Ann Smith

6.0k total citations · 1 hit paper
79 papers, 4.9k citations indexed

About

Ann Smith is a scholar working on Molecular Biology, Cell Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, Ann Smith has authored 79 papers receiving a total of 4.9k indexed citations (citations by other indexed papers that have themselves been cited), including 60 papers in Molecular Biology, 42 papers in Cell Biology and 16 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in Ann Smith's work include Heme Oxygenase-1 and Carbon Monoxide (50 papers), Hemoglobin structure and function (41 papers) and Neonatal Health and Biochemistry (16 papers). Ann Smith is often cited by papers focused on Heme Oxygenase-1 and Carbon Monoxide (50 papers), Hemoglobin structure and function (41 papers) and Neonatal Health and Biochemistry (16 papers). Ann Smith collaborates with scholars based in United States, United Kingdom and Hungary. Ann Smith's co-authors include William T. Morgan, J Alam, John M.C. Gutteridge, Russell J. McCulloh, Massimo De Paoli, Gregory M. Vercellotti, Shigeki Shibahara, Harry A. Dailey, Chunsheng Chen and Julia Nguyen and has published in prestigious journals such as Journal of Biological Chemistry, Blood and Biochemistry.

In The Last Decade

Ann Smith

79 papers receiving 4.8k citations

Hit Papers

align trajectories sort by overperformance

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Heme triggers TLR4 signaling leading to endothelial cell activation and vaso-occlusion in murine sickle cell disease

2013 525 citations Ann Smith et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Ann Smith	3.2k	1.4k	944	681	676	79	4.9k
Ursula Müller‐Eberhard	3.4k 1.1×	1.7k 1.2×	1.1k 1.1×	571 0.8×	525 0.8×	173	6.0k
P Verroust	3.5k 1.1×	1.0k 0.7×	601 0.6×	483 0.7×	700 1.0×	163	8.5k
Paul W. Buehler	2.3k 0.7×	2.4k 1.7×	1.2k 1.2×	1.0k 1.5×	669 1.0×	141	5.4k
John D. Belcher	2.7k 0.9×	970 0.7×	880 0.9×	2.7k 4.0×	1.8k 2.7×	133	6.6k
Abdu I. Alayash	3.5k 1.1×	3.9k 2.7×	1.5k 1.6×	1.3k 1.8×	601 0.9×	151	6.6k
András Váradi	3.1k 1.0×	870 0.6×	1.5k 1.5×	307 0.5×	547 0.8×	116	8.1k
Iqbal Hamza	1.9k 0.6×	608 0.4×	295 0.3×	441 0.6×	943 1.4×	75	4.5k
Arnold W. Strauss	6.4k 2.0×	868 0.6×	1.0k 1.1×	210 0.3×	180 0.3×	220	10.5k
Gérard Feldmann	2.7k 0.8×	878 0.6×	429 0.5×	217 0.3×	285 0.4×	268	9.2k
Marshall A. Lichtman	1.5k 0.5×	421 0.3×	220 0.2×	433 0.6×	764 1.1×	145	4.1k

Countries citing papers authored by Ann Smith

Since Specialization

Citations

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

Fields of papers citing papers by Ann Smith

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ann Smith

This figure shows the co-authorship network connecting the top 25 collaborators of Ann Smith. A scholar is included among the top collaborators of Ann Smith 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 Ann Smith. Ann Smith 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

Hunt, Rachel, et al.. (2017). Identification of oxidative modifications of hemopexin and their predicted physiological relevance. Journal of Biological Chemistry. 292(33). 13658–13671. 14 indexed citations

Rogers, Jack T., Vivek Venkataramani, Yanyan Liu, et al.. (2016). A role for amyloid precursor protein translation to restore iron homeostasis and ameliorate lead (Pb) neurotoxicity. Journal of Neurochemistry. 138(3). 479–494. 37 indexed citations

Jeney, Viktória, Attila Tóth, Éva Csősz, et al.. (2015). Heme-induced contractile dysfunction in Human cardiomyocytes caused by oxidant damage to thick filament proteins. Free Radical Biology and Medicine. 89. 248–262. 20 indexed citations

