R.B. Credo

1.7k total citations
18 papers, 1.3k citations indexed

About

R.B. Credo is a scholar working on Molecular Biology, Pulmonary and Respiratory Medicine and Oncology. According to data from OpenAlex, R.B. Credo has authored 18 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 6 papers in Pulmonary and Respiratory Medicine and 5 papers in Oncology. Recurrent topics in R.B. Credo's work include Blood properties and coagulation (5 papers), Erythrocyte Function and Pathophysiology (4 papers) and Hemoglobin structure and function (3 papers). R.B. Credo is often cited by papers focused on Blood properties and coagulation (5 papers), Erythrocyte Function and Pathophysiology (4 papers) and Hemoglobin structure and function (3 papers). R.B. Credo collaborates with scholars based in United States and United Kingdom. R.B. Credo's co-authors include L. Lóránd, C G Curtis, Hing L. Sham, P. Stenberg, A. G�ray, Todd J. Janus, Koshonna Brown, Robert B. Warner, János Molnár and Qun Li and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Cell Biology and Biochemistry.

In The Last Decade

R.B. Credo

18 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
R.B. Credo United States 15 497 459 334 304 144 18 1.3k
Robert J. Slack United Kingdom 22 263 0.5× 282 0.6× 601 1.8× 67 0.2× 208 1.4× 80 1.6k
D.J. Tyrrell United States 14 123 0.2× 149 0.3× 662 2.0× 133 0.4× 72 0.5× 15 1.2k
Timothy P. Kogan United States 21 101 0.2× 397 0.9× 543 1.6× 69 0.2× 129 0.9× 38 1.2k
E. Friedrich Germany 19 166 0.3× 71 0.2× 333 1.0× 140 0.5× 73 0.5× 48 1.0k
Maureen H. Beresini United States 22 112 0.2× 109 0.2× 560 1.7× 114 0.4× 29 0.2× 34 1.2k
Rama Kannan United States 15 97 0.2× 85 0.2× 446 1.3× 143 0.5× 264 1.8× 22 1.0k
Hans R. Hendriks Netherlands 21 100 0.2× 186 0.4× 580 1.7× 71 0.2× 49 0.3× 49 1.3k
W. E. Berdel Germany 19 93 0.2× 145 0.3× 546 1.6× 383 1.3× 43 0.3× 49 1.3k
Dario Ballinari Italy 19 129 0.3× 178 0.4× 608 1.8× 53 0.2× 33 0.2× 54 1.1k
Masaki Nogawa Japan 19 182 0.4× 111 0.2× 598 1.8× 70 0.2× 49 0.3× 34 1.2k

Countries citing papers authored by R.B. Credo

Since Specialization
Citations

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

Fields of papers citing papers by R.B. Credo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of R.B. Credo

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

All Works

18 of 18 papers shown
1.
Tong, Yunsong, Akiyo Claiborne, Kent D. Stewart, et al.. (2007). Discovery of 1,4-dihydroindeno[1,2-c]pyrazoles as a novel class of potent and selective checkpoint kinase 1 inhibitors. Bioorganic & Medicinal Chemistry. 15(7). 2759–2767. 33 indexed citations
2.
Li, Gaoquan, Lisa Hasvold, Zhi‐Fu Tao, et al.. (2006). Synthesis and biological evaluation of 1-(2,4,5-trisubstituted phenyl)-3-(5-cyanopyrazin-2-yl)ureas as potent Chk1 kinase inhibitors. Bioorganic & Medicinal Chemistry Letters. 16(8). 2293–2298. 29 indexed citations
3.
Tahir, Stephen K., R.B. Credo, Robert B. Warner, et al.. (2003). Biological activity of A-289099: an orally active tubulin-binding indolyloxazoline derivative.. PubMed. 2(3). 227–33. 36 indexed citations
4.
Wang, Le, Keith W. Woods, Qun Li, et al.. (2002). Potent, Orally Active Heterocycle-Based Combretastatin A-4 Analogues:  Synthesis, Structure−Activity Relationship, Pharmacokinetics, and In Vivo Antitumor Activity Evaluation. Journal of Medicinal Chemistry. 45(8). 1697–1711. 381 indexed citations
5.
Gwaltney, Stephen L., Qun Li, Laura Gehrke, et al.. (2001). Novel sulfonate Derivatives: potent antimitotic agents. Bioorganic & Medicinal Chemistry Letters. 11(13). 1671–1673. 18 indexed citations
6.
Gwaltney, Stephen L., Kenneth J. Barr, Qun Li, et al.. (2001). Novel sulfonate analogues of combretastatin A-4. Bioorganic & Medicinal Chemistry Letters. 11(7). 871–874. 49 indexed citations
7.
Han, Edward K., Laura Gehrke, Sajid Khan Tahir, et al.. (2000). Modulation of drug resistance by α-tubulin in paclitaxel-resistant human lung cancer cell lines. European Journal of Cancer. 36(12). 1565–1571. 43 indexed citations
8.
Credo, R.B. & Sandra E. Burke. (1995). Fibrinolytic Mechanism, Biochemistry, and Preclinical Pharmacology of Recombinant Prourokinase. Journal of Vascular and Interventional Radiology. 6(6). 8S–18S. 6 indexed citations
9.
Marcotte, Patrick A., Jack Henkin, R.B. Credo, & Stephen F. Badylak. (1992). A-chain isozymes of recombinant and natural urokinases: Preparation, characterization, and their biochemical and fibrinolytic properties. Fibrinolysis and Proteolysis. 6(2). 69–78. 5 indexed citations
10.
Curtis, C G, Todd J. Janus, R.B. Credo, & L. Lóránd. (1983). REGULATION OF FACTOR XIIIa GENERATION BY FIBRINOGEN*. Annals of the New York Academy of Sciences. 408(1). 567–576. 5 indexed citations
11.
Lóránd, L., R.B. Credo, & Todd J. Janus. (1981). [27] Factor XIII (fibrin-stabilizing factor). Methods in enzymology on CD-ROM/Methods in enzymology. 80 Pt C. 333–341. 106 indexed citations
12.
Credo, R.B., C G Curtis, & L. Lóránd. (1981). .alpha.-Chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspects. Biochemistry. 20(13). 3770–3778. 67 indexed citations
13.
Gudewicz, Paul W., János Molnár, Ming‐Zong Lai, et al.. (1980). Fibronectin-mediated uptake of gelatin-coated latex particles by peritoneal macrophages.. The Journal of Cell Biology. 87(2). 427–433. 146 indexed citations
14.
Molnár, János, et al.. (1979). Purification of opsonically active human and rat cold-insoluble globulin (plasma fibronectin). Biochemistry. 18(18). 3909–3916. 62 indexed citations
15.
Credo, R.B., C G Curtis, & L. Lóránd. (1978). Ca2+-related regulatory function of fibrinogen.. Proceedings of the National Academy of Sciences. 75(9). 4234–4237. 75 indexed citations
16.
Stenberg, P., C G Curtis, Deborah A. Wing, et al.. (1975). Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines. Biochemical Journal. 147(1). 153–163. 45 indexed citations
17.
Curtis, C G, Koshonna Brown, R.B. Credo, et al.. (1974). Calcium-dependent unmasking of active center cysteine during activation of fibrin stabilizing factor. Biochemistry. 13(18). 3774–3780. 149 indexed citations
18.
Lóránd, L., A. G�ray, Koshonna Brown, et al.. (1974). Dissociation of the subunit structure of fibrin stabilizing factor during activation of the zymogen. Biochemical and Biophysical Research Communications. 56(4). 914–922. 86 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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