Jack D. Stopa

612 total citations
13 papers, 493 citations indexed

About

Jack D. Stopa is a scholar working on Cell Biology, Immunology and Pulmonary and Respiratory Medicine. According to data from OpenAlex, Jack D. Stopa has authored 13 papers receiving a total of 493 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Cell Biology, 7 papers in Immunology and 6 papers in Pulmonary and Respiratory Medicine. Recurrent topics in Jack D. Stopa's work include Endoplasmic Reticulum Stress and Disease (7 papers), Toxin Mechanisms and Immunotoxins (6 papers) and Blood properties and coagulation (5 papers). Jack D. Stopa is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (7 papers), Toxin Mechanisms and Immunotoxins (6 papers) and Blood properties and coagulation (5 papers). Jack D. Stopa collaborates with scholars based in United States, Australia and United Kingdom. Jack D. Stopa's co-authors include Bruce Furie, Robert Flaumenhaft, Jeffrey I. Zwicker, Donna Neuberg, Mäneka Puligandla, Freda Passam, Srila Gopal, Mingdong Huang, Lin Lin and Barbara C. Furie and has published in prestigious journals such as Journal of Biological Chemistry, Blood and Biochemistry.

In The Last Decade

Jack D. Stopa

13 papers receiving 491 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jack D. Stopa United States	8	219	167	73	72	69	13	493
Sheryl R. Bowley United States	8	200 0.9×	152 0.9×	62 0.8×	99 1.4×	102 1.5×	14	470
Lisa‐Marie Holbrook United Kingdom	14	236 1.1×	265 1.6×	162 2.2×	155 2.2×	195 2.8×	19	831
Honggang Xiang China	10	47 0.2×	375 2.2×	52 0.7×	61 0.8×	12 0.2×	18	700
Valery Bochkov Austria	12	78 0.4×	274 1.6×	122 1.7×	53 0.7×	21 0.3×	14	541
Shailaja Hegde United States	17	84 0.4×	338 2.0×	122 1.7×	36 0.5×	164 2.4×	33	783
Gabriel L. Navar United States	8	47 0.2×	253 1.5×	58 0.8×	12 0.2×	29 0.4×	9	479
Eunhye Oh South Korea	16	66 0.3×	363 2.2×	54 0.7×	61 0.8×	8 0.1×	31	703
Yuhao Luo China	16	54 0.2×	644 3.9×	67 0.9×	81 1.1×	18 0.3×	40	934

Countries citing papers authored by Jack D. Stopa

Since Specialization

Citations

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

Fields of papers citing papers by Jack D. Stopa

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jack D. Stopa. 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 Jack D. Stopa. The network helps show where Jack D. Stopa may publish in the future.

Co-authorship network of co-authors of Jack D. Stopa

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

All Works

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13 of 13 papers shown

Stopa, Jack D., et al.. (2019). Identification of PDI Substrates by Mechanism-Based Kinetic Trapping. Methods in molecular biology. 1967. 165–182. 6 indexed citations

Zwicker, Jeffrey I., Benjamin L. Schlechter, Jack D. Stopa, et al.. (2019). Targeting protein disulfide isomerase with the flavonoid isoquercetin to improve hypercoagulability in advanced cancer. JCI Insight. 4(4). 128 indexed citations

Iyú, David, Freda Passam, Jack D. Stopa, et al.. (2018). Protein disulfide isomerase regulation by nitric oxide maintains vascular quiescence and controls thrombus formation. Journal of Thrombosis and Haemostasis. 16(11). 2322–2335. 35 indexed citations

Stopa, Jack D. & Jeffrey I. Zwicker. (2018). The intersection of protein disulfide isomerase and cancer associated thrombosis. Thrombosis Research. 164. S130–S135. 26 indexed citations

Zwicker, Jeffrey I., Benjamin L. Schlechter, Jack D. Stopa, et al.. (2018). Targeting Protein Disulfide Isomerase with the Oral Flavonoid Isoquercetin Prevents Venous Thromboembolism in Advanced Cancer: Results of a Multi-Dose, Multi-Center, Phase II Clinical Trial (CATIQ Study). Blood. 132(Supplement 1). 985–985. 1 indexed citations

Stopa, Jack D., et al.. (2017). Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates. Journal of Biological Chemistry. 292(22). 9063–9074. 31 indexed citations

Stopa, Jack D., Donna Neuberg, Mäneka Puligandla, et al.. (2017). Protein disulfide isomerase inhibition blocks thrombin generation in humans by interfering with platelet factor V activation. JCI Insight. 2(1). e89373–e89373. 90 indexed citations

Stopa, Jack D., Donna Neuberg, Mäneka Puligandla, et al.. (2016). PDI Inhibition Blocks Thrombin Generation in Humans By Interfering with Platelet Factor V Activation. Blood. 128(22). 2628–2628. 1 indexed citations

Passam, Freda, Lin Lin, Srila Gopal, et al.. (2015). Both platelet- and endothelial cell–derived ERp5 support thrombus formation in a laser-induced mouse model of thrombosis. Blood. 125(14). 2276–2285. 70 indexed citations

10.

Lin, Lin, Srila Gopal, Anish V. Sharda, et al.. (2015). Quercetin-3-rutinoside Inhibits Protein Disulfide Isomerase by Binding to Its b′x Domain. Journal of Biological Chemistry. 290(39). 23543–23552. 84 indexed citations

11.

Stopa, Jack D., Sushil Chandani, & Dean R. Tolan. (2010). Stabilization of the Predominant Disease-Causing Aldolase Variant (A149P) with Zwitterionic Osmolytes. Biochemistry. 50(5). 663–671. 6 indexed citations

12.

Pezza, John A., et al.. (2007). Thermodynamic Analysis Shows Conformational Coupling and Dynamics Confer Substrate Specificity in Fructose-1,6-bisphosphate Aldolase. Biochemistry. 46(45). 13010–13018. 14 indexed citations

13.

Stopa, Jack D., et al.. (1976). Microgenia as a factor making endotracheal intubation impossible.. PubMed. 3(3). 273–6. 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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