Emer S. Ferro

5.0k total citations
107 papers, 3.1k citations indexed

About

Emer S. Ferro is a scholar working on Molecular Biology, Oncology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Emer S. Ferro has authored 107 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 69 papers in Molecular Biology, 58 papers in Oncology and 42 papers in Cellular and Molecular Neuroscience. Recurrent topics in Emer S. Ferro's work include Peptidase Inhibition and Analysis (57 papers), Neuropeptides and Animal Physiology (34 papers) and Ubiquitin and proteasome pathways (24 papers). Emer S. Ferro is often cited by papers focused on Peptidase Inhibition and Analysis (57 papers), Neuropeptides and Animal Physiology (34 papers) and Ubiquitin and proteasome pathways (24 papers). Emer S. Ferro collaborates with scholars based in Brazil, United States and United Kingdom. Emer S. Ferro's co-authors include Leandro M. Castro, Vanessa Rioli, Antônio Carlos Martins de Camargo, Lloyd D. Fricker, Andrea S. Heimann, Fábio C. Gozzo, Lakshmi A. Devi, Ivone Gomes, Stephen Hyslop and Camila Squarzoni Dale and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and SHILAP Revista de lepidopterología.

In The Last Decade

Emer S. Ferro

105 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Emer S. Ferro Brazil	34	1.9k	1.0k	984	470	387	107	3.1k
Kristen L. Pierce United States	25	5.1k 2.7×	634 0.6×	2.5k 2.5×	635 1.4×	537 1.4×	36	6.5k
Hervé Enslen France	30	3.6k 1.9×	545 0.5×	1.8k 1.8×	404 0.9×	402 1.0×	47	5.2k
Hiroshi Tokumitsu Japan	40	4.5k 2.4×	485 0.5×	1.3k 1.3×	164 0.3×	580 1.5×	117	6.1k
William N. Green United States	36	3.5k 1.9×	292 0.3×	1.5k 1.5×	234 0.5×	426 1.1×	59	4.4k
Avraham Yaron Israel	37	2.7k 1.4×	1.0k 1.0×	1.9k 1.9×	122 0.3×	298 0.8×	74	5.1k
Yasuji Furutani Japan	23	3.1k 1.6×	305 0.3×	2.0k 2.0×	206 0.4×	468 1.2×	34	4.9k
Toshiro Kumanishi Japan	31	2.9k 1.5×	409 0.4×	2.7k 2.8×	93 0.2×	513 1.3×	126	4.9k
Jong‐Ik Hwang South Korea	33	2.6k 1.3×	416 0.4×	892 0.9×	194 0.4×	272 0.7×	110	4.2k
Isamu Kameshita Japan	25	2.2k 1.2×	460 0.5×	407 0.4×	97 0.2×	141 0.4×	114	2.8k
James E. Garrett United States	30	2.1k 1.1×	308 0.3×	559 0.6×	146 0.3×	248 0.6×	51	3.1k

Countries citing papers authored by Emer S. Ferro

Since Specialization

Citations

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

Fields of papers citing papers by Emer S. Ferro

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Emer S. Ferro. 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 Emer S. Ferro. The network helps show where Emer S. Ferro may publish in the future.

Co-authorship network of co-authors of Emer S. Ferro

This figure shows the co-authorship network connecting the top 25 collaborators of Emer S. Ferro. A scholar is included among the top collaborators of Emer S. Ferro 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 Emer S. Ferro. Emer S. Ferro 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

Eichler, Rosangela Aparecida dos Santos, et al.. (2024). Methods for Intracellular Peptidomic Analysis. Methods in molecular biology. 2758. 199–212.

Oliveira, Ivan Pires de, João Agostinho Machado‐Neto, Rosangela Aparecida dos Santos Eichler, et al.. (2022). Effect of FKBP12-Derived Intracellular Peptides on Rapamycin-Induced FKBP–FRB Interaction and Autophagy. Cells. 11(3). 385–385. 7 indexed citations

Camargo, Lívia L., Alexandre Denadai‐Souza, Lidia Yshii, et al.. (2020). The potential anti-inflammatory and anti-nociceptive effects of rat hemopressin (PVNFKFLSH) in experimental arthritis. European Journal of Pharmacology. 890. 173636–173636. 5 indexed citations

Iwai, Leo Kei, et al.. (2019). Characterization of Intracellular Peptides from Zebrafish ( Danio rerio ) Brain. Zebrafish. 16(3). 240–251. 15 indexed citations