Fournier, Clémence, Ann Smith, & Philippe Delepelaire. (2011). Haem release from haemopexin by HxuA allows Haemophilus influenzae to escape host nutritional immunity. Molecular Microbiology. 80(1). 133–148. 50 indexed citations

Berridge, Michael V., et al.. (2007). Interaction of heme and heme–hemopexin with an extracellular oxidant system used to measure cell growth-associated plasma membrane electron transport. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1767(9). 1107–1117. 11 indexed citations

Lin, Qing, Sebastian Weis, Guang Yang, et al.. (2007). Heme Oxygenase-1 Protein Localizes to the Nucleus and Activates Transcription Factors Important in Oxidative Stress. Journal of Biological Chemistry. 282(28). 20621–20633. 356 indexed citations

Smith, Ann, et al.. (2007). An investigation of hemopexin redox properties by spectroelectrochemistry: biological relevance for heme uptake. BioMetals. 21(3). 239–248. 11 indexed citations

Holland, Julie, et al.. (2006). Elemental iron does repress transferrin, haemopexin and haemoglobin receptor expression in Haemophilusinfluenzae. FEMS Microbiology Letters. 150(1). 19–26. 8 indexed citations

Anderson, Gregory J., David M. Frazer, Andrew T. McKie, Chris D. Vulpe, & Ann Smith. (2005). Mechanisms of Haem and Non-Haem Iron Absorption: Lessons from Inherited Disorders of Iron Metabolism. BioMetals. 18(4). 339–348. 55 indexed citations

10.

Bourque, Stephane L., Brian E. McLaughlin, James F. Brien, et al.. (2004). The source of heme for vascular heme oxygenase I: heme uptake in rat aorta. Canadian Journal of Physiology and Pharmacology. 82(4). 209–217. 7 indexed citations

11.

Smith, Ann. (2002). Homeostasis of Heme in Health and Disease: Current Aspects of the Structural Biology of Heme-Protein Interactions and of Gene Regulation. DNA and Cell Biology. 21(4). 245–249. 21 indexed citations

12.

Paoli, Massimo De, Jon Marles‐Wright, & Ann Smith. (2002). Structure–Function Relationships in Heme-Proteins. DNA and Cell Biology. 21(4). 271–280. 154 indexed citations

13.

Escribá, Pablo V., et al.. (2002). Membrane Phospholipid Reorganization Differentially Regulates Metallothionein and Heme Oxygenase by Heme–Hemopexin. DNA and Cell Biology. 21(4). 355–364. 18 indexed citations

14.

Smith, Ann, et al.. (2001). Effects of Reduction and Ligation of Heme Iron on the Thermal Stability of Heme-Hemopexin Complexes. Journal of Protein Chemistry. 20(2). 145–154. 10 indexed citations

15.

Vanacore, Roberto, et al.. (2000). Role for Copper in Transient Oxidation and Nuclear Translocation of MTF-1, but Not of NF- κ B, by the Heme–Hemopexin Transport System. Antioxidants and Redox Signaling. 2(4). 739–752. 30 indexed citations

16.

Vanacore, Roberto, et al.. (1999). Cellular Protection Mechanisms against Extracellular Heme. Journal of Biological Chemistry. 274(2). 638–648. 78 indexed citations

17.

Smith, Ann, et al.. (1997). Role of Heme–Hemopexin in Human T-Lymphocyte Proliferation. Experimental Cell Research. 232(2). 246–254. 23 indexed citations

18.

Hunt, Richard C., et al.. (1996). Hemopexin in the human retina: Protection of the retina against heme-mediated toxicity. Journal of Cellular Physiology. 168(1). 71–80. 57 indexed citations

19.

Faber, H.R., Colin R. Groom, Heather M. Baker, et al.. (1995). 1.8 å crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure. 3(6). 551–559. 76 indexed citations

20.

Smith, Ann. (1987). Mechanisms of Toxicity of Photoactivated Artificial Porphyrins Role of Porphyrin‐Protein Interactions. Annals of the New York Academy of Sciences. 514(1). 309–322. 21 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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