Noa Reis

1.2k total citations
18 papers, 962 citations indexed

About

Noa Reis is a scholar working on Molecular Biology, Oncology and Epidemiology. According to data from OpenAlex, Noa Reis has authored 18 papers receiving a total of 962 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 7 papers in Oncology and 6 papers in Epidemiology. Recurrent topics in Noa Reis's work include Ubiquitin and proteasome pathways (17 papers), Autophagy in Disease and Therapy (6 papers) and Genetics and Neurodevelopmental Disorders (5 papers). Noa Reis is often cited by papers focused on Ubiquitin and proteasome pathways (17 papers), Autophagy in Disease and Therapy (6 papers) and Genetics and Neurodevelopmental Disorders (5 papers). Noa Reis collaborates with scholars based in Israel, United States and Australia. Noa Reis's co-authors include Michael H. Glickman, Oded Kleifeld, Kay Hofmann, Daria Krutauz, Prasad Sulkshane, Anita Thakur, Zoi Erpapazoglou, Steven P. Gygi, Donald S. Kirkpatrick and Inbal Ziv and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Molecular Cell.

In The Last Decade

Noa Reis

18 papers receiving 957 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Noa Reis Israel 15 835 314 277 185 92 18 962
Ido Livneh Israel 14 1.1k 1.3× 376 1.2× 310 1.1× 143 0.8× 74 0.8× 31 1.3k
Chandra Childress United States 15 594 0.7× 183 0.6× 220 0.8× 133 0.7× 62 0.7× 18 843
Ludmila Kaplun United States 11 798 1.0× 151 0.5× 145 0.5× 182 1.0× 89 1.0× 16 1.1k
Mickaël M. Cohen France 16 1.2k 1.5× 373 1.2× 460 1.7× 88 0.5× 72 0.8× 27 1.4k
Silvia Matteoni Italy 13 485 0.6× 360 1.1× 152 0.5× 89 0.5× 32 0.3× 19 862
Rachel Kama Israel 12 676 0.8× 161 0.5× 320 1.2× 93 0.5× 29 0.3× 13 911
Ladislaus Török Austria 6 480 0.6× 457 1.5× 147 0.5× 81 0.4× 40 0.4× 6 819
Gustavo M. Silva United States 13 682 0.8× 148 0.5× 181 0.7× 135 0.7× 59 0.6× 20 856
Vinay V. Eapen United States 14 646 0.8× 193 0.6× 162 0.6× 98 0.5× 25 0.3× 17 808
Michael J. Thomenius United States 12 623 0.7× 100 0.3× 193 0.7× 99 0.5× 40 0.4× 21 756

Countries citing papers authored by Noa Reis

Since Specialization
Citations

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

Fields of papers citing papers by Noa Reis

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Noa Reis

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

All Works

18 of 18 papers shown
1.
Sahu, Indrajit, Monika Bajorek, Daria Krutauz, et al.. (2023). A Role for the Proteasome Alpha2 Subunit N-Tail in Substrate Processing. Biomolecules. 13(3). 480–480. 3 indexed citations
2.
Maniv, Inbal, Elle Koren, Noa Reis, et al.. (2023). Altered ubiquitin signaling induces Alzheimer’s disease-like hallmarks in a three-dimensional human neural cell culture model. Nature Communications. 14(1). 5922–5922. 28 indexed citations
3.
Reis, Noa, et al.. (2022). Coronaviral PLpro proteases and the immunomodulatory roles of conjugated versus free Interferon Stimulated Gene product-15 (ISG15). Seminars in Cell and Developmental Biology. 132. 16–26. 12 indexed citations
4.
Sulkshane, Prasad, et al.. (2021). Ubiquitination and receptor-mediated mitophagy converge to eliminate oxidation-damaged mitochondria during hypoxia. Redox Biology. 45. 102047–102047. 126 indexed citations
5.
Sulkshane, Prasad, et al.. (2020). Inhibition of proteasome reveals basal mitochondrial ubiquitination. Journal of Proteomics. 229. 103949–103949. 27 indexed citations
6.
Gefen, Eran, Teresa Rinaldi, David Jimenez‐Morales, et al.. (2018). Proteasome lid bridges mitochondrial stress with Cdc53/Cullin1 NEDDylation status. Redox Biology. 20. 533–543. 23 indexed citations
7.
Keren‐Kaplan, Tal, Ilan Attali, Oded Kleifeld, et al.. (2016). Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism. Nature Communications. 7(1). 12960–12960. 28 indexed citations
8.
Nowicka, Urszula, Daoning Zhang, Olivier Walker, et al.. (2015). DNA-Damage-Inducible 1 Protein (Ddi1) Contains an Uncharacteristic Ubiquitin-like Domain that Binds Ubiquitin. Structure. 23(3). 542–557. 58 indexed citations
9.
Yu, Zanlin, Nurit Livnat‐Levanon, Oded Kleifeld, et al.. (2015). Base-CP proteasome can serve as a platform for stepwise lid formation. Bioscience Reports. 35(3). 20 indexed citations
10.
Livnat‐Levanon, Nurit, Éva Kevei, Oded Kleifeld, et al.. (2015). Reversible 26S proteasome disassembly upon mitochondrial stress. Mitochondrion. 24. S6–S6. 2 indexed citations
11.
Livnat‐Levanon, Nurit, Éva Kevei, Oded Kleifeld, et al.. (2014). Reversible 26S Proteasome Disassembly upon Mitochondrial Stress. Cell Reports. 7(5). 1371–1380. 143 indexed citations
12.
Nakasone, Mark A., Zanlin Yu, Daria Krutauz, et al.. (2014). Disassembly of Lys11 and Mixed Linkage Polyubiquitin Conjugates Provides Insights into Function of Proteasomal Deubiquitinases Rpn11 and Ubp6. Journal of Biological Chemistry. 290(8). 4688–4704. 40 indexed citations
13.
Krutauz, Daria, Noa Reis, Mark A. Nakasone, et al.. (2014). Extended ubiquitin species are protein-based DUB inhibitors. Nature Chemical Biology. 10(8). 664–670. 28 indexed citations
14.
Ziv, Inbal, Donald S. Kirkpatrick, Zoi Erpapazoglou, et al.. (2011). A Perturbed Ubiquitin Landscape Distinguishes Between Ubiquitin in Trafficking and in Proteolysis. Molecular & Cellular Proteomics. 10(5). M111.009753–M111.009753. 115 indexed citations
15.
Yu, Zanlin, Oded Kleifeld, Maya Kleiman, et al.. (2011). Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome. Molecular Biology of the Cell. 22(7). 911–920. 37 indexed citations
16.
Kirkpatrick, Donald S., Inbal Ziv, Woong Kim, et al.. (2008). Extraproteasomal Rpn10 Restricts Access of the Polyubiquitin-Binding Protein Dsk2 to Proteasome. Molecular Cell. 32(3). 415–425. 76 indexed citations
17.
Gomes, Andreia C., Eduardo Basílio de Oliveira, Noa Reis, et al.. (2005). Reactive oxygen species mediate lethality induced by far-UV inEscherichia colicells. Redox Report. 10(2). 91–95. 19 indexed citations
18.

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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