Heimann, Andrea S., Achla Gupta, Ivone Gomes, et al.. (2017). Generation of G protein-coupled receptor antibodies differentially sensitive to conformational states. PLoS ONE. 12(11). e0187306–e0187306. 9 indexed citations

Reckziegel, Patrícia, William T. Festuccia, Luiz R.G. Britto, et al.. (2017). A novel peptide that improves metabolic parameters without adverse central nervous system effects. Scientific Reports. 7(1). 14781–14781. 19 indexed citations

Rossato, Cristiano, Lilian C. Russo, Leandro M. Castro, et al.. (2016). Interferon-gamma activity is potentiated by an intracellular peptide derived from the human 19S ATPase regulatory subunit 4 of the proteasome. Journal of Proteomics. 151. 74–82. 11 indexed citations

Ferro, Emer S., et al.. (2014). Using Mass Spectrometry-Based Peptidomics to understand the Brain and Disorders such as Parkinson’s Disease and Schizophrenia. Current Topics in Medicinal Chemistry. 14(3). 369–381. 11 indexed citations

Fogaça, Manoela V., Andreza Buzolin Sonego, Vanessa Rioli, et al.. (2014). Anxiogenic-like effects induced by hemopressin in rats. Pharmacology Biochemistry and Behavior. 129. 7–13. 30 indexed citations

10.

Gelman, Julia S., Juan Sironi, Leandro M. Castro, Emer S. Ferro, & Lloyd D. Fricker. (2010). Hemopressins and other hemoglobin‐derived peptides in mouse brain: comparison between brain, blood, and heart peptidome and regulation in Cpe^fat/fat mice. Journal of Neurochemistry. 113(4). 871–880. 54 indexed citations

11.

Gomes, Ivone, Camila Squarzoni Dale, Fábio C. Gozzo, et al.. (2010). Hemoglobin-derived Peptides as Novel Type of Bioactive Signaling Molecules. The AAPS Journal. 12(4). 658–669. 95 indexed citations

12.

Berti, Denise A., Lilian C. Russo, Leandro M. Castro, et al.. (2009). Analysis of Intracellular Substrates and Products of Thimet Oligopeptidase in Human Embryonic Kidney 293 Cells. Journal of Biological Chemistry. 284(21). 14105–14116. 56 indexed citations

13.

Rioli, Vanessa, Benedito C. Prezoto, Katsuhiro Konno, et al.. (2008). A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15. FEBS Journal. 275(10). 2442–2454. 27 indexed citations

14.

Demasi, Marilene, et al.. (2007). Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation. Free Radical Biology and Medicine. 44(6). 1180–1190. 26 indexed citations

15.

Oliveira, Vitor, Alison Colquhoun, Leandro M. Castro, et al.. (2005). Calcium modulates endopeptidase 24.15 (EC 3.4.24.15) membrane association, secondary structure and substrate specificity. FEBS Journal. 272(12). 2978–2992. 17 indexed citations

16.

Oliveira, Vitor, R Gatti, Vanessa Rioli, et al.. (2002). Temperature and salts effects on the peptidase activities of the recombinant metallooligopeptidases neurolysin and thimet oligopeptidase. European Journal of Biochemistry. 269(17). 4326–4334. 13 indexed citations

17.

Fontenele-Neto, J.D., et al.. (2001). Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain. The Journal of Comparative Neurology. 438(4). 399–410. 48 indexed citations

18.

Casatti, Cláudio Aparecido, Akira Kato, Antônio Carlos Martins de Camargo, et al.. (1999). Differential subcellular distribution of neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) in the rat brain. Brain Research. 851(1-2). 261–265. 42 indexed citations

19.

Rodrı́guez-Acosta, Alexis, et al.. (1996). Antimalarial Activity of Tetracycline and a De‐novo Synthesized Quinolone Derivative Against Plasmodium berghei in Mice. Pharmacy and Pharmacology Communications. 2(7). 325–327. 1 indexed citations

20.

Ferro, Emer S., Denise V. Tambourgi, Marcelo D. Gomes, et al.. (1993). Secretion of a Neuropeptide-Metabolizing Enzyme Similar to Endopeptidase 22.19 by Glioma C6-Cells. Biochemical and Biophysical Research Communications. 191(1). 275–281. 29 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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