Houssam Raad

1.1k total citations
16 papers, 844 citations indexed

About

Houssam Raad is a scholar working on Molecular Biology, Immunology and Physiology. According to data from OpenAlex, Houssam Raad has authored 16 papers receiving a total of 844 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 10 papers in Immunology and 3 papers in Physiology. Recurrent topics in Houssam Raad's work include Neutrophil, Myeloperoxidase and Oxidative Mechanisms (10 papers), Immune Response and Inflammation (5 papers) and Immune cells in cancer (3 papers). Houssam Raad is often cited by papers focused on Neutrophil, Myeloperoxidase and Oxidative Mechanisms (10 papers), Immune Response and Inflammation (5 papers) and Immune cells in cancer (3 papers). Houssam Raad collaborates with scholars based in France, United States and Lebanon. Houssam Raad's co-authors include Jamel El‐Benna, Pham My‐Chan Dang, Marie‐Anne Gougerot‐Pocidalo, Tarek Boussetta, Sahra Amel Belambri, Margarita Hurtado-Nédelec, Loïc Rolas, Yolande Kroviarski, Françoise Morel and Hamid Rezvani and has published in prestigious journals such as Blood, PLoS ONE and The FASEB Journal.

In The Last Decade

Houssam Raad

16 papers receiving 838 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Houssam Raad France 13 372 359 150 105 55 16 844
Nurit Hadad Israel 18 330 0.9× 375 1.0× 344 2.3× 76 0.7× 46 0.8× 40 1.2k
Hyunkeun Song South Korea 21 443 1.2× 380 1.1× 62 0.4× 61 0.6× 27 0.5× 38 1.1k
Sven W. Sauer Germany 14 219 0.6× 454 1.3× 88 0.6× 69 0.7× 19 0.3× 17 858
Qinggao Zhang China 20 243 0.7× 404 1.1× 99 0.7× 32 0.3× 27 0.5× 51 919
Erdi Sözen Türkiye 14 309 0.8× 285 0.8× 116 0.8× 105 1.0× 48 0.9× 27 956
Outi Sareila Finland 17 404 1.1× 306 0.9× 106 0.7× 27 0.3× 16 0.3× 31 945
Takuya Yashiro Japan 18 335 0.9× 337 0.9× 126 0.8× 29 0.3× 61 1.1× 53 845
Xunsheng Chen United States 17 110 0.3× 399 1.1× 106 0.7× 83 0.8× 45 0.8× 28 767
Jennifer L. Meitzler United States 18 522 1.4× 537 1.5× 265 1.8× 50 0.5× 36 0.7× 28 1.2k
Donna Zhang United States 8 117 0.3× 1.0k 2.8× 86 0.6× 66 0.6× 29 0.5× 12 1.5k

Countries citing papers authored by Houssam Raad

Since Specialization
Citations

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

Fields of papers citing papers by Houssam Raad

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Houssam Raad

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

All Works

16 of 16 papers shown
1.
Boussetta, Tarek, Houssam Raad, Marie‐Anne Gougerot‐Pocidalo, et al.. (2024). The peptidyl-prolyl isomerase Pin1 controls GM-CSF-induced priming of NADPH oxidase in human neutrophils and priming at inflammatory sites. International Immunopharmacology. 137. 112425–112425. 6 indexed citations
2.
Nehme, Ali, Christelle Debeissat, Marie José Stasia, et al.. (2021). Characterization of NADPH Oxidase Expression and Activity in Acute Myeloid Leukemia Cell Lines: A Correlation with the Differentiation Status. Antioxidants. 10(3). 498–498. 14 indexed citations
3.
Raad, Houssam, Hamad Hassan, Tarek Boussetta, et al.. (2020). The protein kinase A negatively regulates reactive oxygen species production by phosphorylating gp91phox/NOX2 in human neutrophils. Free Radical Biology and Medicine. 160. 19–27. 17 indexed citations
4.
Raad, Houssam, et al.. (2019). Phosphorylation of gp91phox/NOX2 in Human Neutrophils. Methods in molecular biology. 1982. 341–352. 9 indexed citations
5.
Belambri, Sahra Amel, Loïc Rolas, Houssam Raad, et al.. (2018). NADPH oxidase activation in neutrophils: Role of the phosphorylation of its subunits. European Journal of Clinical Investigation. 48(S2). e12951–e12951. 203 indexed citations
6.
Rudolf, Jana, Houssam Raad, Alain Taı̈eb, & Hamid Rezvani. (2017). NADPH Oxidases and Their Roles in Skin Homeostasis and Carcinogenesis. Antioxidants and Redox Signaling. 28(13). 1238–1261. 21 indexed citations
7.
Raad, Houssam, Martin Serrano-Sanchez, Walid Mahfouf, et al.. (2017). NADPH Oxidase-1 Plays a Key Role in Keratinocyte Responses to UV Radiation and UVB-Induced Skin Carcinogenesis. Journal of Investigative Dermatology. 137(6). 1311–1321. 52 indexed citations
8.
Liu, Liang, Hamid Rezvani, Jung Ho Back, et al.. (2014). Inhibition of p38 MAPK Signaling Augments Skin Tumorigenesis via NOX2 Driven ROS Generation. PLoS ONE. 9(5). e97245–e97245. 39 indexed citations
9.
Hosseini, Mohsen, Walid Mahfouf, Martin Serrano-Sanchez, et al.. (2014). Premature Skin Aging Features Rescued by Inhibition of NADPH Oxidase Activity in XPC-Deficient Mice. Journal of Investigative Dermatology. 135(4). 1108–1118. 30 indexed citations
11.
Deken, Xavier De, et al.. (2012). The thyroid oxidative capacity is enhanced by the Th2 cytokines, IL-4 and IL-13, through increased expression of the dual oxidase 2 and its maturation factor DUOXA2. Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles). 4 indexed citations
12.
Grasberger, Helmut, Xavier De Deken, Olga Barca‐Mayo, et al.. (2012). Mice Deficient in Dual Oxidase Maturation Factors Are Severely Hypothyroid. Molecular Endocrinology. 26(3). 481–492. 68 indexed citations
13.
Dang, Pham My‐Chan, Houssam Raad, Tarek Boussetta, et al.. (2011). The NADPH oxidase cytosolic component p67phox is constitutively phosphorylated in human neutrophils: Regulation by a protein tyrosine kinase, MEK1/2 and phosphatases 1/2A. Biochemical Pharmacology. 82(9). 1145–1152. 26 indexed citations
14.
Boussetta, Tarek, Marie‐Anne Gougerot‐Pocidalo, Gilles Hayem, et al.. (2010). The prolyl isomerase Pin1 acts as a novel molecular switch for TNF-α–induced priming of the NADPH oxidase in human neutrophils. Blood. 116(26). 5795–5802. 82 indexed citations
15.
Boussetta, Tarek, Houssam Raad, Philippe Lettéron, et al.. (2009). Punicic Acid a Conjugated Linolenic Acid Inhibits TNFα-Induced Neutrophil Hyperactivation and Protects from Experimental Colon Inflammation in Rats. PLoS ONE. 4(7). e6458–e6458. 106 indexed citations
16.
Raad, Houssam, Tarek Boussetta, Yolande Kroviarski, et al.. (2008). Regulation of the phagocyte NADPH oxidase activity: phosphorylation of gp91 phox /NOX2 by protein kinase C enhances its diaphorase activity and binding to Rac2, p67 phox , and p47 phox. The FASEB Journal. 23(4). 1011–1022. 140 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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