John E. Bylander 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 John E. Bylander. John E. Bylander 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.
Bylander, John E., et al.. (2017). Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes. Journal of Diabetes Research. 2017. 1–11. 11 indexed citations
2.
Wang, Hui, et al.. (2010). Quantitative analysis of creatinine in urine by metalized nanostructured parylene. Journal of Biomedical Optics. 15(2). 27004–27004. 43 indexed citations
3.
Bylander, John E., Qing Li, Ganesan Ramesh, et al.. (2008). Targeted disruption of the meprin metalloproteinase β gene protects against renal ischemia-reperfusion injury in mice. American Journal of Physiology-Renal Physiology. 294(3). F480–F490. 41 indexed citations
4.
Erin, Nuray, Wei Zhao, John E. Bylander, Gary A. Chase, & Gary A. Clawson. (2006). Capsaicin-induced inactivation of sensory neurons promotes a more aggressive gene expression phenotype in breast cancer cells. Breast Cancer Research and Treatment. 99(3). 351–364. 81 indexed citations
5.
Mathew, Roy O., Stephen Futterweit, Elsa Valderrama, et al.. (2005). Meprin-α in chronic diabetic nephropathy: interaction with the renin-angiotensin axis. American Journal of Physiology-Renal Physiology. 289(4). F911–F921. 23 indexed citations
6.
Bertenshaw, Greg P., et al.. (2003). Meprin proteolytic complexes at the cell surface and in extracellular spaces. Biochemical Society Symposia. 70(70). 53–63. 27 indexed citations
7.
Bertenshaw, Greg P., Benjamin E. Turk, Simon J. Hubbard, et al.. (2001). Marked Differences between Metalloproteases Meprin A and B in Substrate and Peptide Bond Specificity. Journal of Biological Chemistry. 276(16). 13248–13255. 93 indexed citations
8.
Castranova, Vincent, Linda J. Huffman, John E. Bylander, et al.. (1998). Enhancement of nitric oxide production by pulmonary cells following silica exposure.. Environmental Health Perspectives. 106(suppl 5). 1165–1169. 49 indexed citations
9.
Gordon, John, John E. Bylander, Dale W. Porter, et al.. (1998). Silica-Induced Pulmonary Inflammation in Rats: Activation of NF-κB and Its Suppression by Dexamethasone. Biochemical and Biophysical Research Communications. 253(1). 181–184. 40 indexed citations
10.
Bylander, John E., Shuli Li, Mary Ann Sens, & Donald A. Sens. (1995). Exposure of human proximal tubule cells to cytotoxic levels of CdCl2 induces the additional expression of metallothionein 1A mRNA. Toxicology Letters. 76(3). 209–217. 9 indexed citations
11.
Bylander, John E., S LI, Mary Ann Sens, et al.. (1994). Induction of metallothionein mRNA and protein following exposure of cultured human proximal tubule cells to cadmium. Toxicology Letters. 71(2). 111–122. 8 indexed citations
12.
Smyth, Brendan, et al.. (1994). Selective exposure of human proximal tubule cells to gentamicin provides evidence for a basolateral component of toxicity. Toxicology Letters. 74(1). 1–13. 1 indexed citations
13.
Sens, Mary Ann, Debra J. Hazen‐Martin, John E. Bylander, & Donald A. Sens. (1994). Heterogeneity in the amount of ionic cadmium necessary to elicit cell death in independent cultures of human proximal tubule cells. Toxicology Letters. 70(2). 185–191. 4 indexed citations
14.
Hazen‐Martin, Debra J., Betty I. Tarnowski, John H. Todd, et al.. (1994). Serum-free culture and characterization of renal epithelial cells isolated from human fetal kidneys of varying gestational age. In Vitro Cellular & Developmental Biology - Animal. 30(6). 356–365. 8 indexed citations
15.
Todd, John H., Mary Ann Sens, Debra J. Hazen‐Martin, et al.. (1993). Variation in the electrical properties of cultured human proximal tubule cells. In Vitro Cellular & Developmental Biology - Animal. 29(5). 371–378. 15 indexed citations
16.
Hazen‐Martin, Debra J., J H Todd, Mary Ann Sens, et al.. (1993). Electrical and freeze-fracture analysis of the effects of ionic cadmium on cell membranes of human proximal tubule cells.. Environmental Health Perspectives. 101(6). 510–516. 18 indexed citations
17.
Hazen‐Martin, Debra J., John H. Todd, Mary Ann Sens, et al.. (1993). Electrical and Freeze-Fracture Analysis of the Effects of Ionic Cadmium on Cell Membranes of Human Proximal Tubule Cells. Environmental Health Perspectives. 101(6). 510–510. 1 indexed citations
18.
Petrash, J. Mark, et al.. (1992). Effects of osmotic stress and hyperglycemia on aldose reductase gene expression in human renal proximal tubule cells. Biochemical and Biophysical Research Communications. 187(1). 201–208. 24 indexed citations
19.
Bylander, John E., et al.. (1992). Variation in Sorbitol Accumulation and Polyol-Pathway Activity in Cultured Human Proximal Tubule Cells. Diabetes. 41(9). 1050–1055. 12 indexed citations
20.
Bylander, John E. & Donald A. Sens. (1990). Elicitation of Sorbitol Accumulation in Cultured Human Proximal Tubule Cells by Elevated Glucose Concentrations. Diabetes. 39(8). 949–954. 9 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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