Frank Church

8.8k total citations · 2 hit papers
128 papers, 7.3k citations indexed

About

Frank Church is a scholar working on Hematology, Cancer Research and Molecular Biology. According to data from OpenAlex, Frank Church has authored 128 papers receiving a total of 7.3k indexed citations (citations by other indexed papers that have themselves been cited), including 77 papers in Hematology, 60 papers in Cancer Research and 34 papers in Molecular Biology. Recurrent topics in Frank Church's work include Blood Coagulation and Thrombosis Mechanisms (74 papers), Protease and Inhibitor Mechanisms (57 papers) and Coagulation, Bradykinin, Polyphosphates, and Angioedema (21 papers). Frank Church is often cited by papers focused on Blood Coagulation and Thrombosis Mechanisms (74 papers), Protease and Inhibitor Mechanisms (57 papers) and Coagulation, Bradykinin, Polyphosphates, and Angioedema (21 papers). Frank Church collaborates with scholars based in United States, United Kingdom and Australia. Frank Church's co-authors include George L. Catignani, Harold E. Swaisgood, David H. Porter, Herbert C. Whinna, Charlotte W. Pratt, Claudia M. Noyes, Lea M. Beaulieu, Robin W. Carrell, James A. Huntington and Michael Griffith and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Blood.

In The Last Decade

Frank Church

123 papers receiving 7.1k citations

Hit Papers

Spectrophotometric Assay Using o-Phthaldialdehyde for Det... 1983 2026 1997 2011 1983 2001 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Frank Church United States 42 2.9k 2.4k 1.9k 1.0k 906 128 7.3k
Dominique Belin Switzerland 52 8.0k 2.7× 2.6k 1.1× 4.2k 2.2× 428 0.4× 1.3k 1.4× 114 15.0k
Ifor R. Williams United States 56 5.6k 1.9× 2.8k 1.2× 841 0.4× 300 0.3× 477 0.5× 156 13.2k
María A. Juliano Brazil 47 4.8k 1.7× 553 0.2× 872 0.4× 175 0.2× 543 0.6× 376 9.1k
Magnus Abrahamson Sweden 52 3.9k 1.3× 625 0.3× 2.5k 1.3× 117 0.1× 723 0.8× 178 9.4k
Helena B. Nader Brazil 53 4.2k 1.5× 527 0.2× 1.0k 0.5× 280 0.3× 3.4k 3.7× 389 10.0k
J.E. Folk United States 50 5.1k 1.8× 873 0.4× 250 0.1× 901 0.9× 1.2k 1.3× 139 10.1k
Joost Schalkwijk Netherlands 59 3.3k 1.1× 502 0.2× 916 0.5× 144 0.1× 1.7k 1.9× 259 11.2k
Alister C. Ward Australia 51 3.1k 1.1× 984 0.4× 782 0.4× 137 0.1× 1.3k 1.4× 201 8.4k
Nobuhiko Katunuma Japan 59 6.4k 2.2× 399 0.2× 2.5k 1.3× 143 0.1× 2.2k 2.4× 362 12.5k
Janko Kos Slovenia 57 4.3k 1.5× 442 0.2× 3.6k 1.9× 131 0.1× 920 1.0× 314 10.9k

