Jenny Presto

2.5k total citations
33 papers, 2.0k citations indexed

About

Jenny Presto is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, Jenny Presto has authored 33 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 18 papers in Physiology and 16 papers in Cell Biology. Recurrent topics in Jenny Presto's work include Alzheimer's disease research and treatments (18 papers), Protein Structure and Dynamics (13 papers) and Endoplasmic Reticulum Stress and Disease (12 papers). Jenny Presto is often cited by papers focused on Alzheimer's disease research and treatments (18 papers), Protein Structure and Dynamics (13 papers) and Endoplasmic Reticulum Stress and Disease (12 papers). Jenny Presto collaborates with scholars based in Sweden, Estonia and United Kingdom. Jenny Presto's co-authors include Jan Johansson, Sara Linse, Henrik Biverstål, Lena Kjellén, Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, Paolo Arosio, André Fisahn and Erik Hermansson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Jenny Presto

31 papers receiving 2.0k citations

Peers

Jenny Presto
May Khanna United States
Judit Oláh Hungary
Michael Y. Sherman United States
Ronald R. Hiebsch United States
Robyn A. Sharples Australia
Kwame Hoyte United States
Wilman Luk United States
Giuseppina Minopoli Italy
Olga Šimáková United States
José L. Zugaza Spain
May Khanna United States
Jenny Presto
Citations per year, relative to Jenny Presto Jenny Presto (= 1×) peers May Khanna

Countries citing papers authored by Jenny Presto

Since Specialization
Citations

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

Fields of papers citing papers by Jenny Presto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jenny Presto

This figure shows the co-authorship network connecting the top 25 collaborators of Jenny Presto. A scholar is included among the top collaborators of Jenny Presto 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 Jenny Presto. Jenny Presto 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.
Sierra, Carlos, Axel Leppert, Antonios N. Pouliopoulos, et al.. (2020). Recombinant BRICHOS chaperone domains delivered to mouse brain parenchyma by focused ultrasound and microbubbles are internalized by hippocampal and cortical neurons. Molecular and Cellular Neuroscience. 105. 103498–103498. 19 indexed citations
2.
Gereñu, Gorka, Torbjörn Persson, Julen Goikolea, et al.. (2019). Thioredoxin-80 protects against amyloid-beta pathology through autophagic-lysosomal pathway regulation. Molecular Psychiatry. 26(4). 1410–1423. 15 indexed citations
3.
Tambaro, Simone, Axel Leppert, Gefei Chen, et al.. (2019). Blood–brain and blood–cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice. Journal of Biological Chemistry. 294(8). 2606–5220. 16 indexed citations
4.
Tambaro, Simone, Marta del Campo, Jeroen J.M. Hoozemans, et al.. (2018). The Bri2 and Bri3 BRICHOS Domains Interact Differently with Aβ42 and Alzheimer Amyloid Plaques. Journal of Alzheimer s Disease Reports. 2(1). 27–39. 30 indexed citations
5.
Vincenz‐Donnelly, Lisa, Roman Körner, Erik C Hansen, et al.. (2017). High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins. The EMBO Journal. 37(3). 337–350. 27 indexed citations
6.
Arosio, Paolo, Thomas C. T. Michaels, Sara Linse, et al.. (2016). Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation. Nature Communications. 7(1). 10948–10948. 214 indexed citations
7.
Cohen, Samuel I. A., Paolo Arosio, Jenny Presto, et al.. (2015). A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers. Nature Structural & Molecular Biology. 22(3). 207–213. 351 indexed citations
8.
Biverstål, Henrik, Erik Hermansson, Axel Leppert, et al.. (2015). Dissociation of a BRICHOS trimer into monomers leads to increased inhibitory effect on Aβ42 fibril formation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(8). 835–843. 22 indexed citations
9.
Landreh, Michael, Anna Rising, Jenny Presto, Hans Jörnvall, & Jan Johansson. (2015). Specific Chaperones and Regulatory Domains in Control of Amyloid Formation. Journal of Biological Chemistry. 290(44). 26430–26436. 31 indexed citations
10.
Sáenz, A., Jenny Presto, Patricia Lara, et al.. (2015). Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane Segment. Journal of Biological Chemistry. 290(28). 17628–17641. 10 indexed citations
11.
Sáenz, A., Jenny Presto, Patricia Lara, et al.. (2015). Folding and intramembraneous BRICHOS binding of the proSP-C transmembrane segment. Microbiology and Immunology. 55(2). 130–4.
12.
Kurudenkandy, Firoz Roshan, Misha Zilberter, Henrik Biverstål, et al.. (2014). Amyloid-β-Induced Action Potential Desynchronization and Degradation of Hippocampal Gamma Oscillations Is Prevented by Interference with Peptide Conformation Change and Aggregation. Journal of Neuroscience. 34(34). 11416–11425. 92 indexed citations
13.
Lee, Hunsang, Patricia Lara, Angela Ostuni, et al.. (2014). Live-cell topology assessment of URG7, MRP6102 and SP-C using glycosylatable green fluorescent protein in mammalian cells. Biochemical and Biophysical Research Communications. 450(4). 1587–1592. 16 indexed citations
14.
Campo, Marta del, Catarina R. Oliveira, Wiep Scheper, et al.. (2014). BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells. Cellular and Molecular Life Sciences. 72(8). 1599–1611. 11 indexed citations
15.
Willander, Hanna, Erik Hermansson, Jan Johansson, & Jenny Presto. (2011). BRICHOS domain associated with lung fibrosis, dementia and cancer – a chaperone that prevents amyloid fibril formation?. FEBS Journal. 278(20). 3893–3904. 58 indexed citations
16.
Johansson, Jan, Charlotte Nerelius, Hanna Willander, & Jenny Presto. (2010). Conformational preferences of non-polar amino acid residues: An additional factor in amyloid formation. Biochemical and Biophysical Research Communications. 402(3). 515–518. 22 indexed citations
17.
Johansson, Hanna, Maria Eriksson, Kerstin Nordling, Jenny Presto, & Jan Johansson. (2009). The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment. Protein Science. 18(6). 1175–1182. 33 indexed citations
18.
Presto, Jenny, Marta Busse, Maria Wilén, et al.. (2008). Heparan sulfate biosynthesis enzymes EXT1 and EXT2 affect NDST1 expression and heparan sulfate sulfation. Proceedings of the National Academy of Sciences. 105(12). 4751–4756. 138 indexed citations
19.
Presto, Jenny, et al.. (2008). Heparin/Heparan Sulfate Biosynthesis. Journal of Biological Chemistry. 283(29). 20008–20014. 109 indexed citations
20.
Busse, Marta, et al.. (2007). Contribution of EXT1, EXT2, and EXTL3 to Heparan Sulfate Chain Elongation. Journal of Biological Chemistry. 282(45). 32802–32810. 147 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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