Mitchell B. Berkenpas

1.3k total citations
9 papers, 1.1k citations indexed

About

Mitchell B. Berkenpas is a scholar working on Cancer Research, Hematology and Molecular Biology. According to data from OpenAlex, Mitchell B. Berkenpas has authored 9 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Cancer Research, 5 papers in Hematology and 4 papers in Molecular Biology. Recurrent topics in Mitchell B. Berkenpas's work include Protease and Inhibitor Mechanisms (7 papers), Blood Coagulation and Thrombosis Mechanisms (5 papers) and Cell Adhesion Molecules Research (3 papers). Mitchell B. Berkenpas is often cited by papers focused on Protease and Inhibitor Mechanisms (7 papers), Blood Coagulation and Thrombosis Mechanisms (5 papers) and Cell Adhesion Molecules Research (3 papers). Mitchell B. Berkenpas collaborates with scholars based in United States, Switzerland and Canada. Mitchell B. Berkenpas's co-authors include Daniel A. Lawrence, David Ginsburg, Ingrid M. Verhamme, Jan-Olov Kvassman, Duane E. Day, Joseph D. Shore, Selvi Palaniappan, Mihály Hajós, Judy A. Lawson and Vincent E. Groppi and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Neuroscience.

In The Last Decade

Mitchell B. Berkenpas

9 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mitchell B. Berkenpas United States 8 642 596 393 139 130 9 1.1k
Soonjung L. Hahn United States 6 654 1.0× 140 0.2× 74 0.2× 59 0.4× 93 0.7× 6 906
Terri Messier United States 19 835 1.3× 196 0.3× 146 0.4× 13 0.1× 189 1.5× 41 1.1k
Alexei Poliakov United Kingdom 13 654 1.0× 144 0.2× 66 0.2× 47 0.3× 436 3.4× 19 1.0k
Michele Pallaoro Italy 10 1.2k 1.9× 84 0.1× 44 0.1× 75 0.5× 108 0.8× 12 1.5k
Kazumi Hayashi Japan 14 521 0.8× 57 0.1× 59 0.2× 72 0.5× 157 1.2× 33 958
Minako Nakazawa Japan 14 656 1.0× 80 0.1× 113 0.3× 20 0.1× 192 1.5× 23 911
Virna D. Leaner South Africa 22 998 1.6× 184 0.3× 44 0.1× 42 0.3× 35 0.3× 43 1.3k
Richard E. Cutler United States 19 1.1k 1.8× 165 0.3× 70 0.2× 31 0.2× 43 0.3× 46 1.6k
Michael Engelke Germany 19 465 0.7× 74 0.1× 85 0.2× 54 0.4× 84 0.6× 36 1.2k
John Anagli United States 21 603 0.9× 157 0.3× 56 0.1× 22 0.2× 143 1.1× 31 1.0k

Countries citing papers authored by Mitchell B. Berkenpas

Since Specialization
Citations

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

Fields of papers citing papers by Mitchell B. Berkenpas

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mitchell B. Berkenpas. 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 Mitchell B. Berkenpas. The network helps show where Mitchell B. Berkenpas may publish in the future.

Co-authorship network of co-authors of Mitchell B. Berkenpas

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

All Works

9 of 9 papers shown
1.
Hurst, Raymond S, Mihály Hajós, M. Raggenbass, et al.. (2005). A Novel Positive Allosteric Modulator of the α7 Neuronal Nicotinic Acetylcholine Receptor:In VitroandIn VivoCharacterization. Journal of Neuroscience. 25(17). 4396–4405. 372 indexed citations
2.
Sharp, Allan M., Penelope E. Stein, N.S. Pannu, et al.. (1999). The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure. 7(2). 111–118. 142 indexed citations
3.
Begley, Dale A., Mitchell B. Berkenpas, Kathleen E. Sampson, & Irene Abraham. (1997). Identification and sequence of human PKY, a putative kinase with increased expression in multidrug-resistant cells, with homology to yeast protein kinase Yak1. Gene. 200(1-2). 35–43. 21 indexed citations
4.
Lawrence, Daniel A., David Ginsburg, Duane E. Day, et al.. (1995). Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme Intermediates. Journal of Biological Chemistry. 270(43). 25309–25312. 220 indexed citations
5.
Berkenpas, Mitchell B., Daniel A. Lawrence, & David Ginsburg. (1995). Molecular evolution of plasminogen activator inhibitor-1 functional stability.. The EMBO Journal. 14(13). 2969–2977. 196 indexed citations
6.
Lawrence, Daniel A., Mitchell B. Berkenpas, Selvi Palaniappan, & David Ginsburg. (1994). Localization of vitronectin binding domain in plasminogen activator inhibitor-1.. Journal of Biological Chemistry. 269(21). 15223–15228. 110 indexed citations
7.
Berkenpas, Mitchell B. & J. P. Quigley. (1991). Transformation-dependent activation of urokinase-type plasminogen activator by a plasmin-independent mechanism: involvement of cell surface membranes.. Proceedings of the National Academy of Sciences. 88(17). 7768–7772. 21 indexed citations
8.
Quigley, James P., et al.. (1990). Serine protease and metallo protease cascade systems involved in pericellular proteolysis. Cell Differentiation and Development. 32(3). 263–275. 22 indexed citations
9.
Berkenpas, Mitchell B. & James P. Quigley. (1989). Secretion of two-chain active plasminogen activator from rsv-transformed chicken embryo fibroblasts: Evidence for a plasmin-independent converting activity. Fibrinolysis and Proteolysis. 3. 3–4. 1 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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