Countries citing papers authored by Frank Church

Since Specialization
Citations

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

Fields of papers citing papers by Frank Church

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Frank Church

This figure shows the co-authorship network connecting the top 25 collaborators of Frank Church. A scholar is included among the top collaborators of Frank Church 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 Frank Church. Frank Church 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.
Church, Frank, et al.. (2020). Integrative Medicine and Health Therapy for Parkinson Disease. Topics in Geriatric Rehabilitation. 36(3). 176–186. 17 indexed citations
2.
Cobbold, P H, et al.. (2020). Potential Role of Vitamin D in the Elderly to Resist COVID-19 and to Slow Progression of Parkinson’s Disease. Brain Sciences. 10(5). 284–284. 63 indexed citations
3.
Carter, Jennifer C. & Frank Church. (2011). Peroxisome Proliferator-Activated Receptor-γLigands Alter Breast Cancer Cell Motility through Modulation of the Plasminogen Activator System. Journal of Oncology. 2011. 1–8. 4 indexed citations
4.
Rau, Jill C., Jennifer W. Mitchell, Yolanda M. Fortenberry, & Frank Church. (2011). Heparin Cofactor II: Discovery, Properties, and Role in Controlling Vascular Homeostasis. Seminars in Thrombosis and Hemostasis. 37(4). 339–348. 27 indexed citations
5.
Campbell, Robert A., et al.. (2010). Enhanced cell‐associated plasminogen activator pathway but not coagulation pathway activity contributes to motility in metastatic breast cancer cells. Journal of Thrombosis and Haemostasis. 8(6). 1323–1332. 5 indexed citations
6.
Carter, Jennifer C. & Frank Church. (2009). Obesity and Breast Cancer: The Roles of Peroxisome Proliferator‐Activated Receptor‐γ and Plasminogen Activator Inhibitor‐1. PPAR Research. 2009(1). 345320–345320. 63 indexed citations
7.
Church, Frank, et al.. (2008). Effect of Locked-Nucleic Acid on a Biologically Active G-Quadruplex. A Structure-Activity Relationship of the Thrombin Aptamer. International Journal of Molecular Sciences. 9(3). 422–433. 69 indexed citations
8.
Fortenberry, Yolanda M., Herbert C. Whinna, Scott Cooper, et al.. (2007). Essential thrombin residues for inhibition by protein C inhibitor with the cofactors heparin and thrombomodulin. Journal of Thrombosis and Haemostasis. 5(7). 1486–1492. 7 indexed citations
9.
Réhault‐Godbert, Sophie, Christopher W. Gregory, Scott Cooper, et al.. (2005). Protein C inhibitor (plasminogen activator inhibitor-3) expression in the CWR22 prostate cancer xenograft. Experimental and Molecular Pathology. 79(1). 23–32. 3 indexed citations
10.
Myles, Timothy, Frank Church, Herbert C. Whinna, Denis Monard, & Stuart R. Stone. (1998). Role of Thrombin Anion-binding Exosite-I in the Formation of Thrombin-Serpin Complexes. Journal of Biological Chemistry. 273(47). 31203–31208. 55 indexed citations
11.
Slate, Cheryl A., et al.. (1995). Engineering of five 88‐residue receptor‐adhesive modular proteins containing a parallel α‐helical coiled coil and two RGD ligand sites. International journal of peptide & protein research. 45(3). 290–298. 6 indexed citations
12.
Crago, Aimeé M., et al.. (1995). Monocyte Chemoattractant Activity of Ser195 → Ala Active Site Mutant Recombinant α-Thrombin. Experimental Cell Research. 219(2). 650–656. 16 indexed citations
13.
Whinna, Herbert C., et al.. (1993). Inhibition of dysthrombins Quick I and II by heparin cofactor II and antithrombin.. Journal of Biological Chemistry. 268(5). 3321–3327. 19 indexed citations
14.
Hoffman, Maureane, et al.. (1991). The effects of heparin cofactor II-derived chemotaxins on neutrophil actin conformation and cyclic AMP levels. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1095(1). 78–82. 4 indexed citations
15.
Pratt, Charlotte W., B. Gail Macik, & Frank Church. (1989). Protein C inhibitor: Purification and proteinase reactivity. Thrombosis Research. 53(6). 595–602. 24 indexed citations
16.
Pratt, Charlotte W., et al.. (1989). Physicochemical Aspects of Heparin Cofactor IIa. Annals of the New York Academy of Sciences. 556(1). 104–115. 44 indexed citations
17.
Church, Frank, et al.. (1988). Antithrombin action of phosvitin and other phosphate‐containing polyanions is mediated by heparin cofactor II. FEBS Letters. 237(1-2). 26–30. 24 indexed citations
18.
Peterson, Cynthia B., et al.. (1987). LYSINE-125 IS ESSENTIAL FOR HEPARIN BINDING TO ANTITHROMBIN. Thrombosis and Haemostasis. 1 indexed citations
19.
Peterson, Cynthia B., et al.. (1987). Identification of a lysyl residue in antithrombin which is essential for heparin binding.. Journal of Biological Chemistry. 262(17). 8061–8065. 63 indexed citations
20.
Church, Frank, et al.. (1985). Effect of divalent cations on the limited proteolysis of prothrombin by thrombin. Archives of Biochemistry and Biophysics. 240(2). 607–612. 8 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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