Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Showing 1-25 of 49 citing articles:

Serum amyloid A – a review
George H. Sack
Molecular Medicine (2018) Vol. 24, Iss. 1
Open Access | Times Cited: 409
High-Density Lipoproteins and Serum Amyloid A (SAA)
Nancy R. Webb
Current Atherosclerosis Reports (2021) Vol. 23, Iss. 2
Open Access | Times Cited: 71
Intestinal Serum amyloid A suppresses systemic neutrophil activation and bactericidal activity in response to microbiota colonization
Caitlin C. Murdoch, Scott T. Espenschied, Molly A. Matty, et al.
PLoS Pathogens (2019) Vol. 15, Iss. 3, pp. e1007381-e1007381
Open Access | Times Cited: 69
Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis
Shobini Jayaraman, Donald Gantz, Christian Haupt, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 32
Open Access | Times Cited: 68
Expression of SAA1, SAA2 and SAA4 genes in human primary monocytes and monocyte-derived macrophages
Claire Jumeau, Fawaz Awad, Eman Assrawi, et al.
PLoS ONE (2019) Vol. 14, Iss. 5, pp. e0217005-e0217005
Open Access | Times Cited: 58
Longitudinal Fluctuations in Protein Concentrations and Higher-Order Structures in the Plasma Proteome of Kidney Failure Patients Subjected to a Kidney Transplant
Sofia Kalaidopoulou Nteak, Franziska Völlmy, Marie V. Lukassen, et al.
Journal of Proteome Research (2024) Vol. 23, Iss. 6, pp. 2124-2136
Open Access | Times Cited: 7
Serum amyloid A and atherosclerosis
Godfrey S. Getz, Paulette A. Krishack, Catherine A. Reardon
Current Opinion in Lipidology (2016) Vol. 27, Iss. 5, pp. 531-535
Closed Access | Times Cited: 60
Serum Amyloid A1 (SAA1) Revisited: Restricted Leukocyte-Activating Properties of Homogeneous SAA1
Sara Abouelasrar Salama, Mirre De Bondt, Mieke De Buck, et al.
Frontiers in Immunology (2020) Vol. 11
Open Access | Times Cited: 49
Renal AA amyloidosis: presentation, diagnosis, and current therapeutic options: a review
Sabine Karam, Mohamad Haidous, Virginie Royal, et al.
Kidney International (2022) Vol. 103, Iss. 3, pp. 473-484
Closed Access | Times Cited: 26
Structural studies of a serum amyloid A octamer that is primed to scaffold lipid nanodiscs
Asal Nady, Sean E. Reichheld, Simon Sharpe
Protein Science (2024) Vol. 33, Iss. 5
Open Access | Times Cited: 5
Molecular insights into the unique properties of the blood‐circulating proteasome
Yegor Leushkin, David Morgenstern, Shifra Ben‐Dor, et al.
Journal of Extracellular Biology (2025) Vol. 4, Iss. 1
Open Access
Serum amyloid A binding to glycosaminoglycans is synergistic with amyloid formation: Therapeutic targeting in the inflammation-linked amyloidosis
Shobini Jayaraman, Angela Urdaneta, Marcus Fändrich, et al.
Journal of Molecular Biology (2025), pp. 169007-169007
Closed Access
Apolipoprotein A-II induces acute-phase response associated AA amyloidosis in mice through conformational changes of plasma lipoprotein structure
Mu Yang, Yingye Liu, Jian Dai, et al.
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 33
Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve
Olga Gursky
Current Atherosclerosis Reports (2020) Vol. 22, Iss. 11
Open Access | Times Cited: 31
Paradoxical effects of SAA on lipoprotein oxidation suggest a new antioxidant function for SAA
Shobini Jayaraman, Christian Haupt, Olga Gursky
Journal of Lipid Research (2016) Vol. 57, Iss. 12, pp. 2138-2149
Open Access | Times Cited: 27
The turning away of serum amyloid A biological activities and receptor usage
Sara Abouelasrar Salama, Mieke Gouwy, Jo Van Damme, et al.
Immunology (2020) Vol. 163, Iss. 2, pp. 115-127
Open Access | Times Cited: 27
Cytokines and serum amyloid A in the pathogenesis of hepatitis C virus infection
Sara Abouelasrar Salama, Muriel Lavie, Mieke De Buck, et al.
Cytokine & Growth Factor Reviews (2019) Vol. 50, pp. 29-42
Closed Access | Times Cited: 26
High-Density Lipoprotein (HDL) in Allergy and Skin Diseases: Focus on Immunomodulating Functions
Athina Trakaki, Gunther Marsche
Biomedicines (2020) Vol. 8, Iss. 12, pp. 558-558
Open Access | Times Cited: 26
Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter
Tim Schulte, Antonio Chaves-Sanjuán, Giulia Mazzini, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 15
Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: A hypothetical function of SAA as a “molecular mop” in immune response
Nicholas M. Frame, Shobini Jayaraman, Donald Gantz, et al.
Journal of Structural Biology (2017) Vol. 200, Iss. 3, pp. 293-302
Open Access | Times Cited: 27
Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A
Nicholas M. Frame, Meera Kumanan, Thomas E. Wales, et al.
Journal of Molecular Biology (2020) Vol. 432, Iss. 7, pp. 1978-1995
Open Access | Times Cited: 21
Pleiotropic functions and clinical importance of circulating HDL-PON1 complex
Abdolkarim Mahrooz
Advances in clinical chemistry (2024), pp. 132-171
Closed Access | Times Cited: 2
Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks
Nicholas M. Frame, Olga Gursky
Amyloid (2016) Vol. 24, Iss. sup1, pp. 13-14
Open Access | Times Cited: 22
Serum amyloid A exhibits pH dependent antibacterial action and contributes to host defense against Staphylococcus aureus cutaneous infection
Han Zheng, Haifeng Li, Jingyuan Zhang, et al.
Journal of Biological Chemistry (2019) Vol. 295, Iss. 9, pp. 2570-2581
Open Access | Times Cited: 21
Single-Cell Transcriptomic Sequencing Analyses of Cell Heterogeneity During Osteogenesis of Human Adipose-Derived Mesenchymal Stem Cells
Rongmei Qu, Kai He, Tingyu Fan, et al.
Stem Cells (2021) Vol. 39, Iss. 11, pp. 1478-1488
Open Access | Times Cited: 15
Page 1 - Next Page

Scroll to top